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2 1,4-naphthoquinol + O2 + 4 H+[side 1]
2 1,4-naphthoquinone + 2 H2O + 4 H+[side 2]
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2 2,3-dimethoxy-5-methyl-1,4-benzoquinol + O2 + 4 H+[side 1]
2 2,3-dimethoxy-5-methyl-1,4-benzoquinone + 2 H2O + 4 H+[side 2]
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-
-
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2 duroquinol + O2 + 4 H+[side 1]
2 duroquinone + 2 H2O + 4 H+[side 2]
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2 menadiol + O2 + 4 H+[side 1]
2 menadione + 2 H2O + 4 H+[side 2]
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-
-
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2 decylubiquinol + O2[side 2] + 4 H+[side 2]
2 decylubiquinone + 2 H2O[side 2] + 4 H+[side 1]
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2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
decylubiquinol + H2O2[side 2] + 2 H+[side 2]
decylubiquinone + H2O[side 2] + 2 H+[side 1]
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-
-
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ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
additional information
?
-
2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
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-
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2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
-
respiratory terminal oxidase
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ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
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-
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ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
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-
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?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
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-
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?
additional information
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enzyme additionally catalyzes oxidation of N,N,N',N'-tetramethyl-p-phenylenediamine. This reaction is sensitive to inhibition by cyanide
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additional information
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enzyme additionally catalyzes oxidation of N,N,N',N'-tetramethyl-p-phenylenediamine. This reaction is sensitive to inhibition by cyanide
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additional information
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after the initial binding of O2, the OO bond is heterolytically cleaved to yield a kinetically competent heme d oxoferryl porphyrin pi-cation radical intermediate magnetically interacting with heme b595. This intermediate accumulates to 0.75-0.85 per enzyme in agreement with its much higher rate of formation at 20000 per s compared with its rate of decay of 1900 per s. The intermediate is next converted to a short lived heme d oxoferryl in a phase kinetically matched to the oxidation of heme b558 before completion of the reaction. The results indicate that cytochrome bd oxidases break the O-O bond in a single four-electron transfer without a peroxide intermediate. The fourth electron is donated by the porphyrin moiety rather than by a nearby amino acid
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additional information
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purified cytochrome bd in turnover with O2 is able to metabolize ONOO- with an apparent turnover rate as high as about 10 mol ONOO- per mol of enzyme and per s at 25°C
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additional information
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purified cytochrome bd in turnover with O2 is able to metabolize ONOO- with an apparent turnover rate as high as about 10 mol ONOO- per mol of enzyme and per s at 25°C
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physiological function
the enzyme contributes to bacterial resistance to nitric oxide and hydrogen peroxide
physiological function
the enzyme contributes to Escherichia coli survival in the mouse bladder
physiological function
-
the expression of cytochrome bd enhances bacterial tolerance to nitrosative stress
physiological function
besides its oxidase activity, cytochrome bd is a genuine quinol peroxidase that reduces hydrogen peroxide to water. The enzyme does not display catalase activity
physiological function
in respiratory mutants, both O2-consumption and aerobic growth are unaffected by up to 200 microM sulfide when cytochrome bd-I or bd-II enzyme actes as the only terminal oxidase. Wild-type Escherichia coli shows sulfide-insensitive respiration and growth under conditions favouring the expression of bd oxidases
physiological function
loss of the flavohemoglobin Hmp and cytochrome bd-I elicit high sensitivity to NO-mediated growth inhibition. The subunits cydAB mutant displays an attenuated colonisation phenotype in a mouse model after 2 days
physiological function
the interheme electron backflow reaction induced by photodissociation of CO from heme d in one-electron reduced cytochrome bd-I comprises two kinetically different phases: the fast electron transfer from heme d to heme b595 within 0.2-1.5 micros and the slower electron equilibration with tau of about 16 micros. At 200 ns, there is no electron transfer
physiological function
the unresolved photodissociation of CO is followed by a four-phased recombination with characteristic times of about 20 micros, 250 micros, 1.1 ms, and 24 ms. The 20x02micros phase most likely reflects bimolecular recombination of CO with heme d. The 250x02micros phase is heterogeneous and includes recombination of CO with about 7% of heme b595 and transition of heme d from a pentacoordinate to a transient hexacoordinate state in this enzyme population. The 24x02ms transition probably reflects a return of heme d to the pentacoordinate state in the same protein fraction. The 1.1x02ms phase reflects a recombination of CO with about 15% of heme b558
physiological function
when cystine is provided and sulfide levels rise, Escherichia coli becomes strictly dependent upon cytochrome bd oxidase for continued respiration. Low-micromolar levels of sulfide inhibit the proton-pumping cytochrome bo oxidase. In the absence of the back-up cytochrome bd oxidase, growth fails. Exogenous sulfide elicits the same effect
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Lenn, T.; Leake, M.C.; Mullineaux, C.W.
Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo
Mol. Microbiol.
70
1397-1407
2008
Escherichia coli
brenda
Yang, K.; Zhang, J.; Vakkasoglu, A.S.; Hielscher, R.; Osborne, J.P.; Hemp, J.; Miyoshi, H.; Hellwig, P.; Gennis, R.B.
Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center
Biochemistry
46
3270-3278
2007
Escherichia coli (P0ABJ9), Escherichia coli (P0ABK2), Escherichia coli
brenda
Zhang, J.; Barquera, B.; Gennis, R.B.
Gene fusions with beta-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O2 reactive site near the periplasmic surface
FEBS Lett.
561
58-62
2004
Escherichia coli (P0ABJ9), Escherichia coli
brenda
Sturr, M.G.; Krulwich, T.A.; Hicks, D.B.
Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a delta cyo delta cyd strain complemented by genes from Bacillus firmus OF4
J. Bacteriol.
178
1742-1749
1996
Escherichia coli (P26458), Escherichia coli
brenda
Miller, M.; Hermodson, M.; Gennis, R.
The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits
J. Biol. Chem.
263
5235-5240
1988
Escherichia coli
brenda
Paulus, A.; Rossius, S.G.; Dijk, M.; de Vries, S.
Oxoferryl-porphyrin radical catalytic intermediate in cytochrome bd oxidases protects cells from formation of reactive oxygen species
J. Biol. Chem.
287
8830-8838
2012
Escherichia coli (P0ABJ9)
brenda
Giuffre, A.; Borisov, V.B.; Arese, M.; Sarti, P.; Forte, E.
Cytochrome bd oxidase and bacterial tolerance to oxidative and nitrosative stress
Biochim. Biophys. Acta
1837
1178-1187
2014
Escherichia coli
brenda
Borisov, V.B.; Forte, E.; Siletsky, S.A.; Sarti, P.; Giuffre, A.
Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition
Biochim. Biophys. Acta
1847
182-188
2015
Escherichia coli, Escherichia coli (P0ABJ9 and P0ABK2 and P56100)
brenda
Degli Esposti, M.; Rosas-Perez, T.; Servin-Garciduenas, L.E.; Bolanos, L.M.; Rosenblueth, M.; Martinez-Romero, E.
Molecular evolution of cytochrome bd oxidases across proteobacterial genomes
Genome Biol. Evol.
7
801-820
2015
Rhodopseudomonas palustris, Magnetospirillum fulvum, Rhodovulum sp. PH10, Pararhodospirillum photometricum, Rhodovulum sulfidophilum (A0A0D6AXR3), Escherichia coli (P0ABJ9), Escherichia coli (P0ABK2), Bacillus subtilis (P94364), Bacillus subtilis (P94365), Acetobacter pasteurianus (S6CX21), Acetobacter pasteurianus (S6D686), Rhodopseudomonas palustris HaA2, Bacillus subtilis 168 (P94364), Bacillus subtilis 168 (P94365), Acetobacter pasteurianus 386B (S6CX21), Acetobacter pasteurianus 386B (S6D686)
brenda
Korshunov, S.; Imlay, K.R.; Imlay, J.A.
The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide
Mol. Microbiol.
101
62-77
2016
Escherichia coli (P0ABJ9 and P0ABK2 and P56100)
brenda
Siletsky, S.A.; Rappaport, F.; Poole, R.K.; Borisov, V.B.
Evidence for fast electron transfer between the high-spin haems in cytochrome bd-I from Escherichia coli
PLoS ONE
11
e0155186
2016
Escherichia coli, Escherichia coli (P0ABJ9 and P0ABK2 and P56100)
brenda
Shepherd, M.; Achard, M.E.; Idris, A.; Totsika, M.; Phan, M.D.; Peters, K.M.; Sarkar, S.; Ribeiro, C.A.; Holyoake, L.V.; Ladakis, D.; Ulett, G.C.; Sweet, M.J.; Poole, R.K.; McEwan, A.G.; Schembri, M.A.
The cytochrome bd-I respiratory oxidase augments survival of multidrug-resistant Escherichia coli during infection
Sci. Rep.
6
35285
2016
Escherichia coli, Escherichia coli (P0ABJ9 and P0ABK2 and P56100), Escherichia coli EC958
brenda
Siletsky, S.A.; Dyuba, A.V.; Elkina, D.A.; Monakhova, M.V.; Borisov, V.B.
Spectral-kinetic analysis of recombination reaction of heme centers of bd-type quinol oxidase from Escherichia coli with carbon monoxide
Biochemistry
82
1354-1366
2017
Escherichia coli (P0ABJ9 and P0ABK2 and P56100)
brenda
Forte, E.; Borisov, V.B.; Falabella, M.; Colaco, H.G.; Tinajero-Trejo, M.; Poole, R.K.; Vicente, J.B.; Sarti, P.; Giuffre, A.
The terminal oxidase cytochrome bd promotes sulfide-resistant bacterial respiration and growth
Sci. Rep.
6
23788
2016
Escherichia coli (P0ABJ9 and P0ABK2 and P56100)
brenda
Al-Attar, S.; Yu, Y.; Pinkse, M.; Hoeser, J.; Friedrich, T.; Bald, D.; De Vries, S.
Cytochrome bd displays significant quinol peroxidase activity
Sci. Rep.
6
27631
2016
Escherichia coli (P0ABJ9 and P0ABK2 and P56100)
brenda