Information on EC 1.3.5.1 - succinate dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P0AC41

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?

fumarate + 2,3-dimethyl-1,4-naphthohydroquinone

succinate + 2,3-dimethyl-1,4-naphthoquinone

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mutation of His-82 to Arg in fumarate reductase subunit C prevents oxidation of 2,3-dimethyl-1,4-naphthohydroquinone

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r

fumarate + electron donor

succinate + oxidized donor

4 entries

fumarate + menaquinol

succinate + menaquinone

fumarate + menaquinol-6

succinate + menaquinone-6

-

-

r

fumarate + quinol

succinate + ubiquinone

fumarate + reduced benzyl viologen

succinate + benzyl viologen

-

-

r

fumarate + reduced plumbagin

succinate + oxidized plumbagin

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-

?

succinate + 2,3-dimethoxy-5-methyl-1,4-benzoquinone

fumarate + 2,3-dimethoxy-5-methyl-1,4-benzohydroquinone

-

-

?

succinate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone

fumarate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol

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-

r

succinate + 2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide

?

-

i.e. MTT, in presence of phenazine methosulfate, i.e. PMS

-

?

succinate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone

fumarate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol

-

the succinate dehydrogenase C subunit is responsible for ubiquinone binding

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?

succinate + a quinone

fumarate + a quinol

-

-

?

succinate + acceptor

fumarate + reduced acceptor

succinate + electron acceptor

fumarate + reduced acceptor

succinate + ferricyanide

fumarate + ferrocyanide

succinate + menaquinone

fumarate + menaquinol

succinate + oxidized 2,6-dichlorophenolindophenol

fumarate + reduced 2,6-dichloroindophenol

-

in the presence of the artificial electron acceptor phenazine methosulfate and the ubiquinone analogue UQ1

698946

-

?

succinate + oxidized phenazine ethosulfate

fumarate + reduced phenazine ethosulfate

-

-

r

succinate + phenazine ethosulfate

fumarate + reduced phenazine ethosulfate

-

656003, 696480

-

?

succinate + phenazine methosulfate

fumarate + reduced phenazine methosulfate

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-

?

succinate + ubiquinone

fumarate + ubiquinol

13 entries

succinate + ubiquinone-2

fumarate + ubiquinol

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-

r

succinate + ubiquinone-8

fumarate + ubiquinol-8

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-

r

ubiquinone-1 + L-malate

?

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-

?

ubiquinone-1 + succinate

ubiquinol-1 + fumarate

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-

?

additional information

?

-

10 entries

succinate + a quinone

fumarate + a quinol

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-

?

fumarate + menaquinol

succinate + menaquinone

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fumarate reductase acts as part of an anaerobic respiratory chain

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r

succinate + a quinone

fumarate + a quinol

-

-

?

succinate + acceptor

fumarate + reduced acceptor

-

656090

-

?

succinate + electron acceptor

fumarate + reduced acceptor

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active in aerobic respiration, repressed during anaerobic respiration

391154

-

?

succinate + menaquinone

fumarate + menaquinol

succinate + ubiquinone

fumarate + ubiquinol

additional information

?

-

-

succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals

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?

FAD

Fe-S cluster

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2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone

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benzyl viologen

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cytochrome b

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FAD

10 entries

Fe-S center

P00363; P0AC47; P0A8Q0; P0A8Q3

iron-sulfur protein FrdB

763400

flavin

-

quantitative determination of content in wild-type and mutant enzymes

flavin adenine dinucleotide

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heme

heme b

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the quinone binding site of succinate dehydrogenase is required for electron transfer to the heme b

674678

heme b556

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ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer

iron-sulfur centre

menaquinol-6

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phenazine methosulfate

-

Plumbagin

-

a quinone analogue

quinone

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with a periplasmically oriented quinone binding site of the enzyme

[3Fe-4S]-center

located in subunit FrdC

additional information

13 entries

-

Fe2+

within three Fe-S clusters

anions

Fe

Fe-S-clusters

Fe2+

-

heme cofactor and [3Fe-4S] cluster, midpoint potentials of wild-type and mutant enzymes, overview

Iron

2-(n-heptyl)-4-hydroxy-quinoline N-oxide

2-alkyl-4,6-dinitrophenol-17

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2-alkyl-4,6-dinitrophenol-20

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2-alkyl-4,6-dinitrophenols

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derivatives of 2-alkyl-4,6-dinitrophenols, competitive inhibitors of both succinate dehydrogenase and fumarate reductase

2-heptyl-4-hydroxyquinoline N-oxide

inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies

2-mercaptoethanol

-

391172

2-n-heptyl-4-hydroxyquinoline-N-oxide

2-Thenoyltrifluoroacetone

2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol

inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies

3'-bromo-carboxin

-

not inhibitory

3'-fluoro-carboxin

-

not inhibitory

3'-n-butyl-carboxin

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not inhibitory

5,5'-dithiobis(2-nitrobenzoate)

-

391170

5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide

i.e., carboxin

atpenin 5A

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carboxin

Chaotropic reagents

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e.g. perchlorate, thiocyanate

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iodoacetamide

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malonate

menaquinone-1

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competitive inhibitor of the succinate oxidation reaction of succinate dehydrogenase

N-ethylmaleimide

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oxaloacetate

p-chloromercuribenzoate

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Pentachlorophenol

siccanin

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ubiquinol-2

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competitive inhibitor of the fumarate reduction reaction of fumarate reductase

additional information

-

residual activity: above 77%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site

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ATP

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diphosphate

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activation

dithiothreitol

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required for activity

Na2SO4

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activation

NaN3

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activation

Sodium citrate

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activation

0.003

2,3-dimethoxy-5-methyl-1,4-benzoquinone

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value below

0.3

ferricyanide

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391154

0.005 - 0.7

fumarate

0.0009 - 0.0054

menaquinol

0.0018 - 0.004

menaquinone

0.11 - 0.19

reduced plumbagin

0.0015 - 0.55

succinate

0.0005 - 0.2

ubiquinone

24 entries

0.0089 - 0.0114

ubiquinone-2

additional information

fumarate

35 - 182

2,3-dimethoxy-5-methyl-1,4-benzoquinone

9.4 - 29.6

2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide

20.1 - 30.4

ferricyanide

0.3 - 250

fumarate

2.8 - 222.2

menaquinol

16 entries

82

oxidized phenazine ethosulfate

-

30°C, pH 7.8

-

7.7 - 23

reduced plumbagin

0.1 - 217

succinate

16 entries

1.7 - 37.9

ubiquinone

17 entries

additional information

fumarate

97 - 232

fumarate

11 - 54

succinate

0.000075 - 0.0002

2-(n-heptyl)-4-hydroxy-quinoline N-oxide

0.0013 - 0.017

2-alkyl-4,6-dinitrophenol-17

0.0015 - 0.019

2-alkyl-4,6-dinitrophenol-20

0.00003 - 0.0002

2-n-heptyl-4-hydroxyquinoline-N-oxide

6 entries

0.03 - 0.035

carboxin

0.005 - 0.025

malonate

0.012

menaquinone-1

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succinate dehydrogenase, succinate oxidation reaction

0.00006 - 0.0003

oxaloacetate

0.013 - 0.083

Pentachlorophenol

0.015

ubiquinol-2

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fumarate reductase, fumarate reduction reaction

additional information

5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide

0.21

siccanin

Escherichia coli

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16

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264

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509

-

additional information

4 entries

6.6 - 6.8

7.4

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assay at

7.4 - 7.8

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for both succinate dehydrogenase and fumarate reductase

7.8

assay at

8

additional information

25

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assay at

685281, 698668

30

38

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assay at

additional information

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aerobic growth on succinate and anaerobic growth on glycerol-fumarate

membrane-associated enzyme complex

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391115, 391169, 391170

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succinate-quinone oxidoreductase is solubilized and purified from Escherichia coli inner membranes

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metabolism

succinate:quinone oxidoreductase (SQR) functions in energy metabolism, coupling the tricarboxylic acid cycle and electron transport chain in bacteria and mitochondria. The biogenesis of flavinylated SdhA, the catalytic subunit of SQR, is assisted by a highly conserved assembly factor termed SdhE in bacteria via an unknown mechanism. Bacterial SdhE proteins, and their mitochondrial homologues, seem to be assembly chaperones that constrain the conformation of SdhA to facilitate efficient flavinylation while regulating succinate dehydrogenase activity for productive biogenesis of SQR

physiological function

succinate:quinone oxidoreductase (SQR) is a multisubunit membrane-associated enzyme found in the cytoplasm of bacteria and in the matrix of mitochondria (where it is commonly termed complex II). The enzyme is central to cellular metabolism and energy conversion, contributing to the tricarboxylic acid cycle and the electron transport chain. It catalyzes the oxidation of succinate to fumarate, which is coupled to electron transfer through flavin adenine dinucleotide (FAD) and three Fe-S clusters, resulting in the reduction of the electron carrier ubiquinone to ubiquinol. Succinate:quinone oxidoreductase (SQR) functions in energy metabolism, coupling the tricarboxylic acid cycle and electron transport chain in bacteria and mitochondria

evolution

metabolism

succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP

physiological function

additional information

120000

3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis

360000

trimer

100000

120000

-

13000

15000

26000

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succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE

391107

27000

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fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase

28000

-

1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE

64000

-

1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE

69000

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fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase

71000

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succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE

391107

trimer

3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis

dimer

tetramer

6 entries

additional information

additional information

posttranslational modifications regulate SDH levels by 4 means: phosphorylation, deacetylation, succinylation and propionylation

purified SdhA in complex with SdhE, hanging-drop vapor diffusion, mixing of 0.001 ml of 6.3 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 300 mM NaCl with 0.001 ml of crystallization solution containing 0.1 M HEPES, pH 7.5, 0.2 M MgCl2 hexahydrate, 30% w/v PEG 3350, and 40 mM NaF, at 20°C, X-ray diffraction structure determination and analysis at 2.15 A resolution

structure of SQR is reported at 2.6 A resolution. The SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of reactive oxygen species

by the hanging-drop vapour-diffusion technique

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crystal structure of QFR to 3.3 A resolution. Enzyme contains two quinone species, presumably menaquinol, bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed QP and QD, indicating their positions proximal, QP, or distal, QD, to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. Co-crystallization studies of the Escherichia coli QFR with the quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH2 at the QP site. In the structures with the inhibitor bound at QP, no density is observed at QD. The conserved acidic residue, Glu29 in subunit FrdC, in the Escherichia coli enzyme may act as a proton shuttle from the quinol during enzyme turnover

crystallization conditions are screened for succinate-quinone oxidoreductase that is solubilized and purified using 2.5% (w/v) sucrose monolaurate and 0.5% (w/v) Lubrol PX, respectively, and two different crystal forms are obtained in the presence of detergent mixtures composed of n-alkyl-oligoethylene glycol monoether and n-alkyl-maltoside. Crystallization takes place before detergent phase separation occurrs and the type of detergent mixture affects the crystal form

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fumarate reductase, determined at 3.3 A, belongs to the type D enzymes: contains two hydrophobic subunits and no heme group

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391139

hanging drop vapor diffusion method, x-ray structure of mutant E49Q

hanging-drop vapour-diffusion method, the enzyme is cocrystallized with the ubiquinone binding-site inhibitor Atpenin A5 (AA5) to confirm the binding position of the inhibitor and reveal additional structural details of the Q-site

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674762

hanging-drop vapour-diffusion, SQR in 20 mM Tris-HCl, pH 7.6, 0.05% THESIT is mixed with an equal volume of reservoir solution containing 100 mM Na-HEPES, pH 7.5, 200 mM, CaCl2 and 28% polyethylene glycol 400, crystals diffract to 2.6 A resolution

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PDB code: 1FUM, structure of the QFR monomer, with the covalently bound FAD cofactor, showing the iron-sulfur clusters [4Fe-4S], [3Fe-3S], and [2Fe-2S] and the two menaquinone molecules

purified enzyme QFR alone r with bound FLiG in two crystal forms, one grown from the lipidic cubic phase and one grown from dodecyl maltoside micelles, the first exhibiting crystal packing similar to previous crystal forms, while the latter displays a unique crystal packing providing the view of the QFR active site without a dicarboxylate ligand. For LCP crystallization 25 mg/ml protein (QFR or QFR-FliG) is mixed in a 40:60 ratio with 1-(9Z-octadecenoyl)-rac-glycerol (9.9 MAG), crystals are grown using 50 nl mesophase and 800 nl precipitant containing 200 mM NH4F, 100 mM Bis-Tris pH 7.5, 22% PEG 400, and 5% pentaerythritol propoxylate, crystals of QFR grow using the same conditions as crystals of QFR-FliG, with the crystals from the QFR-FliG mixture being better suited to diffraction analysis. For micellar crystallization of QFR-FliG in 20 mM Tris pH 7.4, 0.02% DDM, sitting drop vapor diffusion method is used, mixing of with 200 nl of 25 mg/ml protein and 200 nl of reservoir solution, containing 10-20% PEG 400-900, 15-50 mM divalent cation (CaCl2, Ca(CH3COO)2, or MgCl2), and 50 mM Bis-Tris, pH 6.5, X-ray diffraction structure determination and analysis at 7.5 and 3.35 A resolution, respectively

P00363; P0AC47; P0A8Q0; P0A8Q3

763400

purified FrdA mutant E245Q, hanging-drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 25 mM Tris-HCl, pH 7.4, 1 mM EDTA, 0.02% C12E9, with 0.001 ml of reservoir solution containing 275mM sodium malonate, 19% PEG 6000, 100 mM sodium citrate, pH 4.0, 1 mM EDTA, and 0.001% dithiothreitol, and equilibration against 1 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 4.25 A resolution

structure of SQR at 2.6 A resolution

structure of subunits, binding sites, structure of complex II, pathway of electron transfer

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391149

subunit FrdC mutant E29L, to 2.95 A resolution. The sequential removal of the two menaquinol protons may be accompanied by a rotation of the naphthoquinone ring to optimize the interaction with a second proton shuttling pathway

three new structures of Escherichia coli succinate-quinone oxidoreductase are solved. One with the specific quinone-binding site (Q-site) inhibitor carboxin present is solved at 2.4 A resolution and reveals how carboxin inhibits the Q-site. The other new structures are with the Q-site inhibitor pentachlorophenol and with an empty Q-site. Comparison of the new succinate-quinone oxidoreductase structures shows how subtle rearrangements of the quinone-binding site accommodate the different inhibitors. The position of conserved water molecules near the quinone binding pocket leads to a reassessment of possible water-mediated proton uptake networks that complete reduction of ubiquinone

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698946

C247

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mutation in flavoprotein subunit FrdA. Increase in fumarate reduction rate, slight increase in succinate oxidation. Residue C247 of FrdA is responsible for the N-ethylmaleimide sensitivity shown by fumarate reductase but is not required for catalytic activity or the tight-binding of oxalacetate

D288N

site-directed mutagenesis, the FrdAD288N variant shows minimal residual fluorescence, suggesting covalent flavinylation is severely compromised

D95E

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site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme

D95L

-

site-directed mutagenesis of subunit C, the mutant shows a shifted pH-optimum but similar activity compared to the wild-type enzyme

E101D

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site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme

E101L

-

site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme

E245Q

site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation. Mutant crystal structure analysis, overview

E29F

E29L

E49A

decrease in catalytic efficiency of both fumarate reduction and succinate oxidation

E49Q

decrease in catalytic efficiency of both fumarate reduction and succinate oxidation

F20L

-

growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Phe-20 is not involved in the Q binding

G227L

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site-directed mutagenesis of subunit B, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme

G227L/D95E

-

site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0

G227L/D95L

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site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0

H232S

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mutation in flavoprotein subunit FrdA. Decrease in fumarate reduction, strong decrease in succinate oxidation. Residue H232 is the general acid-base catalyst

H30A

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growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, His-30 is not involved in the Q binding

H355S

site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation

H44C

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the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 38% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex

H44R

-

the mutation does not allow cells to grow anaerobically on glycerol and fumarate, the substitution produces an inactive complex

H44S

-

the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 32% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex

H44Y

-

the mutation allows cell growth in glycerol/fumarate medium at a 7fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 17% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex

H71C

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role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Mutant H71C results in a protein that retains penta-coordinated heme b indicating that Cys is not able to provide coordination for the heme in Escherichia coli SQR even in its optimal structural position. Km (ubiquinone): 0.012 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. Mutant H71C retains 43% of ubiquinone reductase activity compared to wild-type SQR, quinone reductase activity is impaired to a greater extent than its succinate-oxidase activity measured with phenazine ethosulfate

H71L

-

mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme

671813

H71Q

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mutation in SdhC subunit, 82% and 69% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively

H71Y

-

mutant lacks heme. Km (ubiquinone): 0.01 mM compared to 0.0025 mM wild-type, lower ubiquinone or phenazine ethosulfate reductase activity compared to mutant H71C or double mutant H71Y/A72C

H71Y/A72C

-

role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Double mutant assembles within the membrane but without heme, and it retains the ability to reduce quinone. Km (ubiquinone): 0.013 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. The Y71C72 double mutant shows significant improvement in its activity compared to H71Y or H71C

H82R

-

menaquinone, ubiquinone and b-type cytochrome levels are present in normal amounts, the mutation alters the electron transfer properties of the iron-sulfur and flavin redox centers of the catalytic domain, functional electron flow from 2,3-dimethyl-1,4-naphthoquinone or from the electron transport chain is impaired, the mutant can be reduced normally by single-electron donors such as benzyl viologen

H84L

-

mutation in SdhC subunit, 54% and 23% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively

H91L

-

mutant enzyme produces more superoxide than the wild-type enzyme

671813

I150E

-

mutation lowers the midpoint potential of the [4Fe-4S] cluster

I150H

-

mutation lowers the midpoint potential of the [4Fe-4S] cluster

I28E

-

mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme

K228L

K228R

L220S

-

mutation does not alter the redox behavior of the [4Fe-4S] cluster but instead lowers the midpoint potential of the [3Fe-4S] cluster

Q78L

-

site-directed mutagenesis of subunit D, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme

R19A

-

growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Arg-19 is not involved in the Q binding

R248H

-

mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation

R248L

-

mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation

R287K

site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation

R28E/E29I

mutation in subunit FrdC, retains normal level of activity

R28L

mutation in subunit FrdC, retains normal level of activity

R28L/E9L

mutation in subunit FrdC, retains normal level of activity

R28L/R81A

mutation in subunits FrdC/FrdD, loss of activtiy with ubiquinone and menaquinol

R28N

mutation in subunit FrdC, retains normal level of activity

R31A

-

the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Arg-31 is a critical residue for succinate-Q-reductase

R31H

-

the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity

R31K

-

the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity, it occupies a much larger space than the primary amine of lysine, extends a longer distance, and may provide more chance for hydrogen bond formation, it may stabilize Q binding through pi-pi interactions between the guanidino group and the benzoquinone ring

R390K

site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation

R390Q

site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation

R81A

mutation in subunit FrdD, retains normal level of activity

R81E

mutation in subunit FrdD, retains normal level of activity

R81K

mutation in subunit FrdD, retains normal level of activity

S27A

-

the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Ser-27 is a critical residue for succinate-Q-reductase, it participates in a hydrogen bond at the Q-binding site of the C subunit

S27C

-

the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding

S27T

-

the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding

S33A

-

the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 35% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase, the mutation of Ser-33 to alanine may greatly reduce enzyme turnover without affecting the affinity for Q

S33C

-

the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 44% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase

S33T

-

the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 88% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase

T17A

-

growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Thr-17 is not involved in the Q binding

T23A

-

the mutation yields cells capable of aerobic growth on M9/succinate medium at a rate slightly slower than that of complement strain, 40% decrease in the specific activity of the mutant to catalyze electron transfer from succinate to Q, apparent Km for Q2 is the same as that of complement reductase, Thr-23 may not be involved in Q binding

additional information

8.8

-

labile at alkaline pH

391110

9

-

20 min, 50% loss of activity

391083

45

anions required for optimal stability

-

dithiothreitol required for optimal stability

-

dithiothreitol stabilizes during storage

-

-20°C

-

-20°C in crude extract, soluble enzyme, 24 h, 50% loss of activity, membrane bound form no loss of activity

-

-70°C

-

-70°C, 0.2 mM dithiothreitol, 1 month

-

391172

recombinant non-tagged SdhA complxed with His6-tagged SdhE from Escherichia coli by nickel affinity chromatography and gel filtration to homogeneity, elution as a heterodimer with FAD covalently bound (to SdhA) within the binary complex

-

from EC 1.3.5.1

-

of both succinate dehydrogenase and fumarate reductase using solubilization with Thesit and DEAE fast-flow chromatography

-

recombinant SQR

-

recombinant SQR, Q-Sepharose, Poros 50HQ, Sephacryl S-300

-

recombinant wild-type and mutant enzymes partially from strain DW35 by membrane preparation

-

soluble recombinant enzyme mutant E245Q from Escherichia coli strain DW35 by anion exchange chromatography, ultrafitration, a second different step of anion exchange chromatography, followed by gel filtration

succinate-quinone oxidoreductase is solubilized and purified using detergents 2.5% (w/v) sucrose monolaurate and 0.5% (w/v) Lubrol PX

-

using solubilization with polyoxyethylene-9-lauryl ether and column chromatography on DEAE-Sepharose CL-6B

-

using treatment with detergent Thesit and chromatography on DEAE-Sepharose FF column, Poros 50HQ column and Sephacryl S-300 gel filtration column

-

gene sdhA from Escherichia coli strain MC4100, recombinant expression of non-tagged SdhA in Escherichia coli strain BL21(DE3) CodonPlus-RIL, coexpression with His6-tagged SdhE

-

cell membranes transformed with plasmid which codes for all four subunits of the fumarate reductase complex

-

391095

cloning of a mutant fumarate reductase operon

-

expressed in Escherichia coli K12 strain

-

expressed in Escherichia coli strain DW35

-

expression in Escherichia coli

-

expression of wild-type and mutant enzymes in strain DW35

-

gene cluster frdABCD encoding 4 subunits, DNA and amino acid sequence analysis, overepression

gene cluster sdhCDAB encoding 4 subunits, DNA and amino acid sequence analysis, overepression

operon FrdABCD, recombinant expression of wild-type and mutant FrdAs in Escherichia coli strain DW35, in which both the frd and sdh operons are disrupted via the insertion of a kanamycin gene

overview succinate dehydrogenase and fumarate reductase

-

391099

transformed strain DW35 used for expression of membrane-bound enzyme

-

fnr and arcA gene products both act to repress SDHC expression in response to oxygen. The EIICBGlc protein (the ptsG gene product) is a crucial mediator of the repression of the sdhCDAB operon in the presence of glucose. It acts via the transcription factor crp, which directly regulates expression of the sdhCDAB operon. The glucose repression of this operon occurs in a cAMP-dependent manner

the QFR complex provides electron transport during anaerobic cell growth conditions. The transcription of the frdABCD operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the succinate-ubiquinone oxidase, EC 1.3.5.1, overview

the SQR complex provides electron transport during aerobic cell growth conditions. The transcription of the sdhCDAB operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the menaquinol-fumarate oxidoreductase, EC 1.3.5.4, overview

the isolated enzyme is resolved into a reconstitutively active, two-subunit succinate dehydrogenase and a two-subunit membrane anchoring protein fraction by alkaline treatment in the presence of urea followed by DEAE-Sepharose CL-6B column chromatography, maximum reconstitution is obtained when the weight ratio of succinate dehydrogenase to the two-subunit membrane anchoring protein reaches 5.26

-

medicine

-

species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics

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Fumarate reductase of Escherichia coli

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391157

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