BRENDA - Enzyme Database
show all sequences of 1.8.7.1

Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin

Kim, J.Y.; Nakayama, M.; Toyota, H.; Kurisu, G.; Hase, T.; J. Biochem. 160, 101-109 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Zea mays
Crystallization (Commentary)
Crystallization
Organism
complex of maize sulfite reductase SiR and ferredoxin. A few negative residues of ferredoxin contact with a narrow area of SiR with positive electrostatic surface potential. The [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Engineering
Amino acid exchange
Commentary
Organism
A493G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
A503G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Arg111Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Arg114Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Arg324Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
L499G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
L502A
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Lys117Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Lys582Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Lys584Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Lys66Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
P501G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
P541G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Q504G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Zea mays
O23813
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hydrogen sulfide + oxidized ferredoxin + H2O
-
742806
Zea mays
sulfite + reduced ferredoxin + H+
-
-
-
?
hydrogen sulfide + oxidized methyl viologen + H2O
-
742806
Zea mays
sulfite + reduced methyl viologen + H+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
[4Fe-4S]-center
in cocrystals, the [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Zea mays
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
[4Fe-4S]-center
in cocrystals, the [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Crystallization (Commentary) (protein specific)
Crystallization
Organism
complex of maize sulfite reductase SiR and ferredoxin. A few negative residues of ferredoxin contact with a narrow area of SiR with positive electrostatic surface potential. The [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Zea mays
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A493G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
A503G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Arg111Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Arg114Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Arg324Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
L499G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
L502A
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Lys117Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Lys582Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Lys584Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
Lys66Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Zea mays
P501G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
P541G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Q504G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Zea mays
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hydrogen sulfide + oxidized ferredoxin + H2O
-
742806
Zea mays
sulfite + reduced ferredoxin + H+
-
-
-
?
hydrogen sulfide + oxidized methyl viologen + H2O
-
742806
Zea mays
sulfite + reduced methyl viologen + H+
-
-
-
?
Other publictions for EC 1.8.7.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742810
Sekine
Characterization of two ferre ...
Cyanidioschyzon merolae 10D, Cyanidioschyzon merolae
J. Biochem.
162
37-43
2017
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1
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2
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6
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3
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1
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2
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741859
Kim
Non-covalent forces tune the ...
Zea mays
Biochem. J.
473
3837-3854
2016
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1
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1
1
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1
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742806
Kim
Structural and mutational stu ...
Zea mays
J. Biochem.
160
101-109
2016
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1
1
14
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14
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2
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726232
Yarmolinsky
Sulfite reductase protects pla ...
Arabidopsis thaliana, Solanum lycopersicum
Plant Physiol.
161
725-743
2013
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-
-
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-
-
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2
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2
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10
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2
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4
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4
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2
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10
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2
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2
2
-
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726121
McManus
Genotypic variation in sulfur ...
Allium cepa
Phytochemistry
83
34-42
2012
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1
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1
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2
1
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3
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3
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1
1
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1
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1
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1
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3
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1
1
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1
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1
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726144
Brychkova
A novel in-gel assay and an im ...
Arabidopsis thaliana, Solanum lycopersicum
Plant Cell Physiol.
53
1507-1516
2012
4
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8
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8
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2
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726184
Kang
In vivo effects of NbSiR silen ...
Nicotiana benthamiana
Plant Mol. Biol.
72
569-583
2010
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1
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1
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2
2
-
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696126
Sekine
A novel variant of ferredoxin- ...
Cyanidioschyzon merolae
Biochem. J.
423
91-98
2009
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1
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2
2
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3
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1
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688412
Schiffer
Structure of the dissimilatory ...
Archaeoglobus fulgidus
J. Mol. Biol.
379
1063-1074
2008
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686650
Sekine
DNA binding and partial nucleo ...
Pisum sativum, Zea mays
FEBS J.
274
2054-2069
2007
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6
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674525
Saitoh
NMR study of the electron tran ...
Zea mays
J. Biol. Chem.
281
10482-10488
2006
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1
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4
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1
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4
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1
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4
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674459
Schnell
Siroheme- and [Fe4-S4]-depende ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
280
27319-27328
2005
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1
1
1
4
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6
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1
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674504
Johnson
A new type of sulfite reductas ...
Methanocaldococcus jannaschii
J. Biol. Chem.
280
38776-38786
2005
1
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2
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2
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1
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676333
Hirasawa
Chemical modification studies ...
Zea mays
Photosyn. Res.
86
325-336
2005
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3
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2
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3
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437707
Chi-Ham
The DNA-compacting protein DCP ...
Glycine max, Pisum sativum
Plant Mol. Biol.
49
621-631
2002
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657926
Champier
Reactivity, secondary structur ...
Escherichia coli
Biochemistry
41
3770-3780
2002
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437706
Yonekura-Sakakibara
Analysis of reductant supply s ...
Zea mays
Plant Physiol.
122
887-894
2000
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1
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437705
Akashi
Comparison of the electrostati ...
Zea mays
J. Biol. Chem.
274
29399-29405
1999
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3
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437704
Takahashi
Purification and characterizat ...
Brassica rapa
Biosci. Biotechnol. Biochem.
61
1486-1490
1997
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1
4
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1
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1
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1
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4
1
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1
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4
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2
1
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1
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1
1
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1
4
1
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437701
Takahashi
-
Effect of sulfur and nitrogen ...
Allium tuberosum
J. Plant Res.
109
363-368
1996
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437702
Takahashi
-
Purification and characterizat ...
Allium tuberosum
J. Plant Res.
109
45-52
1996
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437703
Takahashi
-
Ferredoxin-linked sulfite redu ...
Brassica rapa, Spinacia oleracea
Biosci. Biotechnol. Biochem.
60
142-144
1996
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437687
Koguchi
-
Isolation and partial characte ...
Pyropia yezoensis
Agric. Biol. Chem.
53
1653-1662
1989
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1
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437691
Brunold
Localization of enzymes of ass ...
Pisum sativum
Planta
179
228-234
1989
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437692
Koguchi
-
Reduction of S-sulfoglutathion ...
Arthrospira platensis, Arthrospira platensis OU-1
Agric. Biol. Chem.
53
783-788
1989
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2
2
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4
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437688
Koguchi
-
Purification and partial chara ...
Brassica rapa subsp. chinensis
Agric. Biol. Chem.
52
1867-1868
1988
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437689
Koguchi
-
Ferredoxin-sulfite reductase f ...
Arthrospira platensis, Arthrospira platensis OU-1
Agric. Biol. Chem.
52
373-380
1988
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437693
Hirasawa
-
The interaction of ferredoxin- ...
Spinacia oleracea
FEBS Lett.
221
343-348
1987
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437694
Krueger
Evidence for siroheme-Fe4S4 in ...
Pisum sativum, Spinacia oleracea
Biochemistry
21
2905-2909
1982
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437695
Krueger
Spinach siroheme enzymes: Isol ...
Spinacia oleracea
Biochemistry
21
2892-2904
1982
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6
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1
4
1
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4
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6
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1
1
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437690
Aketagawa
-
Ferredoxin-sulfite reductase f ...
Spinacia oleracea
Agric. Biol. Chem.
44
2371-2378
1980
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4
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437696
Hall
EPR spectroscopy of the iron-s ...
Desulfovibrio gigas, Desulfovibrio gigas No. 9332
Biochim. Biophys. Acta
581
27-33
1979
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437697
Tamura
-
The occurrence of ferredoxin-s ...
Hordeum vulgare
Agric. Biol. Chem.
43
1601-1602
1979
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437698
Tamura
-
Ferredoxin-dependent sulfite r ...
Spinacia oleracea
Agric. Biol. Chem.
42
2165-2167
1978
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437699
Asada
-
Methyl viologen- and ferredoxi ...
Spinacia oleracea
Methods Enzymol.
17B
528-539
1971
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1
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1
1
1
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1
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437700
Laishley
A ferredoxin-linked sulfite re ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Can. J. Microbiol.
17
889-895
1971
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9
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6
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