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Ligand reduced methyl viologen

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.99.33

urocanate + reduced methyl viologen + H+ = dihydrourocanate + methyl viologen

723218

-

1.7.2.4

nitrous oxide + reduced methyl viologen = nitrogen + H2O + methyl viologen

699384

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.12.1.2

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

0

-

1.12.98.1

H2 + oxidized methyl viologen = reduced methyl viologen

0

-

Substrate in Enzyme-catalyzed Reactions (153 results)

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Show Substrate (153 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.30

(2S,3R,4S)-2-hydroxy-3-halogenbutyrolactones + reduced methyl viologen = ?

655713

-

1.1.99.30

(R,S)-2-oxo-3-methylpentanoate + reduced methyl viologen = 2-hydroxy-3-methylpentanoate + oxidized methyl viologen

644550

-

1.1.99.30

(S)-2-oxo-3-methylpentanoate + reduced methyl viologen = 2-hydroxy-3-methylpentanoate + oxidized methyl viologen

644550

-

1.1.99.30

2-oxo-3,3-dimethyl-4-hydroxybutanoate + reduced methyl viologen = 3,3-dimethyl-2,4-dihydroxybutanoate + oxidized methyl viologen

644550

-

1.1.99.30

2-oxo-4-(hydroxy-methyl-phosphinyl)-butanoate + reduced methyl viologen = 2-hydroxy-4-(hydroxymethylphosphinyl)-butanoate + oxidized methyl viologen

644550

-

1.1.99.30

2-oxo-4-methylpentanoate + reduced methyl viologen = 2-hydroxy-4-methylpentanoate + oxidized methyl viologen

644550

-

1.1.99.30

2-oxo-carboxylate + reduced methyl viologen = (2R)-hydroxy-carboxylate + oxidized methyl viologen

655713

-

1.1.99.30

2-oxoadipate + reduced methyl viologen = 2-hydroxyadipate + oxidized methyl viologen

644550

-

1.1.99.30

2-oxoglutarate + reduced methyl viologen = 2-hydroxyglutarate + oxidized methyl viologen

644550

-

1.1.99.30

2-oxononanoate + reduced methyl viologen = 2-hydroxynonanoate + oxidized methyl viologen

644550

-

1.1.99.30

3-fluoropyruvate + reduced methyl viologen = 3-fluoro-2-hydroxypropionate + oxidized methyl viologen

644550

-

1.1.99.30

5-benzyloxyindolylpyruvate + reduced methyl viologen = 3-(5-benzyloxyindolyl)-2-hydroxypropionate + oxidized methyl viologen

644550

-

1.1.99.30

indolylpyruvate + reduced methyl viologen = 2-hydroxy-3-indolylpropionate + oxidized methyl viologen

644550

-

1.1.99.30

phenylglyoxylate + reduced methyl viologen = (R)-mandelic acid

644550

-

1.1.99.30

phenylpyruvate + reduced methyl viologen = 2-hydroxy-3-phenylpropionate + oxidized methyl viologen

644550

-

1.1.99.30

pyruvate + reduced methyl viologen = lactate + oxidized methyl viologen

644550

-

1.12.1.2

H+ + reduced methyl viologen = H2 + methyl viologen

742858

-

1.12.1.2

H+ + reduced methyl viologen = H2 + oxidized methyl viologen

672279, 704606, 712281

-

1.12.1.4

NADH + 3 H+ + 2 reduced methyl viologen = NAD+ + 2 oxidized methyl viologen + 2 H2

740618

-

1.12.1.4

NADH + H+ + reduced methyl viologen = H2 + NAD+ + oxidized methyl viologen

712281

-

1.12.1.4

sodium dithionite + H+ + reduced methyl viologen = H2 + oxidized methyl viologen + ?

716106

-

1.1.99.30

16 entries

1.12.1.2

2 entries

1.12.1.4

3 entries

1.12.1.5

H+ + reduced methyl viologen = H2 + oxidized methyl viologen

722777

-

1.12.2.1

H+ + reduced methyl viologen = H2 + methyl viologen

395561, 395562, 674919, 395560

-

1.12.2.1

reduced methyl viologen + H+ = oxidized methyl viologen + H2

674919

-

1.12.2.1

2 entries

1.12.7.2

H+ + reduced methyl viologen = H2 + oxidized methyl viologen

439665, 711817, 439641, 659110, 439669, 439682, 764411, 656734, 704088

-

1.17.1.10

formate + reduced methyl viologen = CO2 + oxidized methyl viologen

288217, 288223

-

1.17.1.9

CO2 + reduced methyl viologen = formate + methyl viologen

740320

-

1.17.99.6

epoxyqueuosine34 in tRNA + reduced methyl viologen = queuosine34 in tRNA + methyl viologen + H2O

744338, 745333, 730810

-

1.2.1.46

formate + reduced methyl viologen + 2 H+ = formaldehyde + oxidized methyl viologen + H2O

763521

-

1.2.7.1

acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+ = pyruvate + CoA + 2 oxidized methyl viologen

763018

-

1.2.7.11

acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+ = pyruvate + CoA + 2 oxidized methyl viologen

763018

-

1.2.7.4

H2 + reduced methyl viologen = methyl viologen

655446

-

1.2.7.5

acetate + H+ + reduced methyl viologen = acetaldehyde + H2O + oxidized methyl viologen

11935

-

1.21.99.5

1,2,4,5-tetrachlorobenzene + reduced methyl viologen = 1,2,4-trichlorobenzene + chloride + methyl viologen

744981

-

1.21.99.5

1,2,4-trichlorobenzene + reduced methyl viologen = 1,3-dichlorobenzene + 1,4-dichlorobenzene + chloride + methyl viologen

744981

-

1.21.99.5

tetrachloroethene + reduced methyl viologen = cis-1,2-dichloroethene + 2 chloride + methyl viologen

657689, 657605, 657587

-

1.21.99.5

tetrachloroethene + reduced methyl viologen = trichloroethene + chloride + methyl viologen

728432

-

1.21.99.5

tetrachloroethene + reduced methylviologen = trichloroethene + chloride + methylviologen

674151, 714522

-

1.3.1.31

(E)-2-methyl-3-phenyl-2-propenoate + reduced methyl viologen = (R)-2-methyl-3-phenylpropanoate + methyl viologen

390674

-

1.3.1.31

butenoate + reduced methyl viologen = butanoate + methyl viologen

390673

-

1.3.1.31

(E)-2-methylbutenoate + reduced methylviologen = (R)-2-methylbutanoate + methyl viologen

390673, 390674

-

1.21.99.5

5 entries

1.3.1.31

3 entries

1.3.7.1

6-hydroxynicotinate + reduced methyl viologen = 6-oxo-1,4,5,6-tetrahydronicotinate + oxidized methyl viologen

391150

-

1.3.7.8

2-amino-benzoyl-CoA + reduced methyl viologen + ATP = 2-amino-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

2-aminobenzoyl-CoA + reduced methyl viologen + ATP = ?

12559

-

1.3.7.8

2-chloro-benzoyl-CoA + reduced methyl viologen + ATP = 2-chloro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

2-fluoro-benzoyl-CoA + reduced methyl viologen + ATP = 2-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

2-fluorobenzoyl-CoA + reduced methyl viologen + ATP = ?

12559

-

1.3.7.8

2-hydroxy-benzoyl-CoA + reduced methyl viologen + ATP = 2-hydroxy-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

3-fluoro-benzoyl-CoA + reduced methyl viologen + ATP = 3-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

3-fluorobenzoyl-CoA + reduced methyl viologen + ATP = ?

12559

-

1.3.7.8

3-hydroxybenzoyl-CoA + reduced methyl viologen + ATP = ?

12559

-

1.3.7.8

3-methylbenzoyl-CoA + reduced methyl viologen + ATP = ?

12559

-

1.3.7.8

4-hydroxybenzoyl-CoA + reduced methyl viologen + ATP = 4-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized methyl viologen + ADP + phosphate

12559

-

1.3.7.8

benzoyl-CoA + reduced methyl viologen + ATP = cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

furan-2-carbonyl-CoA + reduced methyl viologen + ATP = ? + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

pyridine-2-carbonyl-CoA + reduced methyl viologen + ATP = ? + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

pyridine-4-carbonyl-CoA + reduced methyl viologen + ATP = ? + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

thiophene-2-carbonyl-CoA + reduced methyl viologen + ATP = ? + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

thiophene-3-carbonyl-CoA + reduced methyl viologen + ATP = ? + methyl viologen + ADP + phosphate

654733

-

1.3.8.1

(E)-2-butenoyl-CoA + reduced methylviologen = ? + oxidized methylviologen

696519

-

1.3.8.1

acrolein + reduced methylviologen = ? + oxidized methylviologen

696519

-

1.3.8.1

acryloyl-CoA + reduced methylviologen = propanoyl-CoA + oxidized methylviologen

696519

-

1.3.8.1

ethyl vinyl ketone + reduced methylviologen = ? + oxidized methylviologen

696519

-

1.3.8.1

N-acetyl-S-acryloyl-cysteamine + reduced methylviologen = ? + oxidized methylviologen

696519

-

1.3.99.33

urocanate + reduced methyl viologen + H+ = dihydrourocanate + methyl viologen

723218

-

1.3.99.33

urocanate + reduced methyl viologen = dihydrourocanate + methyl viologen

763503

-

1.4.7.1

L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen + 2 H+ = 2 L-glutamate + 2 oxidized methyl viologen

763185

-

1.4.7.1

L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen = 2 L-glutamate + 2 oxidized methyl viologen

695534

-

1.4.7.1

L-glutamine + 2-oxoglutarate + reduced methyl viologen + H+ = L-glutamate + oxidized methyl viologen

743811, 743815, 743294, 763549

-

1.4.7.1

L-glutamine + 2-oxoglutarate + reduced methylviologen = L-glutamate + oxidized methylviologen

392022, 392002, 392006, 392020, 392021, 392028, 674324, 392026, 392001, 392004, 392010, 392019, 392017, 392007, 392008, 392014, 392012, 392003, 392005, 392011, 391450, 392018, 392009, 391469, 392013

-

1.3.7.8

17 entries

1.3.8.1

5 entries

1.3.99.33

2 entries

1.4.7.1

4 entries

1.5.1.20

nitrate + reduced methyl viologen = nitrite + methyl viologen

659990, 659882

-

1.5.98.3

oxidized coenzyme F420 + reduced methyl viologen = reduced coenzyme F420 + oxidized methyl viologen

742504

-

1.7.1.1

reduced methyl viologen + nitrate = methyl viologen + nitrite

392842, 392838, 392905, 392859, 392870, 654347, 392913, 392890, 392889, 392877, 392898, 392864, 392919, 765636

-

1.7.1.15

nitrite + reduced methyl viologen = ammonia + oxidized methyl viologen

392925, 765636, 721456, 764856

-

1.7.1.15

nitrite + reduced methyl viologen = NH3 + oxidized methyl viologen

764091

-

1.7.1.15

2 entries

1.7.1.2

reduced methyl viologen + nitrate = oxidized methyl viologen + nitrite + H2O

697599

-

1.7.1.3

nitrate + reduced methyl viologen = nitrite + oxidized methyl viologen

741637

-

1.7.1.3

reduced methyl viologen + nitrate = oxidized methyl viologen + nitrite + H2O

764856

-

1.7.1.3

2 entries

1.7.1.4

nitrite + reduced methyl viologen = NH3 + oxidized methyl viologen + H2O

671935

-

1.7.2.1

nitrite + reduced methyl viologen = NO + oxidized methyl viologen

674572

-

1.7.2.1

nitrite + reduced methyl viologen = NO + oxidized methyl viologen + H2O

660459, 727084

-

1.7.2.1

NO2 + reduced methyl viologen = NO + oxidized methylviologen

394526

-

1.7.2.2

hydroxylamine + reduced methyl viologen = ?

698876

-

1.7.2.2

nitrite + reduced methyl viologen + H+ = NH3 + H2O + oxidized methyl viologen

711343

-

1.7.2.2

nitrite + reduced methyl viologen = NH3 + H2O + oxidized methyl viologen

698876, 700033, 696159, 696256, 699990, 742746, 673685

-

1.7.2.2

nitrite + reduced methyl viologen = NH3 + oxidized methyl viologen + H2O

673685, 723828, 765066

-

1.7.2.2

NO radical + reduced methyl viologen = ?

698876

-

1.7.2.2

sulfite + reduced methyl viologen + H+ = H2S + oxidized methyl viologen + H2O

710714

-

1.7.2.2

sulfite + reduced methyl viologen = H2S + oxidized methyl viologen + H2O

723828

-

1.7.2.4

nitrous oxide + 2 reduced methyl viologen = nitrogen + H2O + 2 methyl viologen

742753

-

1.7.2.4

N2O + reduced methyl viologen = N2 + H2O + methyl viologen

673234, 658979

-

1.7.2.4

N2O + reduced methyl viologen = N2 + H2O + oxidized methyl viologen

726100

-

1.7.2.4

N2O + reduced methyl viologen = N2 + oxidized methyl viologen

726523

-

1.7.2.4

nitrous oxide + reduced methyl viologen + H+ = nitrogen + H2O + oxidized methyl viologen

394546

-

1.7.2.4

nitrous oxide + reduced methyl viologen = nitrogen + H2O + methyl viologen

699384

-

1.7.2.6

hydroxylamine + reduced methyl viologen + H+ = NH4+ + oxidized methyl viologen + H2O

711263

-

1.7.2.6

nitrite + reduced methyl viologen + H+ = NH4+ + oxidized methyl viologen + H2O

711263

-

1.7.2.1

3 entries

1.7.2.2

7 entries

1.7.2.4

6 entries

1.7.2.6

2 entries

1.7.2.9

nitrite + reduced methyl viologen = NO + oxidized methyl viologen

763248

-

1.7.5.1

nitrate + reduced methyl viologen = nitrite + oxidized methyl viologen + H2O

674613, 697691, 700254, 672331, 395191, 395164

-

1.7.7.1

nitrite + reduced methyl viologen = NH3 + H2O + oxidized methyl viologen

394394, 394430, 394423, 394389, 394402, 394388, 660264, 726450, 727542

-

1.7.7.2

nitrate + 2 reduced methyl viologen + 2 H+ = nitrite + H2O + 2 oxidized methyl viologen

764139

-

1.7.7.2

nitrate + reduced methyl viologen = nitrite + H2O + oxidized methyl viologen

676328, 740422

-

1.7.7.2

nitrate + reduced methyl viologen = nitrite + methyl viologen

726801, 658201

-

1.7.7.2

nitrate + reduced methyl viologen = nitrite + oxidized methyl viologen

440455, 440456, 440451, 208103, 440447, 440448, 440454, 440450, 440453, 440443, 440444

-

1.7.7.2

reduced methyl viologen + nitrate = methyl viologen + nitrite

764646

-

1.7.7.2

chlorate + reduced methylviologen = chlorite + H2O + oxidized methylviologen

659366

-

1.7.7.2

nitrate + reduced methylviologen = nitrite + H2O + oxidized methylviologen

658175, 659366

-

1.7.7.2

selenate + reduced methylviologen = selenite + H2O + oxidized methylviologen

659366

-

1.7.99.1

hydroxylamine + reduced methyl viologen = ammonia + oxidized methyl viologen

712507

-

1.7.99.1

hydroxylamine + reduced methyl viologen = NH3 + H2O + oxidized methyl viologen

765075

-

1.7.7.2

8 entries

1.7.99.1

2 entries

1.8.1.2

NADP+ + reduced methyl viologen = NADPH + oxidized methyl viologen

392964, 392984

-

1.8.2.2

tetrathionate + reduced methyl viologen = 2 thiosulfate + methyl viologen

765056

-

1.8.2.2

thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen

740640

-

1.8.2.2

tetrathionate + reduced methylviologen = 2 thiosulfate + methylviologen

742887

-

1.8.2.4

dimethyl sulfoxide + reduced methyl viologen + H2O = dimethyl sulfide + oxidized methyl viologen

714886

-

1.8.2.4

lauryldimethylamine N-oxide + reduced methyl viologen + H2O = ?

714886

-

1.8.2.4

trimethylamine N-oxide + reduced methyl viologen + H2O = ?

714886

-

1.8.2.2

3 entries

1.8.2.4

3 entries

1.8.2.5

thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen

740591, 739959, 740639, 740631

-

1.8.5.3

(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O = ethyl 2-pyridyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O = methoxymethyl phenyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O = methyl p-tolyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O = methylthiomethyl methyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

(S)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O = ethyl 2-pyridyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

(S)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O = methoxymethyl phenyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

(S)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O = methyl p-tolyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

(S)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O = methylthiomethyl methyl sulfide + oxidized methyl viologen

712960

-

1.8.5.3

dimethyl sulfoxide + reduced methyl viologen = dimethyl sulfide + H2O + oxidized methyl viologen

712734

-

1.8.5.3

dimethylsulfoxide + reduced methyl viologen = dimethylsulfide + H2O + oxidized methyl viologen

711190, 712000

-

1.8.5.3

trimethylamine-N-oxide + reduced methyl viologen = trimethylamine + H2O + oxidized methyl viologen

712000

-

1.8.5.6

sulfur + reduced methyl viologen + H2O = H2S + oxidized methyl viologen

764198

-

1.8.5.6

tetrathionate + reduced methyl viologen + H2O = ? + oxidized methyl viologen

764198

-

1.8.5.3

11 entries

1.8.5.6

2 entries

1.8.7.1

sulfite + reduced methyl viologen + H+ = hydrogen sulfide + oxidized methyl viologen + H2O

437693, 726144

-

1.8.98.1

coenzyme B-coenzyme M disulfide + reduced methyl viologen = coenzyme B + coenzyme M + methyl viologen

742500

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methyl viologen = coenzyme B + coenzyme M + methyl viologen

639394

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen = coenzyme B + coenzyme M + methyl viologen

655400, 440299

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen = coenzyme B + coenzyme M + methylviologen

639393, 654386

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen = coenzyme B + coenzyme M + oxidized methylviologen

655823

-

1.8.98.1

5 entries

1.8.98.3

sulfite + reduced methyl viologen = hydrogen sulfide + oxidized methyl viologen

674504

-

1.8.99.2

adenylyl sulfate + reduced methyl viologen = AMP + sulfite + methyl viologen

287801, 393952, 393940, 393943, 393928

-

1.8.99.2

guanylyl sulfate + reduced methyl viologen = GMP + methyl viologen + sulfite

393940

-

1.8.99.5

SeO32- + a [DsrC protein]-dithiol + 2 reduced methyl viologen + 2 H+ = HSe- + a [DsrC protein]-disulfide + 2 oxidized methyl viologen + 3 H2O

394898

-

1.8.99.5

sulfite + a [DsrC protein]-dithiol + reduced methyl viologen = trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen

394043, 394040

-

1.8.99.2

2 entries

1.8.99.5

2 entries

1.8.99.B2

tetrathionate + reduced methyl viologen = 2 thiosulfate + oxidized methyl viologen

763962, 764683

-

1.9.6.1

2 reduced methyl viologen + 2 H+ + nitrate = 2 oxidized methyl viologen + nitrite

741478

-

1.9.6.1

nitrate + reduced methyl viologen = nitrite + oxidized methyl viologen

698636

-

1.9.6.1

nitrate + reduced methyl viologen = nitrite + oxidized methyl viologen + H2O

697965, 395185, 696082, 684990, 764685, 697696

-

1.97.1.1

bromate + reduced methyl viologen = bromite + H2O + methyl viologen

659023

-

1.97.1.1

chlorate + reduced methyl viologen = chlorite + H2O + methyl viologen

658779, 659023, 729317

-

1.97.1.1

perchlorate + reduced methyl viologen = chlorate + H2O + methyl viologen

658779

-

1.9.6.1

3 entries

1.97.1.1

3 entries

1.97.1.4

S-adenosyl-L-methionine + reduced methyl viologen + formate acetyltransferase-glycine = 5'-deoxyadenosine + methionine + methyl viologen + formate acetyltransferase-glycine-2-yl-radical

663000

-

1.97.1.9

selenate + reduced methyl viologen = selenite + H2O + methyl viologen

644816

-

1.97.1.9

selenate + reduced methyl viologen = selenite + H2O + oxidized methyl viologen

644812, 714365, 644816, 644811

-

1.97.1.9

2 entries

1.97.1.B1

iodate + reduced methyl viologen = iodite + H2O + methyl viologen

764582

-

Product in Enzyme-catalyzed Reactions (96 results)

top print hide

Show Product (96 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.4

oxidized methyl viologen + reduced coenzyme F420 = reduced methyl viologen + oxidized coenzyme F420

0

-

1.12.1.2

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

439711, 439699, 0

-

1.12.1.2

H2 + oxidized methyl viologen = reduced methyl viologen + H+

0

-

1.12.1.2

2 entries

1.12.1.3

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

0, 439687

-

1.12.1.4

NAD+ + 2 oxidized methyl viologen + 2 H2 = NADH + 3 H+ + 2 reduced methyl viologen

0

-

1.12.2.1

H2 + methyl viologen = H+ + reduced methyl viologen

0

-

1.12.2.1

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

0

-

1.12.7.2

H2 + methyl viologen = reduced methyl viologen + H+

0

-

1.12.7.2

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

0

-

1.12.98.1

H2 + oxidized methyl viologen = reduced methyl viologen

0

-

1.12.98.1

oxidized methyl viologen + H2 = reduced methyl viologen + H+

0

-

1.12.2.1

2 entries

1.12.7.2

2 entries

1.12.98.1

2 entries

1.12.98.3

H2 + oxidized methyl viologen = reduced methyl viologen

440297

-

1.12.98.4

H2 + methyl viologen = H2S + reduced methyl viologen

0

-

1.12.99.6

H2 + methyl viologen = H+ + reduced methyl viologen

0

-

1.12.99.6

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

0

-

1.12.99.6

H2 + oxidized methyl viologen = reduced methyl viologen

0

-

1.12.99.6

H2 + oxidized methyl viologen = reduced methyl viologen + H+

0

-

1.17.1.4

4-hydroxypyrazolo(3,4-d)pyrimidine + methyl viologen + H2O = 4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced methyl viologen

644592

-

1.17.1.4

5-aminoimidazol-4-carboxamide + methyl viologen + H2O = ? + reduced methyl viologen

644592

-

1.17.1.4

6-mercaptopurine + methyl viologen + H2O = ? + reduced methyl viologen

644592

-

1.17.1.4

hypoxanthine + methyl viologen + H2O = xanthine + reduced methyl viologen

644614, 644592

-

1.17.1.4

purine + methyl viologen + H2O = ? + reduced methyl viologen

644592

-

1.17.1.4

xanthine + methyl viologen + H2O = urate + reduced methyl viologen

644568, 644614, 644570, 644592

-

1.12.99.6

4 entries

1.17.1.4

6 entries

1.17.1.9

formate + methyl viologen = CO2 + reduced methyl viologen

0

-

1.17.5.3

formate + methyl viologen = CO2 + reduced methyl viologen

0

-

1.17.98.3

formate + oxidized methyl viologen = CO2 + reduced methyl viologen

0

-

1.17.98.4

formate + methyl viologen = CO2 + reduced methyl viologen

0

-

1.18.1.2

methyl viologen + NADPH = reduced methyl viologen + NADP+

0

-

1.18.1.4

methyl viologen + NADH = reduced methyl viologen + NAD+ + H+

0

-

1.2.1.51

pyruvate + CoA + methyl viologen = acetyl-CoA + CO2 + reduced methyl viologen

0

-

1.2.1.58

phenylglyoxylate + methyl viologen + CoA-SH = benzoyl-S-CoA + CO2 + reduced methyl viologen

0

-

1.2.1.B29

H2 + NADP+ + 2 oxidized methyl viologen = ? + NADPH + H+ + 2 reduced methyl viologen

0

-

1.2.5.3

CO + NADPH + H+ + H2O = CO2 + reduced methyl viologen

0

-

1.2.7.1

2-oxobutyrate + CoA + 2 oxidized methyl viologen = propanoyl-CoA + CO2 + 2 reduced methyl viologen

0

-

1.2.7.1

pyruvate + CoA + 2 oxidized methyl viologen = acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.1

2-oxobutyrate + CoA + oxidized methyl viologen = propanoyl-CoA + CO2 + reduced methyl viologen

0

-

1.2.7.1

oxaloacetate + CoA + oxidized methyl viologen = ? + reduced methyl viologen + H+

0

-

1.2.7.1

pyruvate + CoA + oxidized methyl viologen = acetyl-CoA + CO2 + reduced methyl viologen

0

-

1.2.7.1

pyruvate + CoA + oxidized methyl viologen = acetyl-CoA + CO2 + reduced methyl viologen + H+

0

-

1.2.7.1

pyruvate + H2O + oxidized methyl viologen = acetyl-CoA + reduced methyl viologen + H+

0

-

1.2.7.10

oxalate + methyl viologen = 2 CO2 + reduced methyl viologen

0

-

1.2.7.10

oxalate + methyl viologen = CO2 + reduced methyl viologen

0

-

1.2.7.11

2-oxo-4-methylthiobutyrate + CoA + 2 methyl viologen = 3-methylthiopropanoyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.11

2-oxoadipate + CoA + 2 methyl viologen = glutaryl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.11

2-oxobutyrate + CoA + 2 oxidized methyl viologen = propanoyl-CoA + CO2 + 2 reduced methyl viologen

0

-

1.2.7.11

2-oxoglutarate + CoA + 2 oxidized methyl viologen = succinyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.11

4-hydroxyphenylpyruvate + CoA + 2 methyl viologen = (4-hydroxyphenyl)acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.11

glyoxylate + CoA + 2 oxidized methyl viologen = formyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.11

phenylpyruvate + CoA + 2 methyl viologen = phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.11

pyruvate + CoA + 2 oxidized methyl viologen = acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.11

2-oxoglutarate + CoA + oxidized methyl viologen = succinoyl-CoA + CO2 + reduced methyl viologen

0

-

1.2.7.11

2-oxoglutarate + CoA + oxidized methyl viologen = succinyl-CoA + CO2 + reduced methyl viologen + H+

0

-

1.2.7.12

formylmethanofuran + H2O + oxidized methyl viologen = CO2 + methanofuran + reduced methyl viologen + H+

0

-

1.2.7.12

formylmethanofuran + oxidized methylviologen + H2O = methanofuran + reduced methylviologen + CO2

0, 11920

-

1.2.7.1

7 entries

1.2.7.10

2 entries

1.2.7.11

10 entries

1.2.7.12

2 entries

1.2.7.3

2-oxoglutarate + CoA + oxidized methyl viologen = succinyl-CoA + CO2 + reduced methyl viologen

0

-

1.2.7.4

CO + H2O + methyl viologen = CO2 + reduced methyl viologen

390458, 0, 390473, 390456, 390452, 390451, 390448, 390466, 390463, 390469, 390475, 390459, 390454, 390449, 390468, 390450, 390460, 390471

-

1.2.7.4

CO + H2O + methyl viologen = CO2 + reduced methyl viologen + H+

0

-

1.2.7.4

CO + H2O + oxidized methyl viologen = CO2 + reduced methyl viologen

0

-

1.2.7.4

CO + H2O + oxidized methyl viologen = CO2 + reduced methyl viologen + H+

0

-

1.2.7.5

crotonaldehyde + H2O + oxidized methyl viologen = crotonate + H+ + reduced methyl viologen

0

-

1.2.7.5

crotonaldehyde + H2O + oxidized methyl viologen = crotonate + reduced methyl viologen + H+

0

-

1.2.7.5

formaldehyde + H2O + oxidized methyl viologen = formate + H+ + reduced methyl viologen

0

-

1.2.7.5

glutaraldehyde + H2O + oxidized methyl viologen = glutarate + H+ + reduced methyl viologen

0

-

1.2.7.5

glyceraldehyde + H2O + oxidized methyl viologen = glycerate + H+ + reduced methyl viologen

11938, 0

-

1.2.7.5

hexanal + H2O + oxidized methyl viologen = hexanoate + H+ + reduced methyl viologen

0

-

1.2.7.4

4 entries

1.2.7.5

6 entries

1.2.7.6

D-glyceraldehyde-3-phosphate + H2O + oxidized methyl viologen = 3-phospho-D-glycerate + reduced methyl viologen + H+

0

-

1.2.7.8

3-methyl-2-oxobutanoate + H2O + oxidized methyl viologen = S-(2-methylpropanoyl)-CoA + reduced methyl viologen + H+

0

-

1.2.7.8

phenylpyruvate + CoA + oxidized methyl viologen = phenylacetyl-CoA + CO2 + reduced methyl viologen + H+

0

-

1.2.7.8

indolepyruvate + CoA + oxidized methylviologen = indoleacetyl-CoA + CO2 + reduced methylviologen

0

-

1.2.7.B2

formaldehyde + H2O + 2 oxidized methyl viologen = formate + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.B2

acetaldehyde + H2O + oxidized methyl viologen = acetate + H+ + reduced methyl viologen

0

-

1.2.7.B2

butyraldehyde + H2O + oxidized methyl viologen = butyrate + H+ + reduced methyl viologen

0

-

1.2.7.B2

crotonaldehyde + H2O + oxidized methyl viologen = crotonate + reduced methyl viologen + H+

0

-

1.2.7.B2

formaldehyde + H2O + oxidized methyl viologen = formate + H+ + reduced methyl viologen

0

-

1.2.7.B2

formaldehyde + H2O + oxidized methyl viologen = formate + reduced methyl viologen + H+

0

-

1.2.7.B2

hexanal + H2O + oxidized methyl viologen = hexanoate + reduced methyl viologen + H+

0

-

1.2.7.B2

propionaldehyde + H2O + oxidized methyl viologen = propionate + H+ + reduced methyl viologen

0

-

1.2.7.8

3 entries

1.2.7.B2

8 entries

1.2.7.B3

hexanal + H2O + oxidized methyl viologen = hexanoate + reduced methyl viologen + H+

0

-

1.2.99.6

acetaldehyde + methyl viologen + H2O = acetate + reduced methyl viologen

0

-

1.2.99.6

Acetaldehyde + methyl viologen = acetate + reduced methyl viologen

0

-

1.2.99.6

Butanal + methyl viologen = Butanoate + reduced methyl viologen

0

-

1.2.99.6

Crotonaldehyde + methyl viologen = Crotonate + reduced methyl viologen

0

-

1.2.99.6

Glyceraldehyde + methyl viologen = Glycerate + reduced methyl viologen

0

-

1.2.99.6

Methanal + carbamoyl methyl viologen = Formate + reduced methyl viologen

0

-

1.2.99.6

Propanal + methyl viologen = Propanoate + reduced methyl viologen

0, 11943

-

1.2.99.8

D-glyceraldehyde + H2O + methyl viologen = D-glycerate + reduced methyl viologen

0

-

1.2.99.8

D-glyceraldehyde-3-phosphate + H2O + methyl viologen = 3-phospho-D-glycerate + reduced methyl viologen

0

-

1.2.99.6

7 entries

1.2.99.8

2 entries

1.21.99.5

trichloroethene + chloride + methyl viologen = tetrachloroethene + reduced methyl viologen

0

-

1.5.1.54

NADH + H+ + methylviologen = NAD+ + reduced methylviologen

0

-

1.7.2.3

trimethylamine N-oxide + oxidized methyl viologen + H+ = trimethylamine + reduced methyl viologen + H2O

0

-

1.7.2.6

nitrite + reduced benzyl viologen + H+ = NH4+ + reduced methyl viologen + H2O

0

-

1.7.2.6

hydroxylamine + H2O + methylviologen = NO + reduced methylviologen + 2 H+

0

-

1.7.2.6

2 entries

1.8.5.3

dimethylsulfide + H2O + oxidized methyl viologen = dimethylsulfoxide + reduced methyl viologen

0

-

1.8.7.1

hydrogen sulfide + oxidized methyl viologen + H2O = sulfite + reduced methyl viologen + H+

0

-

1.8.7.3

oxidized methyl viologen + CoB + CoM = reduced methyl viologen + CoM-S-S-CoB + H+

0

-

1.8.98.5

H2 + oxidized methyl viologen + CoM-S-S-CoB = reduced methyl viologen + CoB + CoM + H+

0

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

top print hide

Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.31

-

390673, 390674

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (4 results)

top print hide

Show Turnover Number (4 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.17.1.9

0.032

-

at pH 7.4, temperature not specified in the publication

740320

1.7.2.2

738

-

apparent value, in 0.2 M phosphate buffer pH 7.6, at 37°C

711343

1.8.1.2

605

-

-

392964

1.8.5.3

27

-

pH 8.0, 25°C

711190

K_M Value (21 results)

top print hide

Show KM Value (21 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.12.1.2

0.0306

-

30°C, pH 7.0

672282

1.12.1.2

0.089

-

pH 6.3, 60°C

654821

1.12.1.2

2 entries

1.12.2.1

0.003

-

H2-evolution assay

395560

1.12.7.2

0.57

-

-

704088

1.12.7.2

1.25

-

-

439641

1.12.7.2

6.25

-

hydrogen evolution

439682

1.12.7.2

3 entries

1.17.1.10

2.35

-

-

288217, 288223

1.17.1.9

0.212

-

at pH 7.4, temperature not specified in the publication

740320

1.21.99.5

0.024

-

30°C

657587

1.3.1.31

0.4

-

-

390673, 390674

1.3.7.1

0.3

-

-

391150

1.7.1.1

0.87

-

-

392913

1.7.2.1

0.41

-

pH and temperature not specified in the publication

727084

1.7.2.2

0.015

-

apparent value, in 0.2 M phosphate buffer pH 7.6, at 37°C

711343

1.7.2.4

0.00095

-

-

394546

1.7.7.1

1.9

-

pH 7.0, 60°C

727542

1.7.7.2

0.0028

-

37°C, pH 7.2

726801

1.7.7.2

0.0646

-

120 mM Na2CO3 pH 9, 1 M NaCl, 4 mM methyl viologen, 35 mM KNO3, 17 mM Na2S2O4 (freshly prepared in 0.1 M NaHCO3) and 0.7 mU of enzyme preparations. The samples are incubated for 20 min at 60°C

740422

1.7.7.2

0.066

-

-

440453

1.7.7.2

2.5

-

-

440444

1.7.7.2

4 entries

1.8.7.1

0.006

-

-

437693

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.31

10

-

-

390673, 390674

References & Links

Literature References (244)

top print hide

Show Reference (244 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

11920

7813470

Thermodynamics of the formylmethanofuran dehydrogenase reaction in Methanobacterium thermoautotrophicum

1994

Bertram, P.A.; Thauer, R.K.

Eur. J. Biochem.

226

811-818

11935

7642503

Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1

1995

Heider, J.; Ma, K.; Adams, M.W.W.

J. Bacteriol.

177

4757-4764

11938

1907273

The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway

1991

Mukund, S.; Adams, M.W.W.

J. Biol. Chem.

266

14208-14216

11943

1793519

Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum

1991

White, H.; Feicht, R.; Huber, C.; Lottspeich, F.; Simon, H.

Biol. Chem. Hoppe-Seyler

372

999-1005

12559

8575453

Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thaurea aromatica strain K172

1995

Boll, M.; Fuchs, G.

Eur. J. Biochem.

234

921-933

208103

-

The assimilatory nitrate-reducing system and its regulation

1981

Guerrero, M.G.; Vega, J.M.; Losada, M.

Annu. Rev. Plant Physiol.

32

169-204

287801

-

Metal-containing flavoprotein dehydrogenases

1976

Hatefi, Y.; Stiggall, D.L.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

13

175-297

288217

713844

Formate dehydrogenase, a selenium-tungsten enzyme from Clostridium thermoaceticum

1970

Ljungdahl, L.G.; Andreesen, J.R.

Methods Enzymol.

53

360-372

288223

4154039

Nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum: purification and properties

1974

Andreesen, J.R.; Ljungdahl, L.G.

J. Bacteriol.

120

6-14

390448

3029096

Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum

1987

Bonam, D.; Ludden, P.W.

J. Biol. Chem.

262

2980-2987

390449

3818661

Carbon monoxide dehydrogenase from Methanosarcina barkeri. Disaggregation, purification, and physicochemical properties of the enzyme

1987

Grahame, D.A.; Stadtman, T.C.

J. Biol. Chem.

262

3706-3712

390450

3624199

Purification and properties of carbon monoxide dehydrogenase from Methanococcus vannielii

1987

DeMoll, E.; Grahame, D.A.; Harnly, J.M.; Tsai, L.; Stadtman, T.C.

J. Bacteriol.

169

3916-3920

390451

-

CO2 fixation in acetogenic bacteria: variations on a theme

1986

Fuchs, G.

FEMS Microbiol. Rev.

39

181-213

390452

6687389

Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein

1983

Ragsdale, S.W.; Clark, J.E.; Ljungdahl, L.G.; Lundie, L.L.; Drake, H.L.

J. Biol. Chem.

258

2364-2369

390454

6893049

Purification of carbon monoxide dehydrogenase, a nickel enzyme from Clostridium thermoaceticum

1980

Drake, H.L.; Hu, S.I.; Wood, H.G.

J. Biol. Chem.

255

7174-7180

390456

21159

Carbon monoxide oxidation by methanogenic bacteria

1977

Daniels, L.; Fuchs, G.; Thauer, R.K.; Zeikus, J.G.

J. Bacteriol.

132

118-126

390458

-

The acetyl-CoA pathway of autotrophic growth

1986

Wood, H.G.; Ragsdale, S.W.; Pezacka, E.

FEMS Microbiol. Rev.

39

345-362

390459

2984190

Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis

1985

Ragsdale, S.W.; Wood, H.G.

J. Biol. Chem.

260

3970-3977

390460

-

Nickel-containing CO dehydrogenase catalyzes reversible decarbonylation of acetyl-CoA with retention of stereochemistry at the methyl group

1987

Raybuck, S.A.; Bastian, N.R.; Zydowsky, L.D.; Kobayashi, K.; Floss, H.G.; Orme-Johnson, W.H.; Walsh, C.T.

J. Am. Chem. Soc.

109

3171-3173

390463

8662887

Carbon monoxide dehydrogenase from Methanosarcina frisia Gö1

1996

Eggen, R.I.L.; van Kranenburg, R.; Vriesema, A.J.M.; Geerling, A.C.M.; Verhagen, M.F.J.M.; Hagen, W.R.; de Vos, W.M.

J. Biol. Chem.

271

14256-14263

390466

2510818

Carbonyl sulfide inhibition of CO dehydrogenase from Rhodospirillum rubrum

1989

Hyman, M.R.; Ensign, S.A.; Arp, D.J.; Ludden, P.W.

Biochemistry

28

6821-6826

390468

2905170

Kinetic characterization of the carbon monoxide-acetyl-CoA (carbonyl group) exchange activity of the acetyl-CoA synthesizing CO dehydrogenase from Clostridium thermoaceticum

1988

Raybuck, S.A.; Bastian, N.R.; Orme-Johnson, W.H.; Walsh, C.T.

Biochemistry

27

7698-7702

390469

2569891

Kinetic characterization of the [3'-32P]coenzyme A/acetyl coenzyme A exchange catalyzed ba a three-subunit form of the carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum

1989

Ramer, S.E.; Raybuck, S.A.; Orme-Johnson, W.H.; Walsh, C.T.

Biochemistry

28

4675-4680

390471

-

Anaerobic lactate oxidation to 3 CO2 by Archaeoglobus fulgidus via the carbon monoxide dehydrogenase pathway: demonstration of the acetyl-CoA carbon-carbon cleavage reaction in cell extract

1990

Möller-Zinkhan, D.; Thauer, R.K.

Arch. Microbiol.

153

215-218

390473

2714294

Purification and characterization of an oxygen-stable carbon monoxide dehydrogenase of Methanothrix soehngenii

1989

Jetten, M.S.M.; Stams, A.J.M.; Zehnder, A.J.B.

Eur. J. Biochem.

181

437-441

390475

1995618

Reductive activation of the coenzyme A/acetyl-CoA isotopic exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by nitrous oxide and carbon monoxide

1991

Lu, W.P.; Ragsdale, S.W.

J. Biol. Chem.

266

3554-3564

390673

-

Electroenzymatic and electromicrobial reduction: preparation of chiral compounds

1987

Thanos, I.; Bader, J.; Guenther, H.; Neumann, S.; Krauss, F.; Simon, H.

Methods Enzymol.

136

302-317

390674

-

Electro-enzymic viologen-mediated stereospecific reduction of 2-enoates with free and immobilized enoate reductase on cellulose filters or modified carbon electrodes

1987

Thanos, I.C.G.; Simon, H.

J. Biotechnol.

6

13-29

391150

5767303

Nicotinic acid metabolism. IV. Ferredoxin-dependent reduction of 6-hydroxynicotinic acid to 6-oxo-1,4,5,6-tetrahydronicotinic acid

1969

Holcenberg, J.S.; Tsai, L.

J. Biol. Chem.

244

1204-1211

391450

-

Glutamate synthase in rice roots. Studies on the electron donor specificity

1983

Suzuki, A.; Jacquot, J.P.; Gadal, P.

Phytochemistry

22

1543-1546

391469

12069605

Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit

2002

Ravasio, S.; Dossena, L.; Martin-Figueroa, E.; Florencio, F.J.; Mattevi, A.; Morandi, P.; Curti, B.; Vanoni, M.A.

Biochemistry

41

8120-8133

392001

-

Functional properties of purified ferredoxin-glutamate synthase from Chlamydomonas reinhardtii

1990

Gotor, C.; Martinez-Rivas, J.M.; Marquez, A.J.; Vega, J.M.

Phytochemistry

29

711-717

392002

-

Circular dichroism, binding and immunological studies on the interaction between spinach ferredoxin and glutamate synthase

1989

Hirasawa, M.; Chang, K.T.; Morrow jr., K.J.; Knaff, D.B.

Biochim. Biophys. Acta

977

150-156

392003

3190691

Glutamate synthase in Medicago sativa L. Occurrence and properties of FD-dependent enzyme in plant cell fraction during root nodule development

1988

Suzuki, A.; Carrayol, E.; Zehnacker, C.; Deroche, M.E.

Biochem. Biophys. Res. Commun.

156

1130-1138

392004

16666409

Localization of nitrogen-assimilation enzymes in the chloroplast of Chlamydomonas reinhardtii

1988

Fischer, P.; Klein, U.

Plant Physiol.

88

947-952

392005

16665799

Different characteristics of the two glutamate synthases in the green leaves of Lycopersicon esculentum

1987

Avila, C.; Botella, J.R.; Canovas, F.M.; Nunez de Castro, I.; Valpuesta, V.

Plant Physiol.

85

1036-1039

392006

-

The interaction of ferredoxin with chloroplast ferredoxin-linked enzymes

1986

Hirasawa, M.; Boyer, J.M.; Gray, K.A.; Davis, D.J.; Knaff, D.B.

Biochim. Biophys. Acta

851

23-28

392007

16664732

Detection of the messenger RNA encoding for the ferredoxin-dependent glutamate synthase in maize leaf

1986

Commere, B.; Vidal, J.; Suzuki, A.; Gadal, P.; Caboche, M.

Plant Physiol.

80

859-862

392008

-

Ferredoxin and pyridine nucleotide-dependent glutamate synthase activities in maize endosperm tissue

1985

Misra, S.; Oaks, A.

Plant Sci.

39

1-5

392009

24249443

Glutamate synthase in greening callus of Bouvardia ternifolia Schlecht

1985

Murillo, E.; S¯nchez de Jimenez, E.

Planta

163

448-452

392010

24254054

Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardtii

1984

Galvan, F.; Marquez, A.J.; Vega, J.M.

Planta

162

180-187

392011

6477553

Separation of two forms of glutamate synthase in leaves of tomato (Lycopersicon esculentum)

1984

Avila, C.; Canovas, F.; Nunez de Castro, I.; Valpuesta, V.

Biochem. Biophys. Res. Commun.

122

1125-1130

392012

-

Occurence of ferredoxin-dependent glutamate synthase in plant cell fraction of soybean root nodules (Glycine max)

1984

Suzuki, A.; Vidal, J.; Nguyen, J.; Gadal, P.

FEBS Lett.

173

204-208

392013

6746604

Flavin and iron-sulfur containing ferredoxin-linked glutamate synthase from spinach leaves

1984

Hirasawa, M.; Tamura, G.

J. Biochem.

95

983-994

392014

-

Glutamate synthase isoforms in Tobacco cultured cells

1984

Suzuki, A.; Nato, A.; Gadal, P.

Plant Sci. Lett.

33

93-101

392017

24276154

Changes in the activities of ferredoxin- and NADH-glutamate synthase during seedling development of peas

1982

Matoh, T.; Takahashi, E.

Planta

154

289-294

392018

16662307

Glutamate synthase from rice leaves

1982

Suzuki, A.; Gadal, P.

Plant Physiol.

69

848-852

392019

-

Occurrence of two forms of glutamate synthase in Chlamydomonas reinhardii

1981

Cullimore, J.V.; Sims, A.P.

Phytochemistry

20

597-600

392020

-

Isolation and partial characterization of homogeneous glutamate synthase from Spinacia oleracea

1980

Tamura, G.; Oto, M.; Hirasawa, M.; Aketagawa, J.

Plant Sci. Lett.

19

209-215

392021

-

The purification and properties of glutamate synthase from spinach leaves, and its dependence on ferredoxin

1980

Tamura, G.; Kanki, M.; Hirasawa, M.; Oto, M.

Agric. Biol. Chem.

44

925-927

392022

892179

Ferredoxin-Sepharose as an affinity absorbent for the purification of glutamate synthase and other ferredoxin-dependent enzymes

1977

Wallsgrove, R.M.; Miflin, B.J.

Biochem. Soc. Trans.

5

269-271

392026

9421934

Regulation of the expression of ferredoxin-glutamate synthase in barley

1997

Pajuelo, P.; Pajuelo, E.; Forde, B.G.; Marquez, A.J.

Planta

203

517-525

392028

10898944

Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the Cyanobacterium synechocystis sp. PCC 6803: expression and assembly in Escherichia coli

2000

Navarro, F.; Martin-Figueroa, E.; Candau, P.; Florencio, F.J.

Arch. Biochem. Biophys.

379

267-276

392838

-

Purification and partial characterization of nitrate reductase from barley leaves

1980

Kuo, T.; Kleinhofs, A.; Warner, R.L.

Plant Sci. Lett.

17

371-381

392842

16660726

In vitro stability of nitrate reductase from wheat leaves

1979

Sherrard, J.H.; Dalling, M.J.

Plant Physiol.

63

346-353

392859

16666771

Chloride inhibition of spinach nitrate reductase

1989

Barber, M.J.; Notton, B.A.; Kay, C.J.; Solomonson, L.P.

Plant Physiol.

90

70-94

392864

-

Activation of Thalassiosira pseudonana NADH: nitrate reductase

1980

Smarrelli, J.; Campbell, W.H.

Phytochemistry

19

1601-1605

392870

16667499

Spinach nitrate reductase

1990

Barber, M.J.; Notton, B.A.

Plant Physiol.

93

537-540

392877

3597400

Radiation inactivation analysis of assimilatory NADH:nitrate reductase. Apparent functional sizes of partial activities associated with intact and proteolytically modified enzyme

1987

Solomonson, L.P.; Mc Creery, M.J.; Kay, C.J.; Barber, M.J.

J. Biol. Chem.

262

8934-8939

392889

-

Action kinetics of the inhibition of nitrate reductase of rice plants

1982

Leong, C.C.; Shen, T.C.

Biochim. Biophys. Acta

703

129-133

392890

16658375

Partial purification of the NADH-nitrate reductase complex from Chlorella pyrenoidosa

1973

Schloemer, R.H.; Garrett, R.H.

Plant Physiol.

51

591-593

392898

3015963

Functional domains of assimilatory NADH:nitrate reductase from Chlorella

1986

Solomonson, L.P.; Barber, M.J.; Robbins, A.P.; Oaks, A.

J. Biol. Chem.

261

11290-11294

392905

-

Purification and characterization of NADH-nitrate reductase from leaves of 2-row barley, and its activity as affected by some metabolites

1985

Oji, Y.; Mamano, T.; Ryoma, Y.; Miki, Y.; Okamoto, S.

J. Plant Physiol.

119

247-256

392913

9305729

The assimilatory nitrate reductase from the phototrophic bacterium, Rhodobacter capsulatus E1F1, is a flavoprotein

1997

Blasco, R.; Castillo, F.; Martinez-Luque, M.

FEBS Lett.

414

45-49

392919

-

Purification and properties of NADH: nitrate reductase from the red alga Porphyra yezoensis

1993

Nakamura, Y.; Ikawa, T.

Plant Cell Physiol.

34

1239-1249

392925

6297458

Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12

1982

Cammack, R.; Jackson, R.H.; Cornish-Bowden, A.; Cole, J.A.

Biochem. J.

207

333-339

392964

4150390

Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow

1974

Siegel, L.M.; Davis, P.S.; Kamin, H.

J. Biol. Chem.

249

1572-1586

392984

8001563

The NADPH:sulfite reductase of Escherichia coli is a paraquat reductase

1994

Gaudu, P.; Fontecave, M.

Eur. J. Biochem.

226

459-463

393928

2158885

The active centers of adenylylsulfate reductase from Desulfovibrio gigas. Characterization and spectroscopic studies

1990

Lampreia, J.; Moura, I.; Teixeira, M.; Peck, H.D.; LeGall, J.; Huynh, B.H.; Moura, J.J.G.

Eur. J. Biochem.

188

653-664

393940

235533

Some physical and kinetic properties of adenylyl sulfate reductase from Desulfovibrio vulgaris

1975

Bramlett, R.N.; Peck, H.D.

J. Biol. Chem.

250

2979-2986

393943

4405088

On the mechanism of adenylyl sulfate reductase for the sulfate-reducing bacterium , Desulfovibrio vulgaris

1972

Peck, H.D.; Bramlett, R.; DerVartanian, D.V.

Z. Naturforsch. B

27

1084-1086

393952

12006599

The function of the [4Fe-4S] clusters and FAD in bacterial and archaeal adenylylsulfate reductases: evidence for flavin-catalyzed reduction of adenosine 5'-phosphosulfate

2002

Fritz, G.; Buchert, T.; Kroneck, P.M.H.

J. Biol. Chem.

277

26066-26073

394040

4093441

Characterization of a dissimilatory-type sulfite reductase, desulfoviridin, from Desulfovibrio africanus Benghazi

1985

Seki, Y.; Nagai, Y.; Ishimoto, M.

J. Biochem.

98

1535-1543

394043

6826522

Characterization of a new type of dissimilatory sulfite reductase present in Thermodesulfobacterium commune

1983

Hatchikian, E.C.; Zeikus, J.G.

J. Bacteriol.

153

1211-1220

394388

2119228

Purification and some properties of the nitrite reductase from the cyanobacterium Phormidium laminosum

1990

Arizmendi, J.M.; Serra, J.L.

Biochim. Biophys. Acta

1040

237-244

394389

-

Purification and characterization of molecular and immunological properties of rice ferredoxin-nitrite reductase

1989

Ida, S.; Iwagami, K.; Minobe, S.

Agric. Biol. Chem.

53

2777-2784

394394

-

Purification and properties of the siroheme-containing ferredoxin-nitrite reductase from Chlamydomonas reinhardtii

1987

Romero, L.C.; Galvan, F.; Vega, J.M.

Biochim. Biophys. Acta

914

55-63

394402

-

Nitrite reductase in the cyanobacterium Spirulina plantensis

1985

Yabuki, Y.; Mori, E.; Tamura, G.

Agric. Biol. Chem.

49

3061-3062

394423

-

The effect of lysine- and arginine-modifying reagents on spinach ferredoxin:nitrite oxidoreductase

1993

Hirasawa, M.; de Best, J.H.; Knaff, D.B.

Biochim. Biophys. Acta

1140

304-312

394430

8694757

Purification and characterization of assimilatory nitrite reductase from Candida utilis

1996

Sengupta, S.; Shaila, M.S.; Rao, G.R.

Biochem. J.

317

147-155

394526

8639023

Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans

1996

Hole, U.H.; Vollack, K.U.; Zumft, W.G.; Eisenmann, E.; Siddiqui, R.A.; Friedrich, B.; Kroneck, P.M.H.

Arch. Microbiol.

165

55-61

394546

7356639

First practical assay for soluble nitrous oxide reductase of denitrifying bacteria and a partial kinetic characterization

1980

Kristjansson, J.K.; Hollocher, T.C.

J. Biol. Chem.

255

704-707

394898

6742957

Purification and characterization of an inducible dissimilatory type sulfite reductase from Clostridium pasteurianum

1984

Harrison, G.; Curle, C.; Laishley, E.J.

Arch. Microbiol.

138

72-78

395164

3888257

Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12

1985

Morpeth, F.F.; Boxer, D.H.

Biochemistry

24

40-46

395185

11844760

Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12

2002

Steward, V.; Lu, Y.; Darwin, A.J.

J. Bacteriol.

184

1314-1323

395191

11560477

Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemical modulation of enzyme activity

2001

Anderson, L.J.; Richardson, D.J.; Butt, J.N.

Biochemistry

40

11294-11307

395560

6303306

Purification and properties of the membrane-bound by hydrogenase from Desulfovibrio desulfuricans

1983

Lalla-Maharajh, W.V.; Hall, D.O.; Cammack, R.; Rao, K.K.

Biochem. J.

209

445-454

395561

5650411

Purification and properties of hydrogenases of different origins

1968

Yagi, T.; Honya, M.; Tamiya, N.

Biochim. Biophys. Acta

153

699-705

395562

181372

Properties of purified hydrogenase from the particulate fraction of Desulfovibrio vulgaris, Miyazaki

1976

Yagi, T.; Kimura, K.; Daidoji, H.; Sakai, F.; Tamura, S.; Inokuchi, H.

J. Biochem.

79

661-671

437693

-

The interaction of ferredoxin-linked sulfite reductase with ferredoxin

1987

Hirasawa, M.; Boyer, J.M.; Gray, K.A.; Davis, D.J.; Knaff, D.B.

FEBS Lett.

221

343-348

439641

10714990

Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction

2000

Ma, K.; Weiss, R.; Adams, M.W.W.

J. Bacteriol.

182

1864-1871

439665

8513797

Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii

1993

Happe, T.; Naber, J.D.

Eur. J. Biochem.

214

475-481

439669

6327705

The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I

1984

Adams, M.W.W.; Mortenson, L.E.

J. Biol. Chem.

259

7045-7055

439682

4433567

Purification and properties of hydrogenase from Clostridium pasteurianum W5

1974

Chen, J.S.; Mortenson, L.E.

Biochim. Biophys. Acta

371

283-298

439687

9703971

The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity

1998

De Luca, G.; De Philip, P.; Rousset, M.; Belaich, J.P.; Dermoun, Z.

Biochem. Biophys. Res. Commun.

248

591-596

439699

186126

Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16

1976

Schneider, K.; Schlegel, H.G.

Biochim. Biophys. Acta

452

66-80

439711

9042758

Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22

1997

Grzeszik, C.; Ross, K.; Schneider, K.; Reh, M.; Schlegel, H.G.

Arch. Microbiol.

167

172-176

440297

-

Effect of gamma-radiation on Methanosarcina hydrogenase containing transition metal ions

1990

Arnikar, H.J.; Bhosale, S.B.; Kshirsagar, D.C.; Kapadi, A.H.; Yeole, T.Y.

J. Radioanal. Nucl. Chem.

142

349-358

440299

9555882

Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Go1

1998

Abken, H.J.; Tietze, M.; Brodersen, J.; Baumer, S.; Beifuss, U.; Deppenmeier, U.

J. Bacteriol.

180

2027-2032

440443

-

Reversible inactivation of ferredoxin-nitrate reductase from the cyanobacterium Plectonema boryanum. The role of superoxide anion and cyanide

1986

Mikami, B.; Ida, S.

Plant Cell Physiol.

27

1013-1021

440444

-

Purification and properties of ferredoxin-nitrate reductase from the cyanobacterium Plectonema boryanum

1984

Mikami, B.; Ida, S.

Biochim. Biophys. Acta

791

294-304

440447

6437330

Regulation of the nitrate reductase level in anacystis nidulans: Activity decay under nitrogen stress

1984

Herrero, A.; Flores, E.; Guerrero, M.G.

Arch. Biochem. Biophys.

234

454-459

440448

6780511

Regulation of nitrate reductase levels in the cyanobacteria Anacystis nidulans, Anabaena sp. strain 7119, and Nostoc sp. strain 6719

1981

Herrero, A.; Flores, E.; Guerrero, M.G.

J. Bacteriol.

145

175-180

440450

166876

Ferredoxin-linked nitrate reductase from the phototrophic bacterium Ectothiorhodospira shaposhnikovii

1975

Malofeeva, I.V.; Kondratieva, E.N.; Rubin, A.B.

FEBS Lett.

53

188-189

440451

202590

Studies on nitrate reductase of Clostridium perfringens. Purification, some properties, and effect of tungstate on its formation

1977

Seki-Chiba, S.; Ishimoto, M.

J. Biochem.

82

1663-1671

440453

11731152

Assimilatory nitrate reductase from the haloarchaeon Haloferax mediterranei: Purification and characterization

2001

Martinez-Espinosa, R.M.; Marhuenda-Egea, F.C.; Bonete, M.J.

FEMS Microbiol. Lett.

204

381-385

440454

8624415

A cyanobacterial narB gene encodes a ferredoxin-dependent nitrate reductase

1996

Rubio, L.M.; Herrero, A.; Flores, E.

Plant Mol. Biol.

30

845-850

440455

-

Effect of a constant supply of different nitrogen sources on protein and carbohydrate content and enzyme activities of Anabaena variabilis cells

1995

Sanz, A.P.; Moreno-Vivian, C.; Maldonado, J.M.; Gonzales-Fontes, A.

Physiol. Plant.

95

39-44

440456

-

Multimodal kinetics: Cyanobacterial nitrate reductase and other enzyme, transport and binding systems

1998

Nissen, P.; Martin-Nieto, J.

Physiol. Plant.

104

503-511

639393

9665708

Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila

1998

Simianu, M.; Murakami, E.; Brewer, J.M.; Ragsdale, S.W.

Biochemistry

37

10027-10039

639394

11034998

Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophilo

2001

Murakami, E.; Deppenmeier, U.; Ragsdale, S.W.

J. Biol. Chem.

276

2432-2439

644550

-

On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species

1985

Neumann, S.; Simon, H.

FEBS Lett.

167

29-32

644568

-

Purification and some properties of xanthine dehydrogenase from wheat leaves

1998

Montalbini, P.

Plant Sci.

134

89-102

644570

8706691

Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor

1996

Gremer, L.; Meyer, O.

Eur. J. Biochem.

238

862-866

644592

-

Purification and characterization of xanthine dehydrogenase from Clostridium acidiurici grown in the presence of selenium

1984

Wagner, R.; Cammack, R.; Andreesen, J.R.

Biochim. Biophys. Acta

791

63-74

644614

518233

Selenium requirement for active xanthine dehydrogenase from Clostridium acidiurici and Clostridium cylindrosporum

1979

Wagner, R.; Andreesen, J.R.

Arch. Microbiol.

121

255-260

644811

9295321

Purification and characterization of the selenate reductase from Thauera selenatis

1997

Schroder, I.; Rech, S.; Krafft, T.; Macy, J.M.

J. Biol. Chem.

272

23765-23768

644812

10525169

Bacterial respiration of arsenic and selenium

1999

Stolz, J.F.; Oremland, R.S.

FEMS Microbiol. Rev.

23

615-627

644816

14638434

Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase

2003

Watts, C.A.; Ridley, H.; Condie, K.L.; Leaver, J.T.; Richardson, D.J.; Butler, C.S.

FEMS Microbiol. Lett.

228

273-279

654347

12139973

Bacterial expression of the molybdenum domain of assimilatory nitrate reductase: production of both the functional molybdenum-containing domain and the nonfunctional tungsten analog

2002

Pollock, V.V.; Conover, R.C.; Johnson, M.K.; Barber, M.J.

Arch. Biochem. Biophys.

403

237-248

654386

9914308

Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus voltae

1999

Brodersen, J.; Gottschalk, G.; Deppenmeier, U.

Arch. Microbiol.

171

115-121

654733

14756575

Substrate binding and reduction of benzoyl-CoA reductase: evidence for nucleotide-dependent conformational changes

2004

Mobitz, H.; Friedrich, T.; Boll, M.

Biochemistry

43

1376-1385

654821

12034472

HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria

2002

Schmitz, O.; Boison, G.; Salzmann, H.; Bothe, H.; Schutz, K.; Wang, S.H.; Happe, T.

Biochim. Biophys. Acta

1554

66-74

655400

8174566

Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri

1994

Heiden, S.; Hedderich, R.; Setzke, E.; Thauer, R.K.

Eur. J. Biochem.

221

855-861

655446

12423371

Purification and catalytic properties of a CO-oxidizing:H2-evolving enzyme complex from Carboxydothermus hydrogenoformans

2002

Soboh, B.; Linder, D.; Hedderich, R.

Eur. J. Biochem.

269

5712-5721

655713

-

Properties and mechanistic aspects of newly found redox enzymes from anaerobes suitable for bioconversions on preparatory scale

1993

Simon, H.

Indian J. Chem. B

32

170-175

655823

7961460

Characterization of a CO:heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila

1994

Peer, C.W.; Painter, M.H.; Rasche, M.E.; Ferry, J.G.

J. Bacteriol.

176

6974-6979

656734

15256587

A multisubunit membrane-bound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis

2004

Soboh, B.; Linder, D.; Hedderich, R.

Microbiology

150

2451-2463

657587

12902251

Characterization of the corrinoid iron-sulfur protein tetrachloroethene reductive dehalogenase of Dehalobacter restrictus

2003

Maillard, J.; Schumacher, W.; Vazquez, F.; Regeard, C.; Hagen, W.R.; Holliger, C.

Appl. Environ. Microbiol.

69

4628-4638

657605

15746376

Characterization of hydrogenase and reductive dehalogenase activities of Dehalococcoides ethenogenes strain 195

2005

Nijenhuis, I.; Zinder, S.H.

Appl. Environ. Microbiol.

71

1664-1667

657689

12420164

A non-dechlorinating strain of Dehalospirillum multivorans: evidence for a key role of the corrinoid cofactor in the synthesis of an active tetrachloroethene dehalogenase

2002

Siebert, A.; Neumann, A.; Schubert, T.; Diekert, G.

Arch. Microbiol.

178

443-449

658175

14871493

Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase

2004

Hirasawa, M.; Rubio, L.M.; Griffin, J.L.; Flores, E.; Herrero, A.; Li, J.; Kim, S.K.; Hurley, J.K.; Tollin, G.; Knaff, D.B.

Biochim. Biophys. Acta

1608

155-162

658201

15342113

Respiratory nitrate reductase from haloarchaeon Haloferax mediterranei: biochemical and genetic analysis

2004

Lledo, B.; Martinez-Espinosa, R.M.; Marhuenda-Egea, F.C.; Bonete, M.J.

Biochim. Biophys. Acta

1674

50-59

658779

15927421

Enzymes responsible for chlorate reduction by Pseudomonas sp. are different from those used for perchlorate reduction by Azospira sp

2005

Steinberg, L.M.; Trimble, J.J.; Logan, B.E.

FEMS Microbiol. Lett.

247

153-159

658979

15012115

Reductively activated nitrous oxide reductase reacts directly with Substrate

2004

Chan, J.M.; Bollinger, J.A.; Grewell, C.L.; Dooley, D.M.

J. Am. Chem. Soc.

126

3030-3031

659023

12730181

Characterization of the chlorate reductase from Pseudomonas chloritidismutans

2003

Wolterink, A.F.; Schiltz, E.; Hagedoorn, P.L.; Hagen, W.R.; Kengen, S.W.; Stams, A.J.

J. Bacteriol.

185

3210-3213

659110

15168611

Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I

2004

Hedderich, R.

J. Bioenerg. Biomembr.

36

65-75

659366

15166246

Tuning a nitrate reductase for function: the first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties

2004

Jepson, B.J.N.; Anderson, L.J.; Rubio, L.M.; Taylor, C.J.; Butler, C.S.; Flores, E.; Herrero, A.; Butt, J.N.; Richardson, D.J.

J. Biol. Chem.

279

32212-32218

659882

14663073

The Bradyrhizobium japonicum napEDABC genes encoding the periplasmic nitrate reductase are essential for nitrate respiration

2003

Delgado, M.J.; Bonnard, N.; Tresierra-Ayala, A.; Bedmar, E.J.; Muller, P.

Microbiology

149

3395-3403

659990

14528294

Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase

2003

Arnoux, P.; Sabaty, M.; Alric, J.; Frangioni, B.; Guigliarelli, B.; Adriano, J.M.; Pignol, D.

Nat. Struct. Biol.

10

928-934

660264

-

Purification and characterization of ferredoxin-nitrite reductase from the eukaryotic microalga Monoraphidium braunii

2002

Vigara, J.; Garcia-Sanchez, M.I.; Garbayo, I.; Vilchez, C.; Vega, J.M.

Plant Physiol. Biochem.

40

401-405

660459

12538888

Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: characterization of an active site isoleucine

2003

Boulanger, M.J.; Murphy, M.E.

Protein Sci.

12

248-256

663000

12930520

Biochemical and functional properties of a pyruvate formate-lyase (PFL)-activating system in Streptococcus mutans

2003

Takahashi-Abbe, S.; Abe, K.; Takahashi, N.

Oral Microbiol. Immunol.

18

293-297

671935

15667294

Function of the Rhizobium etli CFN42 nirK gene in nitrite metabolism

2005

Bueno, E.; Gomez-Hernandez, N.; Girard, L.; Bedmar, E.J.; Delgado, M.J.

Biochem. Soc. Trans.

33

162-163

672279

16038606

Use of a reverse micelle system for study of oligomeric structure of NAD+-reducing hydrogenase from Ralstonia eutropha H16

2005

Tikhonova, T.V.; Kurkin, S.A.; Klyachko, N.L.; Popov, V.O.

Biochemistry

70

645-651

672282

17223791

Characterization of catalytic properties of hydrogenase isolated from the unicellular cyanobacterium Gloeocapsa alpicola CALU 743

2006

Serebryakova, L.T.; Sheremetieva, M.E.

Biochemistry

71

1370-1376

672331

15804488

Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135

2005

Pinho, D.; Besson, S.; Silva, P.J.; de Castro, B.; Moura, I.

Biochim. Biophys. Acta

1723

151-162

673234

16234931

Formation of a cytochrome c-nitrous oxide reductase complex is obligatory for N2O reduction by Paracoccus pantotrophus

2005

Rasmussen, T.; Brittain, T.; Berks, B.C.; Watmough, N.J.; Thomson, A.J.

Dalton Trans.

2005

3501-3506

673685

17207484

A needle in a haystack: The active site of the membrane-bound complex cytochrome c nitrite reductase

2007

Almeida, M.G.; Silveira, C.M.; Guigliarelli, B.; Bertrand, P.; Moura, J.J.; Moura, I.; Leger, C.

FEBS Lett.

581

284-288

674151

16190723

Electroenzymatic reactions. Investigation of a reductive dehalogenase by means of electrogenerated redox cosubstrates

2005

Diekert, G.; Gugova, D.; Limoges, B.; Robert, M.; Saveant, J.M.

J. Am. Chem. Soc.

127

13583-13588

674324

17237175

A novel ferredoxin-dependent glutamate synthase from the hydrogen-oxidizing chemoautotrophic bacterium, Hydrogenobacter thermophilus TK-6

2007

Kameya, M.; Ikeda, T.; Nakamura, M.; Arai, H.; Ishii, M.; Igarashi, Y.

J. Bacteriol.

189

2805-2812

674504

16048999

A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii

2005

Johnson, E.F.; Mukhopadhyay, B.

J. Biol. Chem.

280

38776-38786

674572

16613859

A random-sequential mechanism for nitrite binding and active site reduction in copper-containing nitrite reductase

2006

Wijma, H.J.; Jeuken, L.J.; Verbeet, M.P.; Armstrong, F.A.; Canters, G.W.

J. Biol. Chem.

281

16340-16346

674613

16286471

NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly

2006

Vergnes, A.; Pommier, J.; Toci, R.; Blasco, F.; Giordano, G.; Magalon, A.

J. Biol. Chem.

281

2170-2176

674919

16187073

Hydrogenases in Desulfovibrio vulgaris Hildenborough: structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase

2005

Valente, F.M.; Oliveira, A.S.; Gnadt, N.; Pacheco, I.; Coelho, A.V.; Xavier, A.V.; Teixeira, M.; Soares, C.M.; Pereira, I.A.

J. Biol. Inorg. Chem.

10

667-682

676328

16143847

Photosynthetic nitrate assimilation in cyanobacteria

2005

Flores, E.; Frias, J.E.; Rubio, L.M.; Herrero, A.

Photosynth. Res.

83

117-133

684990

17900239

Voltammetric characterization of the aerobic energy-dissipating nitrate reductase of Paracoccus pantotrophus: exploring the activity of a redox-balancing enzyme as a function of electrochemical potential

2008

Gates, A.J.; Richardson, D.J.; Butt, J.N.

Biochem. J.

409

159-168

695534

19468822

Analysis of glutamate homeostasis by overexpression of Fd-GOGAT gene in Arabidopsis thaliana

2009

Ishizaki, T.; Ohsumi, C.; Totsuka, K.; Igarashi, D.

Amino Acids

38

943-950

696082

14674886

NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing

2004

Brondijk, T.H.; Nilavongse, A.; Filenko, N.; Richardson, D.J.; Cole, J.A.

Biochem. J.

379

47-55

696159

18298372

Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens

2008

Tikhonova, T.V.; Slutskaya, E.S.; Filimonenkov, A.A.; Boyko, K.M.; Kleimenov, S.Y.; Konarev, P.V.; Polyakov, K.M.; Svergun, D.I.; Trofimov, A.A.; Khomenkov, V.G.; Zvyagilskaya, R.A.; Popov, V.O.

Biochemistry (Moscow)

73

164-170

696256

18311941

Role of a conserved glutamine residue in tuning the catalytic activity of Escherichia coli cytochrome c nitrite reductase

2008

Clarke, T.A.; Kemp, G.L.; Van Wonderen, J.H.; Doyle, R.M.; Cole, J.A.; Tovell, N.; Cheesman, M.R.; Butt, J.N.; Richardson, D.J.; Hemmings, A.M.

Biochemistry

47

3789-3799

696519

4063066

Purification and some properties of an acryloyl-CoA reductase of Clostridium kluyveri

1985

Sedlmeier, H.; Simon, H.

Biol. Chem. Hoppe-Seyler

366

953-961

697599

-

Purification and some physiochemical properties of nitrate reductase isolated from winter triticale seedlings

2008

Sempruch, C.; Ciepiela, A.; Sprawka, I.; Chrzanowski, G.

Electron. J. Pol. Agric. Univ.

11

1-1

697691

2139607

Purification and further characterization of the second nitrate reductase of Escherichia coli K12

1990

Iobbi-Nivol, C.; Santini, C.L.; Blasco, F.; Giordano, G.

Eur. J. Biochem.

188

679-687

697696

8119278

Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha

1994

Berks, B.C.; Richardson, D.J.; Robinson, C.; Reilly, A.; Aplin, R.T.; Ferguson, S.J.

Eur. J. Biochem.

220

117-124

697965

-

The identification of a periplasmic nitrate reductase in Paracoccus denitrificans

1993

Sears, H.J.; Ferguson, S.J.; Richardson, D.J.; Spiro, S.

FEMS MIcrobiol. Lett.

113

107-112

698636

19060147

Catabolite repression control of napF (periplasmic nitrate reductase) operon expression in Escherichia coli K-12

2009

Stewart, V.; Bledsoe, P.J.; Chen, L.L.; Cai, A.

J. Bacteriol.

191

996-1005

698876

18245085

The nitric oxide reductase activity of cytochrome c nitrite reductase from Escherichia coli

2008

van Wonderen, J.H.; Burlat, B.; Richardson, D.J.; Cheesman, M.R.; Butt, J.N.

J. Biol. Chem.

283

9587-9594

699384

17681606

Anaerobic purification, characterization and preliminary mechanistic study of recombinant nitrous oxide reductase from Achromobacter cycloclastes

2007

Fujita, K.; Chan, J.M.; Bollinger, J.A.; Alvarez, M.L.; Dooley, D.M.

J. Inorg. Biochem.

101

1836-1844

699990

18433623

Escherichia coli cytochrome c nitrite reductase NrfA

2008

Clarke, T.A.; Mills, P.C.; Poock, S.R.; Butt, J.N.; Cheesman, M.R.; Cole, J.A.; Hinton, J.C.; Hemmings, A.M.; Kemp, G.; Soederberg, C.A.; Spiro, S.; Van Wonderen, J.; Richardson, D.J.

Methods Enzymol.

437

63-77

700033

18375814

A combination of cytochrome c nitrite reductase (NrfA) and flavorubredoxin (NorV) protects Salmonella enterica serovar Typhimurium against killing by NO in anoxic environments

2008

Mills, P.C.; Rowley, G.; Spiro, S.; Hinton, J.C.; Richardson, D.J.

Microbiology

154

1218-1228

700254

10564515

Expression of the Escherichia coli NRZ nitrate reductase is highly growth phase dependent and is controlled by RpoS, the alternative vegetative sigma factor

1999

Chang, L.; Wie, L.I.; Audia, J.P.; Morton, R.A.; Schellhorn, H.E.

Mol. Microbiol.

34

756-766

704088

-

Purification and characterization of [Fe]-hydrogenase from high yielding hydrogen-producing strain, Enterobacter cloacae IIT-BT08 (MTCC 5373)

2009

Dutta, T.; Das, A.; Das, D.

Int. J. Hydrogen Energy

34

7530-7537

704606

19801638

Overexpression, isolation and spectroscopic characterization of the bidirectional [NiFe]-hydrogenase from Synechocystis sp. PCC 6803

2009

Germer, F.; Zebger, I.; Saggu, M.; Lendzian, F.; Schulz, R.; Appel, J.

J. Biol. Chem.

284

36462-36472

710714

20944237

Structures of complexes of octahaem cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens with sulfite and cyanide

2010

Trofimov, A.A.; Polyakov, K.M.; Boyko, K.M.; Tikhonova, T.V.; Safonova, T.N.; Tikhonov, A.V.; Popov, A.N.; Popov, V.O.

Acta Crystallogr. Sect. D

66

1043-1047

711190

10387097

Reactions of dimethylsulfoxide reductase from Rhodobacter capsulatus with dimethyl sulfide and with dimethyl sulfoxide: complexities revealed by conventional and stopped-flow spectrophotometry

1999

Adams, B.; Smith, A.T.; Bailey, S.; McEwan, A.G.; Bray, R.C.

Biochemistry

38

8501-8511

711263

20812758

Enzymatic interconversion of ammonia and nitrite: The right tool for the job

2010

Kostera, J.; McGarry, J.; Pacheco, A.

Biochemistry

49

8546-8553

711343

20689707

Measuring the cytochrome C nitrite reductase activity-practical considerations on the enzyme assays

2010

Silveira, C.M.; Besson, S.; Moura, I.; Moura, J.J.; Almeida, M.G.

Bioinorg. Chem. Appl.

2010

634597

711817

19904421

How algae produce hydrogen--news from the photosynthetic hydrogenase

2009

Stripp, S.T.; Happe, T.

Dalton Trans.

2009

9960-9969

712000

15063748

The critical role of tryptophan-116 in the catalytic cycle of dimethylsulfoxide reductase from Rhodobacter capsulatus

2004

Ridge, J.P.; Aguey-Zinsou, K.F.; Bernhardt, P.V.; Hanson, G.R.; McEwan, A.G.

FEBS Lett.

563

197-202

712281

19411328

The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production

2009

Schut, G.J.; Adams, M.W.

J. Bacteriol.

191

4451-4457

712507

19241093

A thermostable hybrid cluster protein from Pyrococcus furiosus: effects of the loss of a three helix bundle subdomain

2009

Overeijnder, M.L.; Hagen, W.R.; Hagedoorn, P.L.

J. Biol. Inorg. Chem.

14

703-710

712734

10835270

Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site

2000

Stewart, L.J.; Bailey, S.; Bennett, B.; Charnock, J.M.; Garner, C.D.; McAlpine, A.S.

J. Mol. Biol.

299

593-600

712960

9720047

Asymmetric reduction of racemic sulfoxides by dimethyl sulfoxide reductases from Rhodobacter capsulatus, Escherichia coli and Proteus species

1998

Hanlon, S.; Graham, D.; Hogan, P.; Holt, R.; Reeve, C.; Shaw, A.; McEwan, A.

Microbiology

144

2247-2253

714365

20547201

Thermostable properties of the periplasmic selenate reductase from Thauera selenatis

2010

Dridge, E.J.; Butler, C.S.

Biochimie

92

1268-1273

714522

20530887

Cloning of a novel dehalogenase from environmental DNA

2010

Kimoto, H.; Suye, S.; Makishima, H.; Arai, J.; Yamaguchi, S.; Fujii, Y.; Yoshioka, T.; Taketo, A.

Biosci. Biotechnol. Biochem.

74

1290-1292

714886

8706745

Dimethylsulfide: acceptor oxidoreductase from Rhodobacter sulfidophilus - The purified enzyme contains b-type haem and a pterin molybdenum cofactor

1996

Hanlon, S.; Toh, T.; Solomon, P.; Holt, R.; McEwan, A.

Eur. J. Biochem.

239

391-396

716106

11265464

Fe-only hydrogenase from Thermotoga maritima

2001

Verhagen, M.; Adams, M.

Methods Enzymol.

331

216-226

721456

16897035

Expression and characterization of the assimilatory NADH-nitrite reductase from the phototrophic bacterium Rhodobacter capsulatus E1F1

2006

Olmo-Mira, M.F.; Cabello, P.; Pino, C.; Martinez-Luque, M.; Richardson, D.J.; Castillo, F.; Roldan, M.D.; Moreno-Vivian, C.

Arch. Microbiol.

186

339-344

722777

22157005

Engineering hyperthermophilic archaeon Pyrococcus furiosus to overproduce its cytoplasmic [NiFe]-hydrogenase

2012

Chandrayan, S.K.; McTernan, P.M.; Hopkins, R.C.; Sun, J.; Jenney, F.E.; Adams, M.W.

J. Biol. Chem.

287

3257-3264

723218

23078170

Urocanate reductase: identification of a novel anaerobic respiratory pathway in Shewanella oneidensis MR-1

2012

Bogachev, A.V.; Bertsova, Y.V.; Bloch, D.A.; Verkhovsky, M.I.

Mol. Microbiol.

86

1452-1463

723828

22281743

Covalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activity

2012

Trofimov, A.A.; Polyakov, K.M.; Tikhonova, T.V.; Tikhonov, A.V.; Safonova, T.N.; Boyko, K.M.; Dorovatovskii, P.V.; Popov, V.O.

Acta Crystallogr. Sect. D

68

144-153

726100

22451106

Biochemical characterization of the purple form of Marinobacter hydrocarbonoclasticus nitrous oxide reductase

2012

DellAcqua, S.; Pauleta, S.; Moura, J.; Moura, I.

Philos. Trans. R. Soc. Lond. B Biol. Sci.

367

1204-1212

726144

22685081

A novel in-gel assay and an improved kinetic assay for determining in vitro sulfite reductase activity in plants

2012

Brychkova, G.; Yarmolinsky, D.; Ventura, Y.; Sagi, M.

Plant Cell Physiol.

53

1507-1516

726450

22238192

Structure-function relationship of assimilatory nitrite reductases from the leaf and root of tobacco based on high-resolution structures

2012

Nakano, S.; Takahashi, M.; Sakamoto, A.; Morikawa, H.; Katayanagi, K.

Protein Sci.

21

383-395

726523

21938458

Expression of the nos operon proteins from Pseudomonas stutzeri in transgenic plants to assemble nitrous oxide reductase

2012

Wan, S.; Mottiar, Y.; Johnson, A.M.; Goto, K.; Altosaar, I.

Transgenic Res.

21

593-603

726801

1654831

Purification and properties of a dissimilatory nitrate reductase from Haloferax denitrificans

1991

Hochstein, L.; Lang, F.

Arch. Biochem. Biophys.

288

380-385

727084

23499847

Cu-NirK from Haloferax mediterranei as an example of metalloprotein maturation and exportation via Tat system

2013

Esclapez, J.; Zafrilla, B.; Martínez-Espinosa, R.M.; Bonete, M.J.

Biochim. Biophys. Acta

1834

1003-1009

727542

11267765

Purification and characterisation of a possible assimilatory nitrite reductase from the halophile archaeon Haloferax mediterranei

2001

Martínez-Espinosa, R.M.; Marhuenda-Egea, F.C.; Bonete, M.J.

FEMS Microbiol. Lett.

196

113-118

728432

23479755

Identification of a reductive tetrachloroethene dehalogenase in Shewanella sediminis

2013

Lohner, S.; Spormann, A.

Philos. Trans. R. Soc. Lond. B Biol. Sci.

368

20120326

729317

25512066

Characterisation of chlorate reduction in the haloarchaeon Haloferax mediterranei

2015

Martínez-Espinosa, R.M.; Richardson, D.J.; Bonete, M.J.

Biochim. Biophys. Acta

1850

587-594

730810

21502530

Discovery of epoxyqueuosine (oQ) reductase reveals parallels between halorespiration and tRNA modification

2011

Miles, Z.D.; McCarty, R.M.; Molnar, G.; Bandarian, V.

Proc. Natl. Acad. Sci. USA

108

7368-7372

739959

242299

Purification and properties of thiosulfate reductase from Desulfovibrio gigas

1975

Hatchikian, E.

Arch. Microbiol.

105

249-256

740320

-

An artificial co-enzyme based on the viologen skeleton for highly efficient CO2 reduction to formic acid with formate dehydrogenase

2017

Ikeyama, S.; Amao, Y.

ChemCatChem

9

833-838

740422

28321615

Nitrate reduction in Haloferax alexandrinus: the case of assimilatory nitrate reductase

2017

Kilic, V.; Kilic, G.A.; Kutlu, H.M.; Martinez-Espinosa, R.M.

Extremophiles

21

551-561

740591

5573735

Thiosulfate reductase of Desulfovibrio vulgaris

1971

Haschke, R.; Campbell, L.

J. Bacteriol.

106

603-607

740618

23316038

A reversible electron-bifurcating ferredoxin- and NAD-dependent [FeFe]-hydrogenase (HydABC) in Moorella thermoacetica

2013

Wang, S.; Huang, H.; Kahnt, J.; Thauer, R.K.

J. Bacteriol.

195

1267-1275

740631

5784203

Thiosulfate reductase isolated from Desulfotomaculum nigrificans

1969

Nakatsukasa, W.; Akagi, J.

J. Bacteriol.

98

429-433

740639

-

Biochemical studies on sulfate-reducing bacteria: VI. separation of hydrogenase and thiosulfate reductase and partial purification of cytochrome and green pigment

1957

Ishimoto, M.; Koyama, J.

J. Biochem.

44

233-242

740640

2993256

Purification and properties of thiosulfate reductase from Desulfovibrio vulgaris, Miyazaki F

1985

Aketagawa, J.; Kobayashi, K.; Ishimoto, M.

J. Biochem.

97

1025-1032

741478

26509703

Periplasmic nitrate reductase and formate dehydrogenase similar molecular architectures with very different enzymatic activities

2015

Cerqueira, N.M.; Gonzalez, P.J.; Fernandes, P.A.; Moura, J.J.; Ramos, M.J.

Acc. Chem. Res.

48

2875-2884

741637

24610039

Antimicrobial activity and physical characterization of silver nanoparticles green synthesized using nitrate reductase from Fusarium oxysporum

2014

Gholami-Shabani, M.; Akbarzadeh, A.; Norouzian, D.; Amini, A.; Gholami-Shabani, Z.; Imani, A.; Chiani, M.; Riazi, G.; Shams-Ghahfarokhi, M.; Razzaghi-Abyaneh, M.

Appl. Biochem. Biotechnol.

172

4084-4098

742500

26573766

Evidence for the involvement of two heterodisulfide reductases in the energy-conserving system of Methanomassiliicoccus luminyensis

2016

Kroeninger, L.; Berger, S.; Welte, C.; Deppenmeier, U.

FEBS J.

283

472-483

742504

-

The F420H2 heterodisulfide oxidoreductase system from Methanosarcina species. 2-Hydroxyphenazine mediates electron transfer from F420H2 dehydrogenase to heterodisulfide reductase

1998

Baeumer, S.; Murakami, E.; Brodersen, J.; Gottschalk, G.; Ragsdale, S.; Deppenmeier, U.

FEBS Lett.

428

295-298

742746

25658043

Resolution of key roles for the distal pocket histidine in cytochrome C nitrite reductases

2015

Lockwood, C.W.; Burlat, B.; Cheesman, M.R.; Kern, M.; Simon, J.; Clarke, T.A.; Richardson, D.J.; Butt, J.N.

J. Am. Chem. Soc.

137

3059-3068

742753

28228011

Spectroscopic definition of the CuZ* intermediate in turnover of nitrous oxide reductase and molecular insight into the catalytic mechanism

2017

Johnston, E.M.; Carreira, C.; DellAcqua, S.; Dey, S.G.; Pauleta, S.R.; Moura, I.; Solomon, E.I.

J. Am. Chem. Soc.

139

4462-4476

742858

24311779

The bidirectional NiFe-hydrogenase in Synechocystis sp. PCC 6803 is reduced by flavodoxin and ferredoxin and is essential under mixotrophic, nitrate-limiting conditions

2014

Gutekunst, K.; Chen, X.; Schreiber, K.; Kaspar, U.; Makam, S.; Appel, J.

J. Biol. Chem.

289

1930-1937

742887

25673691

Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum structural and functional insights into thiosulfate oxidation

2015

Brito, J.A.; Denkmann, K.; Pereira, I.A.; Archer, M.; Dahl, C.

J. Biol. Chem.

290

9222-9238

743294

28012016

The ferredoxin-dependent glutamate synthase (OsFd-GOGAT) participates in leaf senescence and the nitrogen remobilization in rice

2017

Zeng, D.D.; Qin, R.; Li, M.; Alamin, M.; Jin, X.L.; Liu, Y.; Shi, C.H.

Mol. Genet. Genomics

292

385-395

743811

27211925

The Fd-GOGAT1 mutant gene lc7 confers resistance to Xanthomonas oryzae pv. Oryzae in rice

2016

Chen, H.; Li, C.; Liu, L.; Zhao, J.; Cheng, X.; Jiang, G.; Zhai, W.

Sci. Rep.

6

26411

743815

27411448

Direct interaction with ACR11 is necessary for post-transcriptional control of GLU1-encoded ferredoxin-dependent glutamate synthase in leaves

2016

Takabayashi, A.; Niwata, A.; Tanaka, A.

Sci. Rep.

6

29668

744338

26230193

Biochemical and spectroscopic studies of epoxyqueuosine reductase a novel iron-sulfur cluster- and cobalamin-containing protein involved in the biosynthesis of queuosine

2015

Miles, Z.D.; Myers, W.K.; Kincannon, W.M.; Britt, R.D.; Bandarian, V.

Biochemistry

54

4927-4935

744981

28421054

Isolation and characterization of Dehalobacter sp. strain TeCB1 including identification of TcbA a novel tetra- and trichlorobenzene reductive dehalogenase

2017

Alfan-Guzman, R.; Ertan, H.; Manefield, M.; Lee, M.

Front. Microbiol.

8

558

745333

26378237

Epoxyqueuosine reductase structure suggests a mechanism for cobalamin-dependent tRNA modification

2015

Payne, K.A.; Fisher, K.; Sjuts, H.; Dunstan, M.S.; Bellina, B.; Johannissen, L.; Barran, P.; Hay, S.; Rigby, S.E.; Leys, D.

J. Biol. Chem.

290

27572-27581

763018

31276306

New light on ancient enzymes - in vitro CO2 fixation by pyruvate synthase of Desulfovibrio africanus and Sulfolobus acidocaldarius

2019

Witt, A.; Pozzi, R.; Diesch, S.; Haedicke, O.; Grammel, H.

FEBS J.

286

4494-4508

763185

30244570

Exploring ferredoxin-dependent glutamate synthase as an enzymatic bioelectrocatalyst

2018

Wu, F.; Yu, P.; Yang, X.; Han, Z.; Wang, M.; Mao, L.

J. Am. Chem. Soc.

140

12700-12704

763248

24302732

Structural basis of biological no generation by octaheme oxidoreductases

2014

Maalcke, W.; Dietl, A.; Marritt, S.; Butt, J.; Jetten, M.; Keltjens, J.; Barends, T.; Kartal, B.

J. Biol. Chem.

289

1228-1242

763503

33649331

Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production

2021

Venskutonyte, R.; Koh, A.; Stenstroem, O.; Khan, M.T.; Lundqvist, A.; Akke, M.; Baeckhed, F.; Lindkvist-Petersson, K.

Nat. Commun.

12

1347

763521

-

Activation of the catalytic function of formaldehyde dehydrogenase for formate reduction by single-electron reduced methylviologen

2018

Ishibashi, T.; Ikeyama, S.; Amao, Y.

New J. Chem.

42

18508-18512

763549

28975508

Identification of the ferredoxin interaction sites on ferredoxin-dependent glutamate synthase from Synechocystis sp. PCC 6803

2017

Hirasawa, M.; Solis, J.; Vaidyanathan, N.; Srivastava, A.P.; Wynn, R.M.; Sutton, R.B.; Knaff, D.B.

Photosynth. Res.

134

317-328

763962

32978134

Possible involvement of a tetrathionate reductase homolog in dissimilatory arsenate reduction by Anaeromyxobacter sp. strain PSR-1

2020

Muramatsu, F.; Tonomura, M.; Yamada, M.; Kasahara, Y.; Yamamura, S.; Iino, T.; Amachi, S.

Appl. Environ. Microbiol.

86

e00829-20

764091

-

Expression, characterization and molecular docking of the assimilatory NADH-nitrite reductase from Acidovorax wautersii QZ-4

2020

Song, Q.; Wang, B.; Zhao, F.; Han, Y.; Zhou, Z.

Biochem. Eng. J.

159

107589

764139

28520412

Identification of the ferredoxin-binding site of a ferredoxin-dependent cyanobacterial nitrate reductase

2017

Srivastava, A.P.; Hardy, E.P.; Allen, J.P.; Vaccaro, B.J.; Johnson, M.K.; Knaff, D.B.

Biochemistry

56

5582-5592

764198

32735861

Sulfite oxidation by the quinone-reducing molybdenum sulfite dehydrogenase SoeABC from the bacterium Aquifex aeolicus

2020

Boughanemi, S.; Infossi, P.; Giudici-Orticoni, M.T.; Schoepp-Cothenet, B.; Guiral, M.

Biochim. Biophys. Acta

1861

148279

764411

-

Photobiocatalytic H2 evolution of GaN ZnO and [FeFe]-hydrogenase recombinant Escherichia coli

2020

Kosem, N.; Honda, Y.; Watanabe, M.; Takagaki, A.; Tehrani, Z.; Haydous, F.; Lippert, T.; Ishihara, T.

Catal. Sci. Technol.

10

4042-4052

764582

32190953

A novel dimethylsulfoxide reductase family of molybdenum enzyme, Idr, is involved in iodate respiration by Pseudomonas sp. SCT

2020

Yamazaki, C.; Kashiwa, S.; Horiuchi, A.; Kasahara, Y.; Yamamura, S.; Amachi, S.

Environ. Microbiol.

22

2196-2212

764646

28321615

Nitrate reduction in Haloferax alexandrinus the case of assimilatory nitrate reductase

2017

Kilic, V.; Kilic, G.A.; Kutlu, H.M.; Martinez-Espinosa, R.M.

Extremophiles

21

551-561

764683

28062520

TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA

2017

Kurth, J.M.; Schuster, A.; Seel, W.; Herresthal, S.; Simon, J.; Dahl, C.

FEMS Microbiol. Lett.

364

fnx003

764685

29931366

Molecular cloning, expression and biochemical characterization of periplasmic nitrate reductase from Campylobacter jejuni

2018

Mintmier, B.; McGarry, J.M.; Sparacino-Watkins, C.E.; Sallmen, J.; Fischer-Schrader, K.; Magalon, A.; McCormick, J.R.; Stolz, J.F.; Schwarz, G.; Bain, D.J.; Basu, P.

FEMS Microbiol. Lett.

365

fny151

764856

28389402

Heterologous expression and biochemical characterization of assimilatory nitrate and nitrite reductase reveals adaption and potential of Bacillus megaterium NCT-2 in secondary salinization soil

2017

Chu, S.; Zhang, D.; Wang, D.; Zhi, Y.; Zhou, P.

Int. J. Biol. Macromol.

101

1019-1028

765056

31467084

Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes

2019

Jenner, L.P.; Kurth, J.M.; van Helmont, S.; Sokol, K.P.; Reisner, E.; Dahl, C.; Bradley, J.M.; Butt, J.N.; Cheesman, M.R.

J. Biol. Chem.

294

18002-18014

765066

32518164

Cytochrome c nitrite reductase from the bacterium Geobacter lovleyi represents a new NrfA subclass

2020

Campecino, J.; Lagishetty, S.; Wawrzak, Z.; Sosa Alfaro, V.; Lehnert, N.; Reguera, G.; Hu, J.; Hegg, E.L.

J. Biol. Chem.

295

11455-11465

765075

33652023

Characterization of a nitrite-reducing octaheme hydroxylamine oxidoreductase that lacks the tyrosine cross-link

2021

Ferousi, C.; Schmitz, R.; Maalcke, W.; Lindhoud, S.; Versantvoort, W.; Jetten, M.; Reimann, J.; Kartal, B.

J. Biol. Chem.

296

100476

765636

30884848

Isoform-specific NO synthesis by Arabidopsis thaliana nitrate reductase

2019

Mohn, M.A.; Thaqi, B.; Fischer-Schrader, K.

Plants (Basel)

8

67