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2 2,3-dimethyl-1,4-naphthoquinol + O2 + n H+[side 1]
2 2,3-dimethyl-1,4-naphthoquinone + 2 H2O + n H+[side 2]
2 demethylmenaquinol + O2 + n H+[side 1]
2 demethylmenaquinone + 2 H2O + n H+[side 2]
-
-
-
-
?
2,3-dimethylnaphthohydroquinone + O2 + H+[side 1]
?
-
-
-
-
?
dimethylnitrosamine + O2
?
duroquinol + O2
duroquinone + H2O
ferricytochrome c + O2
ferrocytochrome c + H2O
menadiol + O2 + n H+[side 1]
menadione + H2O + n H+[side 2]
menadione + O2 + H+[side 1]
?
-
-
-
-
?
menaquinol + O2
menaquinone + H2O
menaquinol-4 + O2 + H+[side 1]
menaquinone-4 + H2O + H+[side 2]
-
menaquinols are oxidized at 6-12fold higher rates than ubiquinols
-
-
?
thermoplasmaquinol + O2 + H+[side 1]
thermoplasmaquinone + H2O + H+[side 2]
-
likely candidate to the physiological electron donor
-
-
?
ubiquinol-1 + O2 + H+[side 1]
ubiquinone-1 + H2O + H+[side 2]
-
-
-
-
?
ubiquinol-10 + O2 + H+[side 1]
ubiquinone-10 + H2O + H+[side 2]
-
menaquinols are oxidized at 6-12fold higher rates than ubiquinols. However, because of the greater tendency for autoxidation of menaquinols, ubiquinol is a more convenient substrate for the enzyme assay
-
-
?
ubiquinol-6 + O2 + H+[side 1]
ubiquinone-6 + H2O + H+[side 2]
-
-
-
-
?
additional information
?
-
2 2,3-dimethyl-1,4-naphthoquinol + O2 + n H+[side 1]
2 2,3-dimethyl-1,4-naphthoquinone + 2 H2O + n H+[side 2]
-
-
-
-
?
2 2,3-dimethyl-1,4-naphthoquinol + O2 + n H+[side 1]
2 2,3-dimethyl-1,4-naphthoquinone + 2 H2O + n H+[side 2]
-
best substrate
-
-
?
2 2,3-dimethyl-1,4-naphthoquinol + O2 + n H+[side 1]
2 2,3-dimethyl-1,4-naphthoquinone + 2 H2O + n H+[side 2]
-
best substrate
-
-
?
dimethylnitrosamine + O2
?
-
-
-
-
?
dimethylnitrosamine + O2
?
-
-
-
-
?
duroquinol + O2
duroquinone + H2O
-
-
-
-
?
duroquinol + O2
duroquinone + H2O
-
-
-
-
?
ferricytochrome c + O2
ferrocytochrome c + H2O
-
low activity
-
-
?
ferricytochrome c + O2
ferrocytochrome c + H2O
-
low activity
-
-
?
menadiol + O2 + n H+[side 1]
menadione + H2O + n H+[side 2]
-
-
-
-
?
menadiol + O2 + n H+[side 1]
menadione + H2O + n H+[side 2]
-
-
-
-
?
menaquinol + O2
menaquinone + H2O
-
-
-
-
?
menaquinol + O2
menaquinone + H2O
-
cyt aa3-600 is strictly a menaquinol oxidase
-
-
?
menaquinol + O2
menaquinone + H2O
-
-
-
-
?
menaquinol + O2
menaquinone + H2O
-
-
-
-
?
menaquinol + O2
menaquinone + H2O
-
-
-
-
?
menaquinol + O2
menaquinone + H2O
-
-
-
-
?
additional information
?
-
-
cytochrome aa3-600 is a proton-pumping terminal oxidase
-
-
?
additional information
?
-
-
no activity with 1,4-naphthoquinol, N,N,N',N'-tetramethyl-1,4-phenylenediamine plus ascorbate or reduced cytochrome c
-
-
?
additional information
?
-
-
the enzyme does not oxidize 1,4-naphthoquinol, 2,3-dimethoxy-5-methyl-6-(n-nonyl)-1,4-benzoquinol, and 2,3-dimethoxy-5-methyl- 1,4-benzoquinol
-
-
?
additional information
?
-
-
cytochrome aa3-600 is a proton-pumping terminal oxidase
-
-
?
additional information
?
-
-
the enzyme does not oxidize 1,4-naphthoquinol, 2,3-dimethoxy-5-methyl-6-(n-nonyl)-1,4-benzoquinol, and 2,3-dimethoxy-5-methyl- 1,4-benzoquinol
-
-
?
additional information
?
-
-
no activity with 1,4-naphthoquinol, N,N,N',N'-tetramethyl-1,4-phenylenediamine plus ascorbate or reduced cytochrome c
-
-
?
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metabolism
-
the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cyo, Cyd and Nar contribute to the proton motive force that drives ATP formation. oxygen-dependent cytochrome oxidases, cytochrome bo3 (Cyo) and cytochrome bd (Cyd) oxidase, sustain up to 67% (Cyd) and 78% (Cyo) of HemG activity in the absence of ubiquinone, indicating a tight association of the quinones with the enzyme complexes during preparation
physiological function
-
cytochrome aa3 is the most important terminal oxidase contributing to proton motive force generation in exponentially growing cells
physiological function
-
cytochrome aas-600 is the major terminal oxidase in lopgh ase cells
physiological function
-
the enzyme is important during murine infection
physiological function
Q8YAV0; Q8YAU9
both cytochrome bd-type CydAB, EDC 7.1.1.7, and cytochrome aa3-type menaquinol QoxAB oxidase, EC 7.1.1.5, are used for respiration under different oxygen tensions. Possession of both terminal oxidases is important in infection. In air, the CydAB bd-type oxidase is essential for aerobic respiration and intracellular replication, and cydAB mutants are highly attenuated in mice. At 1% O2 (vol/vol), both oxidases are functional, and the presence of either is sufficient for aerobic respiration and intracellular replication. At 0.2% O2 (vol/vol), both oxidases are necessary for maximum growth
physiological function
-
demethylmenaquinol in the respiratory chain in the bacterial cytoplasmic membrane is crucial for the extracellular electron transfer. Heme proteins are not involved, and cytochrome bd oxidase activity attenuates extracellular electron transfer
physiological function
L7N662; O06139
mutants lacking subunits cydA and cydAB are hypersusceptible to compounds targeting the mycobacterial bc1 menaquinol cytochrome c oxidoreductase and exhibit bioenergetic profiles indistinguishable from strains deficient in the ABC-type transporter, CydDC, predicted to be essential for cytochrome bd assembly
physiological function
-
cytochrome aa3 is the most important terminal oxidase contributing to proton motive force generation in exponentially growing cells
-
physiological function
-
cytochrome aas-600 is the major terminal oxidase in lopgh ase cells
-
physiological function
-
both cytochrome bd-type CydAB, EDC 7.1.1.7, and cytochrome aa3-type menaquinol QoxAB oxidase, EC 7.1.1.5, are used for respiration under different oxygen tensions. Possession of both terminal oxidases is important in infection. In air, the CydAB bd-type oxidase is essential for aerobic respiration and intracellular replication, and cydAB mutants are highly attenuated in mice. At 1% O2 (vol/vol), both oxidases are functional, and the presence of either is sufficient for aerobic respiration and intracellular replication. At 0.2% O2 (vol/vol), both oxidases are necessary for maximum growth
-
physiological function
-
mutants lacking subunits cydA and cydAB are hypersusceptible to compounds targeting the mycobacterial bc1 menaquinol cytochrome c oxidoreductase and exhibit bioenergetic profiles indistinguishable from strains deficient in the ABC-type transporter, CydDC, predicted to be essential for cytochrome bd assembly
-
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13686
-
1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
144000
-
calculated from sequence of cDNA
15000
-
1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
20000
-
1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
22670
-
1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
33640
-
1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
54000
-
1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
57000
-
the preparation consists of two major (57000 Da and 36000 Da) polypeptides
73834
-
1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
36000
-
the preparation consists of two major (57000 Da and 36000 Da) polypeptides
36000
-
1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
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Lemma, E.; Schagger, H.; Kroger, A.
The menaquinol oxidase of Bacillus subtilis W23
Arch. Microbiol.
159
574-578
1993
Bacillus subtilis, Bacillus subtilis W23
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Lemma, E.; Simon, J.; Schagger, H.; Kroger, A.
Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis
Arch. Microbiol.
163
432-438
1995
Bacillus subtilis, Bacillus subtilis W23
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Transient-state reduction and steady-state kinetic studies of menaquinol oxidase from Bacillus subtilis, cytochrome aa3-600 nm. Spectroscopic characterization of the steady-state species
Biochemistry
40
13331-13341
2001
Bacillus subtilis
brenda
Powers, L.; Lauraeus, M.; Reddy, K.S.; Chance, B.; Wikstroem, M.
Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis
Biochim. Biophys. Acta
1183
504-512
1994
Bacillus subtilis
brenda
Winstedt, L.; Frankenberg, L.; Hederstedt, L.; von Wachenfeldt, C.
Enterococcus faecalis V583 contains a cytochrome bd-type respiratory oxidase
J. Bacteriol.
182
3863-3866
2000
Enterococcus faecalis
brenda
Winstedt, L.; von Wachenfeldt, C.
Terminal oxidases of Bacillus subtilis strain 168: one quinol oxidase, cytochrome aa3 or cytochrome bd, is required for aerobic growth
J. Bacteriol.
182
6557-6564
2000
Bacillus subtilis, Bacillus subtilis 168
brenda
Lauraeus, M.; Wikstroem, M.
The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties
J. Biol. Chem.
268
11470-11473
1993
Bacillus subtilis, Bacillus subtilis 168
brenda
Yi, S.M.; Narasimhulu, K.V.; Samoilova, R.I.; Gennis, R.B.; Dikanov, S.A.
Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis
J. Biol. Chem.
285
18241-18251
2010
Bacillus subtilis
brenda
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.
Heme biosynthesis is coupled to electron transport chains for energy generation
Proc. Natl. Acad. Sci. USA
107
10436-10441
2010
Escherichia coli
brenda
Bossis, F.; De Grassi, A.; Palese, L.L.; Pierri, C.L.
Prediction of high- and low-affinity quinol-analogue-binding sites in the aa3 and bo3 terminal oxidases from Bacillus subtilis and Escherichia coli
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461
305-314
2014
Bacillus subtilis
brenda
Yi, S.M.; Taguchi, A.T.; Samoilova, R.I.; OMalley, P.J.; Gennis, R.B.; Dikanov, S.A.
Plasticity in the high affinity menaquinone binding site of the cytochrome aa3-600 menaquinol oxidase from Bacillus subtilis
Biochemistry
54
5030-5044
2015
Bacillus subtilis, Bacillus subtilis 1A1
brenda
Corbett, D.; Goldrick, M.; Fernandes, V.E.; Davidge, K.; Poole, R.K.; Andrew, P.W.; Cavet, J.; Roberts, I.S.
Listeria monocytogenes has both a bd-type and an aa3-type terminal oxidase which allow growth in different oxygen levels and both are important in infection
Infect. Immun.
85
e00354-17
2017
Listeria monocytogenes
brenda
Gartner, P.
Characterization of a quinole-oxidase activity in crude extracts of Thermoplasma acidophilum and isolation of an 18-kDa cytochrome
Eur. J. Biochem.
200
215-222
1991
Thermoplasma acidophilum
brenda
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Susceptibility of Mycobacterium tuberculosis cytochrome bd oxidase mutants to compounds targeting the terminal respiratory oxidase, cytochrome c
Antimicrob. Agents Chemother.
61
e01338
2017
Mycobacterium tuberculosis (L7N662 and O06139), Mycobacterium tuberculosis H37Rv (L7N662 and O06139)
brenda
Pankratova, G.; Leech, D.; Gorton, L.; Hederstedt, L.
Extracellular electron transfer by the gram-positive bacterium Enterococcus faecalis
Biochemistry
57
4597-4603
2018
Enterococcus faecalis
brenda
Corbett, D.; Goldrick, M.; Fernandes, V.E.; Davidge, K.; Poole, R.K.; Andrew, P.W.; Cavet, J.; Roberts, I.S.
Listeria monocytogenes has both a bd-type and an aa3 -type terminal oxidase which allow growth in different oxygen levels and both are important in infection
Infect. Immun.
85
e00354
2017
Listeria monocytogenes serotype 1/2a (Q8YAV0 and Q8YAU9), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8YAV0 and Q8YAU9)
brenda
Safarian, S.; Rajendran, C.; Mueller, H.; Preu, J.; Langer, J.D.; Ovchinnikov, S.; Hirose, T.; Kusumoto, T.; Sakamoto, J.; Michel, H.
Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases
Science
352
583-586
2016
Geobacillus thermodenitrificans (A4IKP6 and A4IKP7), Geobacillus thermodenitrificans NG80-2 (A4IKP6 and A4IKP7)
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