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Information on EC 7.1.1.7 - quinol oxidase (electrogenic, proton-motive force generating)
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7.1.1.7 quinol oxidase (electrogenic, proton-motive force generating)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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Word Map
- 7.1.1.7
- oxidases
-
cyddc
-
low-spin
-
photodissociation
-
aa3-type
- menaquinol
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
+
+
4
=
2
+
2
+
4
Synonyms
cytochrome bd-i, cytochrome bd quinol oxidase, cydabdc, cytochrome bd-i respiratory oxidase, cytochrome bd-i complex, cytochrome bd-i ubiquinol oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bd-I type oxidase
CydA
CydAB
CydB
CydX
cytochrome bd
cytochrome bd oxidase
cytochrome bd-I respiratory oxidase
cytochrome bd-type quinol oxidase
EC 1.10.3.14
-
-
formerly
-
ubiquinol oxidase (electrogenic, proton-motive force generating)
-
-
-
-
ubiquinol:oxygen oxidoreductase (electrogenic, non H+-transporting)
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 quinol + O2[side 2] + 4 H+[side 2] = 2 quinone + 2 H2O[side 2] + 4 H+[side 1]
overall reaction
-
-
-
2 quinol = 2 quinone + 4 H+[side 1] + 4 e-
(1a)
-
-
-
O2[side 2] + 4 H+[side 2] + 4 e- = 2 H2O[side 2]
(1b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, , ,
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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).
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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
2 1,4-naphthoquinol + O2 + 4 H+[side 1]
2 1,4-naphthoquinone + 2 H2O + 4 H+[side 2]
-
-
-
?
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]
-
-
-
?
2 decylubiquinol + O2[side 2] + 4 H+[side 2]
2 decylubiquinone + 2 H2O[side 2] + 4 H+[side 1]
-
-
-
?
2 duroquinol + O2 + 4 H+[side 1]
2 duroquinone + 2 H2O + 4 H+[side 2]
-
-
-
?
2 menadiol + O2 + 4 H+[side 1]
2 menadione + 2 H2O + 4 H+[side 2]
-
-
-
?
decylubiquinol + H2O2[side 2] + 2 H+[side 2]
decylubiquinone + H2O[side 2] + 2 H+[side 1]
-
-
-
?
2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
-
-
-
-
?
2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
-
respiratory terminal oxidase
-
-
?
menadiol + O2 + H+[side 1]
menadione + H2O + H+[side 2]
-
-
-
-
?
menadiol + O2 + H+[side 1]
menadione + 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 + O2 + H+[side 1]
ubiquinone + 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 + O2 + H+[side 1]
ubiquinone + 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 + O2 + H+[side 1]
ubiquinone + 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 + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
-
-
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
enzyme additionally catalyzes oxidation of N,N,N',N'-tetramethyl-p-phenylenediamine. This reaction is sensitive to inhibition by cyanide
-
-
?
additional information
?
-
-
enzyme additionally catalyzes oxidation of N,N,N',N'-tetramethyl-p-phenylenediamine. This reaction is sensitive to inhibition by cyanide
-
-
?
additional information
?
-
-
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
?
-
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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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
2 ubiquinol + O2 + 4 H+[side 1]
2 ubiquinone + 2 H2O + 4 H+[side 2]
-
respiratory terminal oxidase
-
-
?
ubiquinol + O2 + H+[side 1]
ubiquinone + 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 + O2 + H+[side 1]
ubiquinone + 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 + O2 + H+[side 1]
ubiquinone + 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 + O2 + H+[side 1]
ubiquinone + 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 + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
heme b558 and the heme b595/heme d complex are likely to be close to each other. All three hemes are predicted to be near the periplasmic surface
heme
two- to threefold increase in cydAB gene expression upon reduction of the pO2 of the growth medium from 21 to 0.5% air saturation with concomitant increase in d-heme absorbance in spectra of membranes isolated from wild-type Mycobacterium smegmatis cultured at 1% air saturation
heme
the enzyme contains one low-spin haem (b558) and the two high-spin haems (b595 and d) as the redox-active cofactors
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The cytochrome bd-I respiratory oxidase augments survival of multidrug-resistant Escherichia coli during infection.
Sepsis
Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence.
Tuberculosis
Characterization of the cydAB-encoded cytochrome bd oxidase from Mycobacterium smegmatis.
Tuberculosis
The carboxy-terminal insert in the Q-loop is needed for functionality of Escherichia coli cytochrome bd-I.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
101
H2O2[side 2]
pH 7.0, temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
H2O2[side 2]
pH 7.0, temperature not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q927C3 i.e. subunit cydA, Q927C4 i.e. subunit cydB
Q927C3; Q927C4
UniProt
brenda
Q927C3 i.e. subunit cydA, Q927C4 i.e. subunit cydB
Q927C3; Q927C4
UniProt
brenda
B2HQZ0 i.e. subunit cydA, B2HQY9 i.e. subunit cydB
B2HQZ0; B2HQY9
UniProt
brenda
B2HQZ0 i.e. subunit cydA, B2HQY9 i.e. subunit cydB
B2HQZ0; B2HQY9
UniProt
brenda
P0ABJ9 i.e. subunit cydA, P0ABK2 i.e. subunit cydB, P56100 i.e. subunit cydX
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
level of the catalytic subunit, CydA, of the bd oxidase is low in spore extracts derived from the wild type, and is upregulated in a mutant lacking the bcc-aa3 supercomplex, EC 7.1.1.5
brenda
-
level of the catalytic subunit, CydA, of the bd oxidase is low in spore extracts derived from the wild type, and is upregulated in a mutant lacking the bcc-aa3 supercomplex, EC 7.1.1.5
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the cytochrome bd-I complexis concentrated in mobile patches in the plasma membrane
brenda
subnit cydA has nine transmembrane helices with the O2 reactive site near the periplasmic surface. Residue His19, the ligand to the high spin heme b595 component of the oxidase, is located near the periplasmic surface of the protein
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
inactivation of cydA or cydB by gene disruption results in loss of d-heme absorbance at 631 nm. Inactivation of cydA has no effect on the ability of Mycobacterium smegmatis to exit from stationary phase at 37 or 42°C. No discernible growth defect of the mutant is observed under moderately aerobic conditions, while the mutant displays a significant growth disadvantage when cocultured with the wild type under extreme microaerophilia. The cydA mutant displays a competitive growth disadvantage in the presence of the terminal oxidase inhibitor, cyanide, when cocultured with wild type at 21% air saturation in an oxystat
physiological function
inactivation of cydA or cydB gene disruption results in loss of d-heme absorbance at 631 nm
physiological function
-
induction of cytochrome bd helps Salmonella grow and respire in the presence of inhibitory nitric oxide
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 enzyme is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress
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
Q927C3; Q927C4
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
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 bd oxidase functions in controlling electron flux. A mutant lacking the cytochrome bd oxidase shows developmental defects during growth on buffered rich medium plates with glucose as the energy substrate. Cytochrome bd oxidase is essential for the bacterium to grow and complete its developmental cycle under oxygen limitation
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
physiological function
-
the bd oxidase functions in controlling electron flux. A mutant lacking the cytochrome bd oxidase shows developmental defects during growth on buffered rich medium plates with glucose as the energy substrate. Cytochrome bd oxidase is essential for the bacterium to grow and complete its developmental cycle under oxygen limitation
-
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
-
the enzyme is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress
-
physiological function
-
the enzyme contributes to Escherichia coli survival in the mouse bladder
-
Show AA Sequence and Transmembrane Helices (332 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the purified, enzymatically active cytochrome d complex solubilized in Triton X-100 is an alphabeta heterodimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by mycolic acid biosynthesis inhibitors such as isoniazid and especially by drugs targeting oxidative phosphorylation
expression is not induced by inhibitors of protein-, DNA- or RNA synthesis
two- to threefold increase in cydAB gene expression upon reduction of the pO2 of the growth medium from 21 to 0.5% air saturation
expression is induced by mycolic acid biosynthesis inhibitors such as isoniazid and especially by drugs targeting oxidative phosphorylation
B2HQZ0; B2HQY9
expression is induced by mycolic acid biosynthesis inhibitors such as isoniazid and especially by drugs targeting oxidative phosphorylation
-
-
expression is not induced by inhibitors of protein-, DNA- or RNA synthesis
B2HQZ0; B2HQY9
expression is not induced by inhibitors of protein-, DNA- or RNA synthesis
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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
analysis
B2HQZ0; B2HQY9
development of a mCherry-based fluorescent reporter for detection of cytochrome bd expression in Mycobacterium marinum. The expression reporter is suitable for monitoring mycobacterial cytochrome bd expression during mouse macrophage infection and in a zebrafish embryo infection model
analysis
-
development of a mCherry-based fluorescent reporter for detection of cytochrome bd expression in Mycobacterium marinum. The expression reporter is suitable for monitoring mycobacterial cytochrome bd expression during mouse macrophage infection and in a zebrafish embryo infection model
-
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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
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
Kana, B.D.; Weinstein, E.A.; Avarbock, D.; Dawes, S.S.; Rubin, H.; Mizrahi, V.
Characterization of the cydAB-encoded cytochrome bd oxidase from Mycobacterium smegmatis
J. Bacteriol.
183
7076-7086
2001
Mycolicibacterium smegmatis (Q9L8R6), Mycolicibacterium smegmatis (Q9L8R7 and Q9L8R6), Mycolicibacterium smegmatis
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
Acetobacter pasteurianus (S6CX21), Acetobacter pasteurianus (S6D686), Acetobacter pasteurianus 386B (S6CX21), Acetobacter pasteurianus 386B (S6D686), Bacillus subtilis (P94364), Bacillus subtilis (P94365), Bacillus subtilis 168 (P94364), Bacillus subtilis 168 (P94365), Escherichia coli (P0ABJ9), Escherichia coli (P0ABK2), Magnetospirillum fulvum, Pararhodospirillum photometricum, Rhodopseudomonas palustris, Rhodopseudomonas palustris HaA2, Rhodovulum sp. PH10, Rhodovulum sulfidophilum (A0A0D6AXR3)
brenda
Jones-Carson, J.; Husain, M.; Liu, L.; Orlicky, D.J.; Vazquez-Torres, A.
Cytochrome bd-dependent bioenergetics and antinitrosative defenses in Salmonella pathogenesis
mBio
7
e02052-16
2016
Salmonella sp.
brenda
Toyoda, K.; Inui, M.
The extracytoplasmic function sigma factor sigma(C) regulates expression of a branched quinol oxidation pathway in Corynebacterium glutamicum
Mol. Microbiol.
100
486-509
2016
Corynebacterium glutamicum
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
Lu, P.; Heineke, M.H.; Koul, A.; Andries, K.; Cook, G.M.; Lill, H.; van Spanning, R.; Bald, D.
The cytochrome bd-type quinol oxidase is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress
Sci. Rep.
5
10333
2015
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155
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
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 (Q927C3 and Q927C4), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q927C3 and Q927C4)
brenda
Dadashipour, M.; Iwamoto, M.; Hossain, M.; Akutsu, J.; Zhang, Z.; Kawarabayasi, Y.
Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii
J. Bacteriol.
200
e00239-18
2018
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
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
Boot, M.; Jim, K.K.; Liu, T.; Commandeur, S.; Lu, P.; Verboom, T.; Lill, H.; Bitter, W.; Bald, D.
A fluorescence-based reporter for monitoring expression of mycobacterial cytochrome bd in response to antibacterials and during infection
Sci. Rep.
7
10665
2017
Mycobacterium marinum (B2HQZ0 and B2HQY9), Mycobacterium marinum ATCC BAA-535 (B2HQZ0 and B2HQY9)
brenda
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EXTERNAL LINKS (specific for EC-Number 7.1.1.7)
Transporter Classification Database (TCDB): 3.D.4.3.2
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Release 2023.1 (January 2023)
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