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Information on EC 7.1.1.7 - quinol oxidase (electrogenic, proton-motive force generating) and Organism(s) Escherichia coli and UniProt Accession P56100

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EC Tree
IUBMB Comments
This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. cf. EC 7.1.1.3, ubiquinol oxidase (H+-transporting).
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Escherichia coli
UNIPROT: P56100 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
cytochrome bd-i, cytochrome bd quinol oxidase, cydabdc, cytochrome bd-i respiratory oxidase, cytochrome bd-i complex, cytochrome bd-i ubiquinol oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bd-I type oxidase
-
cytochrome bd
-
-
cytochrome bd oxidase
cytochrome bd quinol oxidase
-
cytochrome bd-I
-
-
cytochrome bd-I complex
-
-
cytochrome bd-I oxidase
-
-
cytochrome bd-I respiratory oxidase
-
-
cytochrome bd-I ubiquinol oxidase
-
cytochrome bd-II oxidase subunit II
-
ubiquinol oxidase (electrogenic, proton-motive force generating)
-
-
-
-
ubiquinol:oxygen oxidoreductase (electrogenic, non H+-transporting)
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
quinol:oxygen oxidoreductase (electrogenic, non H+-transporting)
This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. cf. EC 7.1.1.3, ubiquinol oxidase (H+-transporting).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 1,4-naphthoquinol + O2 + 4 H+[side 1]
2 1,4-naphthoquinone + 2 H2O + 4 H+[side 2]
show the reaction diagram
-
-
-
?
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]
show the reaction diagram
-
-
-
?
2 decylubiquinol + O2[side 2] + 4 H+[side 2]
2 decylubiquinone + 2 H2O[side 2] + 4 H+[side 1]
show the reaction diagram
-
-
-
?
2 duroquinol + O2 + 4 H+[side 1]
2 duroquinone + 2 H2O + 4 H+[side 2]
show the reaction diagram
-
-
-
?
2 menadiol + O2 + 4 H+[side 1]
2 menadione + 2 H2O + 4 H+[side 2]
show the reaction diagram
-
-
-
?
2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
show the reaction diagram
decylubiquinol + H2O2[side 2] + 2 H+[side 2]
decylubiquinone + H2O[side 2] + 2 H+[side 1]
show the reaction diagram
-
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
show the reaction diagram
-
respiratory terminal oxidase
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NO
reversible inhibition
peroxynitrite
addition of ONOO- to cytochrome bd in turnover with ascorbate and N,N,N',N'-tetramethyl-p-phenylenediamine causes the irreversible inhibition of about 15% of the enzyme fraction, due to the NO radical generated from ONOO-. Addition of ONOO- to cells expressing cytochrome bd as the only terminal oxidase, causes about 5% irreversible inhibition of O2 consumption. 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
additional information
enzyme is insensitive to sulfide up to 0.058 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.072
decylubiquinol
pH 7.0, temperature not specified in the publication
6.6
H2O2[side 2]
pH 7.0, temperature not specified in the publication
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
101
H2O2[side 2]
pH 7.0, temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
H2O2[side 2]
pH 7.0, temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
substrate 2,4-dimethoxy-5-methyl-1,4-benzoquinol, pH 6.3, 37°C
15.3
substrate menadiol, pH 6.3, 37°C
17.1
substrate menadiol, presence of 50 mM NCl, pH 6.3, 37°C
17.3
substrate menadiol, presence of 50 mM KCl, pH 6.3, 37°C
6.2
substrate duroquinol, pH 6.3, 37°C
7.7
substrate 1,4-naphtoquinol, pH 6.3, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
35% of the activity at pH 7.0, substrate H2O2
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the cytochrome bd-I complexis concentrated in mobile patches in the plasma membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E2QIA5_ECOLX
522
9
58205
TrEMBL
-
A0A2S4MV64_ECOLX
37
1
4042
TrEMBL
-
C3TIJ7_ECOLX
379
8
42453
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
-
sedimentation equilibrium study
43000
-
1 * 58000, plus 1 * 43000, SDS-PAGE
58000
-
1 * 58000, plus 1 * 43000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 58000, plus 1 * 43000, SDS-PAGE
heterotrimer
-
1 * 57000 + 1 * 43000 + 1 * 4000, SDS-PAGE
additional information
-
the purified, enzymatically active cytochrome d complex solubilized in Triton X-100 is an alphabeta heterodimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D239A
mutation in subunit cydA. Mutant is not able to confer the ability to grow aerobically to a strain that has no genomically encoded respiratory oxidases. Heme content similar to wild-type, complete loss of ubiquinol oxidase activity
D239N
mutation in subunit cydA. Mutant is not able to confer the ability to grow aerobically to a strain that has no genomically encoded respiratory oxidases. Heme content similar to wild-type, complete loss of ubiquinol oxidase activity
D29E
mutation in subunit cydB. Mutant is totally inactive, and hemes d and b595 are not present in the isolated enzyme
E107D
mutation in subunit cydA. About 15% of the heme contant of wild-type, complete loss of ubiquinol oxidase activity
E107Q
mutation in transmembrane helix III of subunit cydA. Mutant is totally inactive, but retains its hemes. Residue E107 is protonated at pH 7.6 and is perturbed by the reduction of the heme d/heme b595 binuclear center at the active site
E257A
mutation of an acidic residue of subunit cydA at or near the quinol-binding site, mutation inactivates the enzyme but has no substantial influence on the Fourier transform infrared redox difference spectrum
E99A
mutation in subunit cydA. Mutant is not able to confer the ability to grow aerobically to a strain that has no genomically encoded respiratory oxidases. Complete loss of heme d and heme b595 and of ubiquinol oxidase activity
E99Q
mutation in subunit cydA. Mutant is not able to confer the ability to grow aerobically to a strain that has no genomically encoded respiratory oxidases. Complete loss of heme d and heme b595 and of ubiquinol oxidase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
preapration of highly pure and active enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli GO105/pTK1 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
cytochrome bd-I respiratory oxidase is the main contributor to NO tolerance and host colonisation under microaerobic conditions. Uropathogenic Escherichia coli strains have acquired a host of specialized mechanisms to evade nitrosative stresses
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team