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Information on EC 7.1.1.3 - ubiquinol oxidase (H+-transporting) and Organism(s) Escherichia coli and UniProt Accession P26458
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7.1.1.3 ubiquinol oxidase (H+-transporting)IUBMB Comments
Contains a dinuclear centre comprising two hemes, or heme and copper. This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) depends on the enzyme; for example, for the bo3 oxidase it is 2. cf. EC 7.1.1.7, ubiquinol oxidase ubiquinol oxidase (electrogenic, proton-motive force generating).
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Word Map
- 7.1.1.3
- oxidases
- heme
-
heme-copper
-
low-spin
- cyanide
-
binuclear
-
high-spin
- dioxygen
-
aa3-type
- vinelandii
- azotobacter
- ubiquinol-1
-
microaerobic
-
soret
-
quinone-binding
- protoheme
-
q-loop
-
air-oxidized
-
four-electron
-
cyanide-resistant
-
cyanide-insensitive
- qh
-
ubisemiquinone
- vitreoscilla
- ubiquinone-8
-
photodissociation
-
heme-heme
-
flow-flash
- arca
-
alpha-band
-
co-bound
-
oxygen-binding
-
ubiquinone-binding
-
oxoferryl
-
redox-coupled
- synthesis
- n,n,n',n'-tetramethyl-p-phenylenediamine
-
co-binding
-
oxygen-reducing
-
di-heme
- hqno
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cytochrome bd, ubiquinol oxidase, cytochrome bo, cydab, cytochrome bd oxidase, cytochrome bo3, cytochrome o complex, bo-type ubiquinol oxidase, bd-type quinol oxidase, cytochrome bo3 ubiquinol oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
appB
cyoB
cytochrome bd-I oxidase
-
-
-
-
cytochrome bd-II oxidase
cytochrome bo oxidase
cytochrome bo3
cytochrome bo3 ubiquinol oxidase
-
-
cytochrome bd-II oxidase
-
-
-
-
cytochrome bo oxidase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ubiquinol:oxygen oxidoreductase (H+-transporting)
Contains a dinuclear centre comprising two hemes, or heme and copper. This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) depends on the enzyme; for example, for the bo3 oxidase it is 2. cf. EC 7.1.1.7, ubiquinol oxidase ubiquinol oxidase (electrogenic, proton-motive force generating).
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ubiquinol-1 + O2 + H+[side 1]
ubiquinone-1 + H2O + H+[side 2]
-
-
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
-
-
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
additional information
?
-
-
a significant interaction is observed only between Vitreoscilla hemoglobin and subunit I of cytochrome bo
-
-
?
additional information
?
-
-
electron transfer between hemes d and b595 is not electrogenic, although heme b595 is the major electron acceptor for heme d during the backflow, and therefore is not likely to be accompanied by net H+ uptake or release
-
-
?
additional information
?
-
-
the enzyme does not interact with cytochrome c
-
-
?
additional information
?
-
-
enzymatic activity of Cyt-bo3 was estimated by measuring consumption of oxygen for ubiquinol oxidation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
-
-
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
the enzyme contains a hexa-coordinated low-spin heme, heme B and a penta-coordinated high-spin heme, heme O
heme
-
the enzyme contains a low-spin b-like heme and a high-spin 6-like heme, designated cytochromes b and o respectively
heme
-
the high-spin heme is magnetically coupled to a copper, CuB, forming a binuclear center which is the site of oxygen reduction to water
heme
-
the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family
heme
-
the enzyme contains the low spin hexacoordinate heme b558 and the high spin pentacoordinate hemes b595 and d
ubiquinone-8
-
the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
Fe
-
the pure four-subunit enzyme contains two equivalents of iron (19.5 ng/mg)
additional information
-
the enzyme contains no zinc. The equivalent of CuA of the aa3-type cytochrome c oxidases is absent in this quinol oxidase
copper
the enzyme is a four-subunit heme-copper oxidase containing CuB
copper
-
the high-spin heme is magnetically coupled to a copper, CuB, forming a binuclear center which is the site of oxygen reduction to water
Cu2+
-
the pure four-subunit enzyme contains one equivalent of copper (7.5 ng/mg)
Cu2+
-
the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sulfide
low-micromolar levels of sulfide directly inhibit the proton-pumping cytochrome bo oxidase, but not cytochrome bd oxidase
additional information
enzyme is insensitive to sulfide up to 0.058 mM
-
additional information
enzyme is insensitive to sulfide up to 0.058 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
ubiquinol-1
wild type enzyme, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C
0.023
ubiquinol-1
mutant enzyme Q101N, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C
0.024
ubiquinol-1
mutant enzyme Q101N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C
0.045
ubiquinol-1
wild type enzyme, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C
0.175
ubiquinol-1
mutant enzyme H98N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00074
2-heptyl-4-hydroxyquinoline N-oxide
-
wild type enzyme, at 37°C, pH 7.0
0.0007
2-n-heptyl-4-hydroxyquinoline N-oxide
-
wild type enzyme, at pH 7.0 and 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
loss of cytochrome bd-I oxidase subunit II (gene cydB) causes diminished respiration rates, impaired motility and enhanced acid resistance. CydB cells contain elevated heme d, particularly at low pH. The GABA/glutamate gadC antiporter is highly up-regulated in cydB cells. Eschrichia coli can compensate for the loss of cytochrome bd-I activity
physiological function
physiological function
-
cytochrome bd-II-mediated quinol oxidation prevents the accumulation of NADH, whereas GABA synthesis/antiport maintains the proton motive force for ATP production
physiological function
-
cytochrome bo is a four-subunit quinol oxidase in the aerobic respiratory chain of Escherichia coli and functions as a redox-coupled proton pump
physiological function
-
cytochrome bo-type ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli catalyzes the reduction of dioxygen to water with ubiquinol-8, and utilizes the redox reactions to drive vectorial translocation of protons across the cytoplasmic membrane
physiological function
cytochrome bo3 ubiquinol oxidase from Escherichia coli is a four-subunit heme-copper oxidase that catalyzes the four-electron reduction of O2 to water and functions as a proton pump
physiological function
-
cytochrome bo3 ubiquinol oxidase serves as part of a proton loading site that regulates proton translocation across the protein matrix of the enzyme
physiological function
-
the ubiquinol oxidase, cytochrome b03, of Escherichia coli is a member of the respiratory heme-copper oxidase family and conserves energy from the reduction of dioxygen to water by translocation of protons across the bacterial membrane
physiological function
the enzyme prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide
physiological function
in respiratory mutants, both O2-consumption and aerobic growth are severely impaired by sulfide when respiration is sustained by the bo3 oxidase alone
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
in the absence of the tightly bound quinone, a strongly diminished rate of electrocatalytic reduction of oxygen is detected, which can be restored by adding quinones. The stabilization of the radical is not necessary for the oxygen reaction. The reaction mechanism should involve a one electron transfer step from the quinone radical to the next electron acceptor, the heme b
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 9-10% (w/v) PEG 1500, 100 mM HEPES pH 7.0, 100 mM NaCl, 100 mM MgCl2, 5% (v/v) ethanol
-
hanging drop vapor diffusion method, using 9-10% (w/v) PEG 1500, 100 mM NaCl, 100 mM MgCl2 and 5% (v/v) ethanol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D135K
-
the mutant is deficient in proton pumping (23% activity compared to the wild type enzyme)
D135N
D188N
D256N
D36V
-
the mutant of subunit III shows 160% activity compared to the wild type enzyme
D407N
D75E
D75H
D75N
E164A
-
the mutant of subunit I shows 28% activity compared to the wild type enzyme
E164K
-
the mutant of subunit I shows 54% activity compared to the wild type enzyme
E259A
-
the mutant of subunit II shows 135% activity compared to the wild type enzyme
E259K
-
the mutant of subunit II shows 97% activity compared to the wild type enzyme
E286C
E286D
E286Q
E445A
-
heme b595 is present in the E445A mutant. Formation of the oxoferryl state in the mutant is about 100fold slower than in the wild type enzyme. The E445A substitution does not affect intraprotein electron re-equilibration after the photolysis of CO bound to ferrous heme d in the one-electron-reduced enzyme. The mutation does not affect membrane potential generation coupled to intramolecular electron redistribution between hemes d2+ and b558
E540Q
-
the mutation affects the CO-binding by the heme-copper binuclear center
F138G
-
the mutant shows 63% proton-translocating activity compared to the wild type enzyme
F138R
-
the mutant shows 55% proton-translocating activity compared to the wild type enzyme
F165A
-
the mutant of subunit I shows 37% activity compared to the wild type enzyme
F29I
-
the mutant of subunit III shows 115% activity compared to the wild type enzyme
F93A
-
the mutant shows 37% activity with ubiquinol-1 and 102% activity with ubiquinol-2 compared to the wild type enzyme
F93Y
G132A
-
the mutant shows wild type proton-translocation activity (113% activity compared to the wild type enzyme)
G132D/D135N
-
the mutant shows 66% proton-translocating activity compared to the wild type enzyme
H333L
-
the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
H334L
-
the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
H98F
mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials
H98N
H98T
I102W
mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials
K25L
-
the mutant of subunit III shows75 % activity compared to the wild type enzyme
K362Q
K55Q
-
the mutant possesses 100% copper and 73% cytochrome o compared to the wild type enzyme
L160W
-
the mutant shows 58% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
L171A
-
the mutant of subunit I shows 79% activity compared to the wild type enzyme
N124D
-
the mutant is deficient in proton pumping (56% activity compared to the wild type enzyme)
N124D/D135N
-
the mutant shows 21% proton-translocating activity compared to the wild type enzyme
N124H
-
the mutant is deficient in proton pumping (16% activity compared to the wild type enzyme)
N142D
-
the mutant is deficient in proton pumping (48% activity compared to the wild type enzyme)
N142D/D135N
-
the mutant shows 33% proton-translocating activity compared to the wild type enzyme
N142Q
-
the mutant shows wild type proton-translocation activity (109% activity compared to the wild type enzyme)
N142V
-
the mutant is deficient in proton pumping (22% activity compared to the wild type enzyme)
N157V
-
the mutant shows 23% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
P128A
-
the mutant shows wild type proton-translocation activity (115% activity compared to the wild type enzyme)
P139E/D135N
-
the mutant shows 95% proton-translocating activity compared to the wild type enzyme
Pl39A
-
the mutant shows wild type proton-translocation activity (67% activity compared to the wild type enzyme)
Pl39E
-
the mutant shows wild type proton-translocation activity (46% activity compared to the wild type enzyme)
Q101A
Q101E
-
the mutant shows 55% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
Q101L
Q101M
-
the mutant shows 51% activity with ubiquinol-1 and 72% activity with ubiquinol-2 compared to the wild type enzyme
Q101N
Q101T
-
the mutant shows 27% activity with ubiquinol-1 and 62% activity with ubiquinol-2 compared to the wild type enzyme
Q167A
-
the mutant of subunit I shows 57% activity compared to the wild type enzyme
Q167K
-
the mutant of subunit I shows 75% activity compared to the wild type enzyme
Q195L
-
the mutant of subunit I shows 119% activity compared to the wild type enzyme
Q82A
-
the mutant shows 88% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
R134P
-
the mutant shows 112% proton-translocating activity compared to the wild type enzyme
R176A
-
the mutant of subunit III shows 70% activity compared to the wild type enzyme
R257Q
-
the mutations specifically eliminates the CuB center from the oxidase complex
R481Q
R482Q
-
the mutant possesses 82% copper and 100% cytochrome o compared to the wild type enzyme
R71H
mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials
R71Q
R80Q
-
the mutation causes loss of a diagnostic peak for low-spin heme b in the 77 K redox difference spectrum
S177A
-
the mutant of subunit I shows 91% activity compared to the wild type enzyme
T168A
-
the mutant of subunit I shows 118% activity compared to the wild type enzyme
T247V
-
the mutant of subunit I shows 173% activity compared to the wild type enzyme
W136A
-
the mutant of subunit II shows 89% activity compared to the wild type enzyme
W136K
-
the mutant of subunit II shows 105% activity compared to the wild type enzyme
W156A
-
the mutant of subunit III shows 70% activity compared to the wild type enzyme
Y173F
-
the mutant possesses 91% copper and 108% cytochrome o compared to the wild type enzyme
Y288F
-
the mutations specifically eliminates the CuB center from the oxidase complex
D135N
-
the mutant is deficient in proton pumping (45% activity compared to the wild type enzyme)
D135N
-
the mutant shows 45% activity compared to the wild type enzyme, with proton pumping decoupled from the electron-transfer activity
D135N
-
the mutations specifically eliminates the CuB center from the oxidase complex
D188N
-
the mutant possesses 100% copper and 81% cytochrome o compared to the wild type enzyme
D256N
-
the mutant possesses 103% copper and 74% cytochrome o compared to the wild type enzyme
D407N
-
the mutation affects the CO-binding by the heme-copper binuclear center
D75E
-
the mutant shows 48% activity with ubiquinol-1 and 88% activity with ubiquinol-2 compared to the wild type enzyme
D75H
mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials
E286C
-
the mutant shows 3% activity compared to the wild type enzyme as a result of the inhibition of proton transfer from the D-channel
E286C
-
the mutant still reduces oxygen to oxidize ubiquinol, transporting chemical protons across the membrane in the process, but is unable to pump protons
E286D
-
the mutant does not show significant perturbations on the redox metal centers even though it is still inactive
E286Q
-
the mutant shows 4% activity compared to the wild type enzyme and is unable to bind azide ions
E286Q
-
the mutations specifically eliminates the CuB center from the oxidase complex
F93Y
-
the mutant shows 81% activity with ubiquinol-1 and 107% activity with ubiquinol-2 compared to the wild type enzyme
F93Y
mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV
H98N
-
the mutant shows 3% activity with ubiquinol-1 and 10% activity with ubiquinol-2 compared to the wild type enzyme
H98T
-
the mutant shows 4% activity with ubiquinol-1 and 9% activity with ubiquinol-2 compared to the wild type enzyme
K362Q
-
the mutation affects the CO-binding by the heme-copper binuclear center
Q101A
-
the mutant shows 26% activity with ubiquinol-1 and 82% activity with ubiquinol-2 compared to the wild type enzyme
Q101A
mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV
Q101L
-
the mutant shows 11% activity with ubiquinol-1 and 58% activity with ubiquinol-2 compared to the wild type enzyme
Q101L
mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV
Q101N
the mutation inhibits activity by 75% and causes a 10fold increase in the apparent KM for ubiquinol-1
Q101N
-
the mutant shows 10% activity with ubiquinol-1 and 61% activity with ubiquinol-2 compared to the wild type enzyme
R481Q
-
the mutant possesses 91% copper and 73% cytochrome o compared to the wild type enzyme
R71Q
-
the mutant shows 3% activity with ubiquinol-1 and 8% activity with ubiquinol-2 compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged on subunit II Cyt-bo3 from Escherichia coli strain C43 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of Cyt-bo3 samples in Escherichia coli strain C43, each plasmid encodes the cyoABCDE operon expressing Cyt-bo3 with a 6-His tag on the C-terminus of subunit II. Functional cell-free in vitro expression of Cyt-bo3, employing T7 promoter, and insertion into the artificial membrane
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
inactivating the cytochrome bd-II oxidase of the aerobic respiratory chain is a simple and effective strategy to improve poly(3-hydroxybutyrate) biosynthesis in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abramson, J.; Larsson, G.; Byrne, B.; Puustinen, A.; Garcia-Horsman, A.; Iwata, S.
Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli
Acta Crystallogr. Sect. D
56
1076-1078
2000
Escherichia coli, Escherichia coli GO105
Minghetti, K.C.; Goswitz, V.C.; Gabriel, N.E.; Hill, J.J.; Barassi, C.A.; Georgiou, C.D.; Chan, S.I.; Gennis, R.B.
Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity
Biochemistry
31
6917-6924
1992
Escherichia coli, Escherichia coli RG145
Thomas, J.W.; Puustinen, A.; Alben, J.O.; Gennis, R.B.; Wikstroem, M.
Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity
Biochemistry
32
10923-10928
1993
Escherichia coli, Escherichia coli GL101
Thomas, J.W.; Lemieux, L.J.; Alben, J.O.; Gennis, R.B.
Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center
Biochemistry
32
11173-11180
1993
Escherichia coli, Escherichia coli GL101
Calhoun, M.W.; Hill, J.J.; Lemieux, L.J.; Ingledew, W.J.; Alben, J.O.; Gennis, R.B.
Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands
Biochemistry
32
11524-11529
1993
Escherichia coli, Escherichia coli GLlOl
Garcia-Horsman, J.; Puustinen, A.; Gennis, R.; Wikstrom, M.
Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135-->Asn
Biochemistry
34
4428-4433
1995
Escherichia coli
Ek, M.S.; Brzezinski, P.
Oxidation of ubiquinol by cytochrome bo3 from Escherichia coli: Kinetics of electron and proton transfer
Biochemistry
36
5425-5431
1997
Escherichia coli
Mogi, T.; Minagawa, J.; Hirano, T.; Sato-Watanabe, M.; Tsubaki, M.; Uno, T.; Hori, H.; Nakamura, H.; Nishimura, Y.; Anraku, Y.
Substitutions of conserved aromatic amino acid residues in subunit I perturb the metal centers of the Escherichia coli bo-type ubiquinol oxidase
Biochemistry
37
1632-1639
1998
Escherichia coli, Escherichia coli GO103/pMFO2
Egawa, T.; Lin, M.T.; Hosler, J.P.; Gennis, R.B.; Yeh, S.R.; Rousseau, D.L.
Communication between R481 and CuB in cytochrome bo3 ubiquinol oxidase from Escherichia coli
Biochemistry
48
12113-12124
2009
Escherichia coli
Bolgiano, B.; Salmon, I.; Poole, R.K.
Reactions of the membrane-bound cytochrome bo terminal oxidase of Escherichia coli with carbon monoxide and oxygen
Biochim. Biophys. Acta
1141
95-104
1993
Escherichia coli, Escherichia coli RG145
Yap, L.L.; Lin, M.T.; Ouyang, H.; Samoilova, R.I.; Dikanov, S.A.; Gennis, R.B.
The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli
Biochim. Biophys. Acta
1797
1924-1932
2010
Escherichia coli
Egawa, T.; Ganesan, K.; Lin, M.T.; Yu, M.A.; Hosler, J.P.; Yeh, S.R.; Rousseau, D.L.; Gennis, R.B.
Differential effects of glutamate-286 mutations in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo3 ubiquinol oxidase from Escherichia coli
Biochim. Biophys. Acta
1807
1342-1348
2011
Escherichia coli, Escherichia coli C43 (DE3)
Salerno, J.C.; Ingledew, W.J.
Orientation of the haems of the ubiquinol oxidase:O2 reductase, cytochrome bo of Escherichia coli
Eur. J. Biochem.
198
789-792
1991
Escherichia coli, Escherichia coli RG145
Orii, Y.; Mogi, T.; Kawasaki, M.; Anraku, Y.
Facilitated intramolecular electron transfer in cytochrome bo-type ubiquinol oxidase initiated upon reaction of the fully reduced enzyme with dioxygen
FEBS Lett.
352
151-154
1994
Escherichia coli, Escherichia coli GO103
Tsubaki, M.; Hori, H.; Mogi, T.
Glutamate-286 mutants of cytochrome bo-type ubiquinol oxidase from Escherichia coli: influence of mutations on the binuclear center structure revealed by FT-IR and EPR spectroscopies
FEBS Lett.
416
247-250
1997
Escherichia coli, Escherichia coli GO103
Mogi, T.; Sato-Watanabe, M.; Miyoshi, H.; Orii, Y.
Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen
FEBS Lett.
457
223-226
1999
Escherichia coli, Escherichia coli GO103/pHN3795-1
Kawasaki, M.; Mogi, T.; Anraku, Y.
Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase
J. Biochem.
122
422-429
1997
Escherichia coli, Escherichia coli ST4676
Park, K.W.; Kim, K.J.; Howard, A.J.; Stark, B.C.; Webster, D.A.
Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases
J. Biol. Chem.
277
33334-33337
2002
Escherichia coli, Escherichia coli JM103, Pseudomonas aeruginosa, Vitreoscilla sp.
Shepherd, M.; Sanguinetti, G.; Cook, G.M.; Poole, R.K.
Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism
J. Biol. Chem.
285
18464-18472
2010
Escherichia coli, Escherichia coli BW25113
Abramson, J.; Riistama, S.; Larsson, G.; Jasaitis, A.; Svensson-Ek, M.; Laakkonen, L.; Puustinen, A.; Iwata, S.; Wikstrom, M.
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site
Nat. Struct. Biol.
7
910-917
2000
Escherichia coli (P0ABJ1), Escherichia coli
Belevich, I.; Borisov, V.B.; Zhang, J.; Yang, K.; Konstantinov, A.A.; Gennis, R.B.; Verkhovsky, M.I.
Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site
Proc. Natl. Acad. Sci. USA
102
3657-3662
2005
Escherichia coli, Escherichia coli GO105
Yildiz, A.A.; Knoll, W.; Gennis, R.B.; Sinner, E.K.
Cell-free synthesis of cytochrome bo3 ubiquinol oxidase in artificial membranes
Anal. Biochem.
423
39-45
2012
Escherichia coli
Sun, C.; Taguchi, A.T.; Vermaas, J.V.; Beal, N.J.; OMalley, P.J.; Tajkhorshid, E.; Gennis, R.B.; Dikanov, S.A.
Q-band electron-nuclear double resonance reveals out-of-plane hydrogen bonds stabilize an anionic ubisemiquinone in cytochrome bo3 from Escherichia coli
Biochemistry
55
5714-5725
2016
Escherichia coli
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
Choi, S.K.; Lin, M.T.; Ouyang, H.; Gennis, R.B.
Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli
Biochim. Biophys. Acta
1858
366-370
2017
Escherichia coli
Li, M.; Khan, S.; Rong, H.; Tuma, R.; Hatzakis, N.S.; Jeuken, L.J.C.
Effects of membrane curvature and pH on proton pumping activity of single cytochrome bo3 enzymes
Biochim. Biophys. Acta
1858
763-770
2017
Escherichia coli
Hoeser, J.; Hong, S.; Gehmann, G.; Gennis, R.B.; Friedrich, T.
Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site
FEBS Lett.
588
1537-1541
2014
Escherichia coli
Choi, S.K.; Schurig-Briccio, L.; Ding, Z.; Hong, S.; Sun, C.; Gennis, R.B.
Location of the substrate binding site of the cytochrome bo3 ubiquinol oxidase from Escherichia coli
J. Am. Chem. Soc.
139
8346-8354
2017
Escherichia coli
Liu, Q.; Lin, Z.; Zhang, Y.; Li, Y.; Wang, Z.; Chen, T.
Improved poly(3-hydroxybutyrate) production in Escherichia coli by inactivation of cytochrome bd-II oxidase or/and NDH-II dehydrogenase in low efficient respiratory chains
J. Biotechnol.
192
170-176
2014
Escherichia coli, Escherichia coli JM109
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, Escherichia coli (P0ABJ1 and P0ABI8 and P0ABJ3 and P0ABJ6)
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 (P0ABI8), Escherichia coli
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 (P0ABJ1 and P0ABI8 and P0ABJ3 and P0ABJ6), Escherichia coli (P26459 and P26458), Escherichia coli
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Transporter Classification Database (TCDB): 3.D.4.5.1
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