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Ligand menaquinone

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

heme metabolism, propionate fermentation

KEGG

Biosynthesis of cofactors, Biosynthesis of secondary metabolites, Two-component system, Ubiquinone and other terpenoid-quinone biosynthesis, Vitamin digestion and absorption

MetaCyc

(S)-lactate fermentation to propanoate, acetate and hydrogen, 3,8-divinyl-chlorophyllide a biosynthesis II (anaerobic), 7,8-dimethylmenaquinone biosynthesis, 8-methylmenaquinone biosynthesis, dissimilatory sulfate reduction I (to hydrogen sufide)), formate to dimethyl sulfoxide electron transfer, formate to nitrite electron transfer, formate to trimethylamine N-oxide electron transfer, glycerol-3-phosphate to fumarate electron transfer, glycerol-3-phosphate to hydrogen peroxide electron transport, heme b biosynthesis II (oxygen-independent), hydrogen to dimethyl sulfoxide electron transfer, hydrogen to fumarate electron transfer, hydrogen to trimethylamine N-oxide electron transfer, incomplete reductive TCA cycle, mixed acid fermentation, NADH to dimethyl sulfoxide electron transfer, NADH to fumarate electron transfer, NADH to hydrogen peroxide electron transfer, NADH to trimethylamine N-oxide electron transfer, nitrate reduction III (dissimilatory), nitrate reduction IX (dissimilatory), nitrate reduction VII (denitrification), nitrate reduction VIII (dissimilatory), pyruvate fermentation to propanoate I, reductive TCA cycle I, reductive TCA cycle II, sulfite oxidation II, sulfite oxidation III, sulfite oxidation V (SoeABC), TCA cycle VI (Helicobacter), thiosulfate disproportionation III (quinone) more

Show all BRENDA pathways known for menaquinone

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Natural Substrate (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.4

menaquinone + reduced coenzyme F420 = menaquinol + oxidized coenzyme F420

722170, 722162

-

1.17.5.3

formate + menaquinone = ?

390364

-

1.17.5.3

formate + menaquinone = CO2 + menaquinol

677117

-

1.3.5.1

succinate + a menaquinone = fumarate + a menaquinol

391149

-

1.3.5.1

succinate + menaquinone = fumarate + menaquinol

726316, 763250, 763727, 763400

-

1.17.5.3

2 entries

1.3.5.1

2 entries

1.3.5.3

protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol

726366

-

1.8.5.3

dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol

742743

-

1.8.5.9

a [DsbA protein] with reduced L-cysteine residues + menaquinone = a [DsbA protein] carrying a disulfide bond + menaquinol

757693

-

1.8.5.9

[DsbA protein] with reduced L-cysteine residues + menaquinone = [DsbA protein] carrying a disulfide bond + menaquinol

757516, 758211

-

1.8.5.9

2 entries

4.1.1.90

peptidyl-L-glutamate + CO2 + O2 + menaquinone = ?

695615

-

7.1.1.12

succinate + menaquinone + 2 H+[side 1] = fumarate + menaquinol + 2 H+[side 2]

764191, 763727, 764131, 764193

-

7.1.1.2

NADH + H+ + menaquinone = NAD+ + menaquinol

700003

-

In Vivo Product in Enzyme-catalyzed Reactions (7 results)

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Show Natural Product (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.5.1

fumarate + a menaquinol = succinate + a menaquinone

0

-

1.3.5.1

fumarate + menaquinol = succinate + menaquinone

0, 391089, 391090

-

1.3.5.1

2 entries

1.7.5.2

NO + menaquinol = N2O + H2O + menaquinone

0

-

1.8.5.3

dimethylsulfoxide + menaquinol = dimethylsulfide + menaquinone + H2O

0

-

7.1.1.12

fumarate + menaquinol + 2 H+[side 2] = succinate + menaquinone + 2 H+[side 1]

0

-

7.1.1.3

menaquinol + O2 + H+[side 1] = menaquinone + H2O + H+[side 2]

0

-

7.1.1.5

menaquinol + O2 = menaquinone + H2O

0

-

Substrate in Enzyme-catalyzed Reactions (21 results)

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Show Substrate (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.4

menaquinone + reduced coenzyme F420 = menaquinol + oxidized coenzyme F420

722170, 722162

-

1.12.5.1

H2 + menaquinone = menaquinol

676044

-

1.17.5.3

formate + menaquinone = ?

390364

-

1.17.5.3

formate + menaquinone = CO2 + menaquinol

677117

-

1.17.5.3

2 entries

1.2.5.1

pyruvate + menaquinone + H2O = acetate + CO2 + menaquinol

740357

-

1.3.5.1

succinate + a menaquinone = fumarate + a menaquinol

391149

-

1.3.5.1

succinate + menaquinone = fumarate + menaquinol

726316, 674634, 707470, 707545, 763250, 674532, 763727, 763400

-

1.3.5.1

2 entries

1.3.5.3

protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol

726366

-

1.5.5.3

trans-4-hydroxy-L-proline + menaquinone = (3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + menaquinol

741855

-

1.6.5.9

NADH + H+ + menaquinone = NAD+ + menaquinol

392679

-

1.7.5.1

nitrite + menaquinone + H2O = nitrate + menaquinol

741971

-

1.8.5.3

dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol

742743

-

1.8.5.5

sulfite + hydrogen sulfide + menaquinone = thiosulfate + menaquinol

725273

-

1.8.5.9

a [DsbA protein] with reduced L-cysteine residues + menaquinone = a [DsbA protein] carrying a disulfide bond + menaquinol

757136, 757693

-

1.8.5.9

[DsbA protein] with reduced L-cysteine residues + menaquinone = [DsbA protein] carrying a disulfide bond + menaquinol

757516, 758211

-

1.8.5.9

2 entries

4.1.1.90

peptidyl-L-glutamate + CO2 + O2 + menaquinone = ?

695615

-

7.1.1.12

succinate + menaquinone + 2 H+[side 1] = fumarate + menaquinol + 2 H+[side 2]

764191, 763727, 764131, 764193

-

7.1.1.2

NADH + H+ + menaquinone = NAD+ + menaquinol

731312, 700003

-

7.1.1.2

NADH + menaquinone + H+ = NAD+ + menaquinol

657643

-

7.1.1.2

NADH + menaquinone = NAD+ + menaquinol

674533

-

7.1.1.2

3 entries

7.2.1.1

NADH + menaquinone = NAD+ + reduced menaquinone

671351

-

Product in Enzyme-catalyzed Reactions (16 results)

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Show Product (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.18.3

propylene + menaquinol + O2 = propylene oxide + menaquinone + H2O

0

-

1.3.5.1

fumarate + a menaquinol = succinate + a menaquinone

0

-

1.3.5.1

fumarate + menaquinol = succinate + menaquinone

0, 391089, 391090

-

1.3.5.1

2 entries

1.7.2.5

NO + menaquinol = N2O + H2O + menaquinone

0

-

1.7.5.1

nitrate + menaquinol = nitrite + menaquinone + H2O

0

-

1.7.5.2

nitric oxide + menaquinol = nitrous oxide + menaquinone + H2O

0

-

1.7.5.2

NO + menaquinol = N2O + H2O + menaquinone

0

-

1.8.5.3

dimethylsulfoxide + menaquinol = dimethylsulfide + menaquinone + H2O

0

-

1.8.5.3

DL-methionine sulfoxide + menaquinol = DL-methionine sulfide + menaquinone + H2O

0

-

1.8.5.3

S-biotin sulfoxide + menaquinol = S-biotin sulfide + menaquinone + H2O

0

-

1.8.5.3

trimethylamine-N-oxide + menaquinol = ? + menaquinone + H2O

0

-

1.7.5.2

2 entries

1.8.5.3

4 entries

1.8.5.5

thiosulfate + menaquinol = sulfite + hydrogen sulfide + menaquinone

0

-

7.1.1.12

fumarate + menaquinol + 2 H+[side 2] = succinate + menaquinone + 2 H+[side 1]

0

-

7.1.1.3

menaquinol + O2 + H+[side 1] = menaquinone + H2O + H+[side 2]

0

-

7.1.1.5

menaquinol + O2 = menaquinone + H2O

0

-

7.1.1.8

menaquinol + 2 ferricytochrome c = menaquinone + 2 ferrocytochrome c + 2 H+

0

-

Enzyme Cofactor/Cosubstrate (8 results)

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Show Cofactor (8 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.5.4

-

722575

-

1.17.5.3

the structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 A through the enzyme. In the catalytic site, the Mo directly takes up electrons from the bound substrate. These electrons are transferred to the beta subunit through the [4Fe4S] cluster (FeS-0) in the alpha subunit. The four [4Fe-4S] clusters in the beta subunit, which are aligned in the order of FeS-1, FeS-4, FeS-2, and FeS-3, connect the alpha and gamma subunits like an electric wire. From FeS-3 of the beta subunit, electrons are transferred to heme bP (P for periplasm) in the gamma subunit and then across the membrane to heme bC (C for cytoplasm). Menaquinone binds to a histidine ligand (Hisg169) of heme bC and can directly accept electrons through this residue

677117

-

1.17.9.1

active in 4-hydroxybenzyl alcohol oxidation

674335

-

1.21.99.5

membrane-bound menaquinone

349702

-

1.3.5.1

one menaquinone molecule is bound near heme bL in the hydrophobic subunit C

763727

-

1.7.2.7

predominant menaquinone is MK-7

742381

-

1.7.5.1

there are more than one menaquinol binding sites in NarGHI

696201

-

1.8.5.3

-

763950

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.12.99.6

-

742788

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.5.1

-

394971

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.5.5.3

0.28

-

at pH 7.5 and 25°C

741855

7.1.1.2

423

-

pH 7.0, temperature not specified in the publication

731312

K_M Value (6 results)

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Show KM Value (6 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.5.1

0.0018

-

mutant E29L, pH 7.0, 30°C

674634

1.3.5.1

0.004

-

wild-type, pH 7.0, 30°C

674634

1.3.5.1

2 entries

1.3.5.3

0.0173

-

recombinant His-tagged enzyme, pH and temperature not specified in the publication

726366

1.5.5.3

0.025

-

at pH 7.5 and 25°C

741855

7.1.1.2

0.1

-

-

657643

7.1.1.2

0.1

-

pH 7.0, temperature not specified in the publication

731312

7.1.1.2

2 entries

References & Links

Literature References (44)

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Show Reference (44 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

349702

8636034

The proton/electron ratio of the menaquinone-dependent electron transport from dihydrogen to tetrachloroethene in "Dehalobacter restrictus"

1996

Schumacher, W.; Holliger, C.

J. Bacteriol.

178

2328-2333

390364

6639943

Low-potential cytochrome b as an essential electron-transport component of menaquinone reduction by formate in Vibrio succinogenes

1983

Unden, G.; Kroeger, A.

Biochim. Biophys. Acta

725

325-331

391089

3609021

Cloning and expression of the genes of two fumarate reductase subunits from Wolinella succinogenes

1987

Lauterbach, F.; Körtner, C.; Tripier, D.; Unden, G.

Eur. J. Biochem.

166

447-452

391090

2388563

Wolinella succinogenes fumarate reductase contains a dihaem cytochrome b

1990

Körtner, C.; Lauterbach, F.; Tripier, D.; Unden, G.; Kröger, A.

Mol. Microbiol.

4

855-860

391149

11004459

Succinate:quinone oxidoreductases: new insights from x-ray crystal structures

2000

Lancaster, C.R.D.; Kroger, A.

Biochim. Biophys. Acta

1459

422-431

392679

3138118

Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae

1988

De Vries, S.; Grivell, L.A.

Eur. J. Biochem.

176

377-384

394971

6102989

Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B

1980

Olsiewski, P.J.; Kaczorowski, G.J.; Walsh, C.

J. Biol. Chem.

255

4487-4494

657643

11811946

Evidence that a type-2 NADH:quinone oxidoreductase mediates electron transfer to particulate methane monooxygenase in Methylococcus capsulatus

2002

Cook, S.A.; Shiemke, A.K.

Arch. Biochem. Biophys.

398

32-40

671351

16756485

Energy converting NADH:quinone oxidoreductase (complex I)

2006

Brandt, U.

Annu. Rev. Biochem.

75

69-92

674335

17449613

Genes, enzymes, and regulation of para-cresol metabolism in Geobacter metallireducens

2007

Peters, F.; Heintz, D.; Johannes, J.; van Dorsselaer, A.; Boll, M.

J. Bacteriol.

189

4729-4738

674532

16484232

Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain

2006

Maklashina, E.; Iverson, T.M.; Sher, Y.; Kotlyar, V.; Andrell, J.; Mirza, O.; Hudson, J.M.; Armstrong, F.A.; Rothery, R.A.; Weiner, J.H.; Cecchini, G.

J. Biol. Chem.

281

11357-11365

674533

16469750

Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis type-II NADH-menaquinone oxidoreductase (NDH-2)

2006

Yano, T.; Li, L.S.; Weinstein, E.; Teh, J.S.; Rubin, H.

J. Biol. Chem.

281

11456-11463

674634

16829675

Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli

2006

Maklashina, E.; Hellwig, P.; Rothery, R.A.; Kotlyar, V.; Sher, Y.; Weiner, J.H.; Cecchini, G.

J. Biol. Chem.

281

26655-26664

676044

9822828

Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2

1998

Gross, R.; Simon, J.; Lancaster, R.D.; Kröger, A.

Mol. Microbiol.

30

639-646

677117

11884747

Molecular basis of proton motive force generation: structure of formate dehydrogenase-N

2002

Jormakka, M.; Toernroth, S.; Byrne, B.; Iwata, S.

Science

295

1863-1868

695615

3896125

Vitamin K-dependent carboxylase

1985

Suttie, J.W.

Annu. Rev. Biochem.

54

459-477

696201

12731882

Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol

2003

Zhao, Z.; Rothery, R.A.; Weiner, J.H.

Biochemistry

42

5403-5413

700003

19348896

Type II NADH:quinone oxidoreductases of Plasmodium falciparum and Mycobacterium tuberculosis kinetic and high-throughput assays

2009

Fisher, N.; Warman, A.J.; Ward, S.A.; Biagini, G.A.

Methods Enzymol.

456

303-320

707470

17154542

Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate:menaquinone oxidoreductase from the Gram-positive bacterium Bacillus licheniformis

2006

Madej, M.G.; Nasiri, H.R.; Hilgendorff, N.S.; Schwalbe, H.; Unden, G.; Lancaster, C.R.

Biochemistry

45

15049-15055

707545

19103151

Purification, characterization and crystallization of menaquinol:fumarate oxidoreductase from the green filamentous photosynthetic bacterium Chloroflexus aurantiacus

2009

Xin, Y.; Lu, Y.K.; Fromme, R.; Fromme, P.; Blankenship, R.E.

Biochim. Biophys. Acta

1787

86-96

722162

8055920

F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters

1994

Kunow, J.; Linder, D.; Stetter, K.O.; Thauer, R.K.

Eur. J. Biochem.

223

503-511

722170

10971593

Structure of the F420H2:quinone oxidoreductase of Archaeoglobus fulgidus identification and overproduction of the F420H2-oxidizing subunit

2000

Brueggemann, H.; Falinski, F.; Deppenmeier, U.

Eur. J. Biochem.

267

5810-5814

722575

23143325

Purification and characterization of malate:quinone oxidoreductase from thermophilic Bacillus sp. PS3

2013

Kabashima, Y.; Sone, N.; Kusumoto, T.; Sakamoto, J.

J. Bioenerg. Biomembr.

45

131-136

725273

22081391

Thiosulfate reduction in Salmonella enterica is driven by the proton motive force

2012

Stoffels, L.; Krehenbrink, M.; Berks, B.C.; Unden, G.

J. Bacteriol.

194

475-485

726316

23308253

Atypical features of Thermus thermophilus succinate:quinone reductase

2013

Kolaj-Robin, O.; Noor, M.R.; OKane, S.R.; Baymann, F.; Soulimane, T.

PLoS ONE

8

e53559

726366

20484676

Heme biosynthesis is coupled to electron transport chains for energy generation

2010

Moebius, K.; Arias-Cartin, R.; Breckau, D.; Haennig, A.L.; Riedmann, K.; Biedendieck, R.; Schroeder, S.; Becher, D.; Magalon, A.; Moser, J.; Jahn, M.; Jahn, D.

Proc. Natl. Acad. Sci. USA

107

10436-10441

731312

24447297

Mycobacterium tuberculosis type II NADH-menaquinone oxidoreductase catalyzes electron transfer through a two-site ping-pong mechanism and has two quinone-binding sites

2014

Yano, T.; Rahimian, M.; Aneja, K.K.; Schechter, N.M.; Rubin, H.; Scott, C.P.

Biochemistry

53

1179-1190

740357

26734697

Oxygen as acceptor

2015

Borisov, V.B.; Verkhovsky, M.I.

EcoSal Plus

6

2

741855

25697095

Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria

2015

Summitt, C.B.; Johnson, L.C.; Joensson, T.J.; Parsonage, D.; Holmes, R.P.; Lowther, W.T.

Biochem. J.

466

273-281

741971

25976528

Demethylmenaquinol is a substrate of Escherichia coli nitrate reductase A (NarGHI) and forms a stable semiquinone intermediate at the NarGHI quinol oxidation site

2015

Rendon, J.; Pilet, E.; Fahs, Z.; Seduk, F.; Sylvi, L.; Hajj Chehade, M.; Pierrel, F.; Guigliarelli, B.; Magalon, A.; Grimaldi, S.

Biochim. Biophys. Acta

1847

739-747

742381

25367004

Physiological characterization of anaerobic ammonium oxidizing bacterium Candidatus Jettenia caeni

2015

Ali, M.; Oshiki, M.; Awata, T.; Isobe, K.; Kimura, Z.; Yoshikawa, H.; Hira, D.; Kindaichi, T.; Satoh, H.; Fujii, T.; Okabe, S.

Environ. Microbiol.

17

2172-2189

742743

24884723

Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on monooxo Mo(IV) and bisoxo Mo(VI) bis-dithiolenes insights into the mechanism of oxo transfer in sulfite oxidase and its relation to the mechanism of DMSO reductase

2014

Ha, Y.; Tenderholt, A.L.; Holm, R.H.; Hedman, B.; Hodgson, K.O.; Solomon, E.I.

J. Am. Chem. Soc.

136

9094-9105

742788

25368299

Physiology and bioenergetics of [NiFe]-hydrogenase 2-catalyzed H2-consuming and H2-producing reactions in Escherichia coli

2015

Pinske, C.; Jaroschinsky, M.; Linek, S.; Kelly, C.L.; Sargent, F.; Sawers, R.G.

J. Bacteriol.

197

296-306

757136

16027117

Reactivities of quinone-free DsbB from Escherichia coli

2005

Inaba, K.; Takahashi, Y.H.; Ito, K.

J. Biol. Chem.

280

33035-33044

757516

18421137

Protein disulfide bond generation in Escherichia coli DsbB-DsbA

2008

Inaba, K.

J. Synchrotron Radiat.

15

199-201

757693

11967064

Oxidative protein folding in bacteria

2002

Collet, J.; Bardwell, J.

Mol. Microbiol.

44

1-8

758211

16384917

Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB

2006

Inaba, K.; Takahashi, Y.; Ito, K.; Hayashi, S.

Proc. Natl. Acad. Sci. USA

103

287-292

763250

28615448

Structural and biochemical analyses reveal insights into covalent flavinylation of the Escherichia coli Complex II homolog quinol fumarate reductase

2017

Starbird, C.A.; Maklashina, E.; Sharma, P.; Qualls-Histed, S.; Cecchini, G.; Iverson, T.M.

J. Biol. Chem.

292

12921-12933

763400

29158068

New crystal forms of the integral membrane Escherichia coli quinol fumarate reductase suggest that ligands control domain movement

2018

Starbird, C.A.; Tomasiak, T.M.; Singh, P.K.; Yankovskaya, V.; Maklashina, E.; Eisenbach, M.; Cecchini, G.; Iverson, T.M.

J. Struct. Biol.

202

100-104

763727

30297797

Structural insights into the electron/proton transfer pathways in the quinol fumarate reductase from Desulfovibrio gigas

2018

Guan, H.H.; Hsieh, Y.C.; Lin, P.J.; Huang, Y.C.; Yoshimura, M.; Chen, L.Y.; Chen, S.K.; Chuankhayan, P.; Lin, C.C.; Chen, N.C.; Nakagawa, A.; Chan, S.I.; Chen, C.J.

Sci. Rep.

8

14935

763950

28687647

Deep-sea bacterium Shewanella piezotolerans WP3 has two dimethyl sulfoxide reductases in distinct subcellular locations

2017

Xiong, L.; Jian, H.; Xiao, X.

Appl. Environ. Microbiol.

83

e01262-17

764131

17154542

Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate menaquinone oxidoreductase from the Gram-positive bacterium Bacillus licheniformis

2006

Madej, M.; Nasiri, H.; Hilgendorff, N.; Schwalbe, H.; Unden, G.; Lancaster, C.

Biochemistry

45

15049-15055

764191

12409197

Wolinella succinogenes quinol fumarate reductase - 2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer

2002

Lancaster, C.

Biochim. Biophys. Acta

1565

215-231

764193

23466335

The di-heme family of respiratory complex II enzymes

2013

Lancaster, C.

Biochim. Biophys. Acta

1827

679-687

Links to other databases for menaquinone

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ChEBI

PubChem

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