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2 ubiquinol + n H+ + O2
2 ubiquinone + n H+ + 2 H2O
-
-
-
?
decylubiquinol + O2 + H+/in
decylubiquinone + H2O + H+/out
-
-
-
-
?
duroquinol + O2 + H+/in
duroquinone + H2O + H+/out
-
-
-
-
?
menaquinol + O2 + H+[side 1]
menaquinone + H2O + H+[side 2]
-
-
-
-
?
N,N,N',N'-tetramethylphenylene diamine + O2
?
-
-
-
-
?
ubiquinol + O2 + H+/in
ubiquinone + H2O + H+/out
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
ubiquinol-1 + O2 + H+[side 1]
ubiquinone-1 + H2O + H+[side 2]
ubiquinol-2 + O2 + H+[side 1]
ubiquinone-2 + H2O + H+[side 2]
-
-
-
-
?
ubiquinol-8 + O2 + H+/in
ubiquinone-8 + H2O + H+/out
ubiquinol-8 + O2 + H+[side 1]
ubiquinone-8 + H2O + H+[side 2]
-
-
-
-
?
additional information
?
-
ubiquinol + O2 + H+/in
ubiquinone + H2O + H+/out
-
-
-
-
?
ubiquinol + O2 + H+/in
ubiquinone + H2O + H+/out
-
-
-
-
?
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-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
-
-
-
-
?
ubiquinol-1 + O2 + H+[side 1]
ubiquinone-1 + H2O + H+[side 2]
-
-
-
-
?
ubiquinol-1 + O2 + H+[side 1]
ubiquinone-1 + H2O + H+[side 2]
-
-
-
-
?
ubiquinol-8 + O2 + H+/in
ubiquinone-8 + H2O + H+/out
-
-
-
-
?
ubiquinol-8 + O2 + H+/in
ubiquinone-8 + 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
-
-
?
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
?
-
-
a significant interaction is observed only between Vitreoscilla hemoglobin and subunit I of cytochrome bo
-
-
?
additional information
?
-
-
the enzyme does not interact with cytochrome c
-
-
?
additional information
?
-
-
a significant interaction is observed only between Vitreoscilla hemoglobin and subunit I of cytochrome bo
-
-
?
additional information
?
-
-
horse heart reduced cytochrome c is not oxidized by this enzyme
-
-
?
additional information
?
-
-
a significant interaction is observed only between Vitreoscilla hemoglobin and subunit I of cytochrome bo
-
-
?
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Colitis
Epithelial-Derived Reactive Oxygen Species Enable AppBCX-Mediated Aerobic Respiration of Escherichia coli during Intestinal Inflammation.
Infections
A fluorescence-based reporter for monitoring expression of mycobacterial cytochrome bd in response to antibacterials and during infection.
Infections
Arylvinylpiperazine Amides, a New Class of Potent Inhibitors Targeting QcrB of Mycobacterium tuberculosis.
Infections
Cytochrome bd in Mycobacterium tuberculosis: A respiratory chain protein involved in the defense against antibacterials.
Infections
Cytochrome bd Protects Bacteria against Oxidative and Nitrosative Stress: A Potential Target for Next-Generation Antimicrobial Agents.
Infections
Exploiting the synthetic lethality between terminal respiratory oxidases to kill Mycobacterium tuberculosis and clear host infection.
Infections
Redox control of fast ligand dissociation from Escherichia coli cytochrome bd.
Infections
Respiratory Heterogeneity Shapes Biofilm Formation and Host Colonization in Uropathogenic Escherichia coli.
Infections
The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB.
Persistent Infection
Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration.
Trypanosomiasis, African
Three redox states of trypanosoma brucei alternative oxidase identified by infrared spectroscopy and electrochemistry.
Tuberculosis
A fluorescence-based reporter for monitoring expression of mycobacterial cytochrome bd in response to antibacterials and during infection.
Tuberculosis
A Mycobacterium tuberculosis cytochrome bd oxidase mutant is hypersensitive to bedaquiline.
Tuberculosis
Arylvinylpiperazine Amides, a New Class of Potent Inhibitors Targeting QcrB of Mycobacterium tuberculosis.
Tuberculosis
Carbon metabolism modulates the efficacy of drugs targeting the cytochrome bc1:aa3 in Mycobacterium tuberculosis.
Tuberculosis
Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration.
Tuberculosis
Cytochrome bd in Mycobacterium tuberculosis: A respiratory chain protein involved in the defense against antibacterials.
Tuberculosis
Cytochrome bd oxidase and hydrogen peroxide resistance in Mycobacterium tuberculosis.
Tuberculosis
Dual inhibition of the terminal oxidases eradicates antibiotic-tolerant Mycobacterium tuberculosis.
Tuberculosis
Exploiting the synthetic lethality between terminal respiratory oxidases to kill Mycobacterium tuberculosis and clear host infection.
Tuberculosis
Features and Functional Importance of Key Residues of the Mycobacterium tuberculosis Cytochrome bd Oxidase.
Tuberculosis
Host immunity increases Mycobacterium tuberculosis reliance on cytochrome bd oxidase.
Tuberculosis
Identification of 4-Amino-Thieno[2,3-d]Pyrimidines as QcrB Inhibitors in Mycobacterium tuberculosis.
Tuberculosis
Pyrrolo[3,4-c]pyridine-1,3(2H)-diones: A Novel Antimycobacterial Class Targeting Mycobacterial Respiration.
Tuberculosis
Structure guided generation of thieno[3,2-d]pyrimidin-4-amine Mycobacterium tuberculosis bd oxidase inhibitors.
Tuberculosis
Susceptibility of Mycobacterium tuberculosis Cytochrome bd Oxidase Mutants to Compounds Targeting the Terminal Respiratory Oxidase, Cytochrome c.
Tuberculosis
The anti-mycobacterial activity of the cytochrome bcc inhibitor Q203 can be enhanced by small-molecule inhibition of cytochrome bd.
Tuberculosis
The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB.
Tuberculosis
The cytochrome bd-type quinol oxidase is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress.
ubiquinol oxidase (h+-transporting) deficiency
Cytochrome bd promotes Escherichia coli biofilm antibiotic tolerance by regulating accumulation of noxious chemicals.
Urinary Tract Infections
Respiratory Heterogeneity Shapes Biofilm Formation and Host Colonization in Uropathogenic Escherichia coli.
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0.015
ubiquinol-1
-
mutant enzyme D36V, at pH 7.0 and 25°C
0.016
ubiquinol-1
-
mutant enzyme D75E, at pH 7.0 and 25°C
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
0.02
ubiquinol-1
-
mutant enzyme E164A, at pH 7.0 and 25°C
0.021
ubiquinol-1
-
mutant enzyme T247V, at pH 7.0 and 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
0.024
ubiquinol-1
-
mutant enzyme Q101M, at pH 7.0 and 25°C
0.026
ubiquinol-1
-
mutant enzyme Q167K, at pH 7.0 and 25°C
0.027
ubiquinol-1
-
mutant enzyme E259A, at pH 7.0 and 25°C
0.027
ubiquinol-1
-
mutant enzyme E259K, at pH 7.0 and 25°C
0.027
ubiquinol-1
-
mutant enzyme Q167A, at pH 7.0 and 25°C
0.03
ubiquinol-1
-
mutant enzyme L160W, at pH 7.0 and 25°C
0.03
ubiquinol-1
-
mutant enzyme Q101A, at pH 7.0 and 25°C
0.031
ubiquinol-1
-
mutant enzyme T168A, at pH 7.0 and 25°C
0.032
ubiquinol-1
-
mutant enzyme S177A, at pH 7.0 and 25°C
0.033
ubiquinol-1
-
mutant enzyme F165A, at pH 7.0 and 25°C
0.033
ubiquinol-1
-
mutant enzyme W136A, at pH 7.0 and 25°C
0.039
ubiquinol-1
-
mutant enzyme W136K, at pH 7.0 and 25°C
0.042
ubiquinol-1
-
mutant enzyme L171A, at pH 7.0 and 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
0.045
ubiquinol-1
-
mutant enzyme Q82A, at pH 7.0 and 25°C
0.046
ubiquinol-1
-
mutant enzyme E164K, at pH 7.0 and 25°C
0.05
ubiquinol-1
-
wild type enzyme, at pH 7.0 and 25°C
0.052
ubiquinol-1
-
mutant enzyme D188N, at 37°C, pH 7.0
0.053
ubiquinol-1
-
wild type enzyme, at 37°C, pH 7.0
0.056
ubiquinol-1
-
mutant enzyme D188A, at 37°C, pH 7.0
0.06
ubiquinol-1
-
mutant enzyme R257Q, at 37°C, pH 7.0
0.067
ubiquinol-1
-
mutant enzyme Q195L, at pH 7.0 and 25°C
0.072
ubiquinol-1
-
mutant enzyme F93Y, at pH 7.0 and 25°C
0.072
ubiquinol-1
-
mutant enzyme Q101N, at pH 7.0 and 25°C
0.091
ubiquinol-1
-
mutant enzyme F93A, at pH 7.0 and 25°C
0.1
ubiquinol-1
-
mutant enzyme N157V, at pH 7.0 and 25°C
0.124
ubiquinol-1
-
mutant enzyme Q101E, at pH 7.0 and 25°C
0.141
ubiquinol-1
-
mutant enzyme Q101L, at pH 7.0 and 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
0.2
ubiquinol-1
-
mutant enzyme Q101T, at pH 7.0 and 25°C
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metabolism
-
Gluconobacter oxydans oxidizes a variety of substrates in the periplasm by membrane-bound dehydrogenases, which transfer the reducing equivalents to ubiquinone. Two quinol oxidases, cytochrome bo3 and cytochrome bd, then catalyze transfer of the electrons from ubiquinol to molecular oxygen
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
malfunction
-
deletion of the cydAB genes for cytochrome bd has no obvious influence on growth, whereas the lack of the cyoBACD genes for cytochrome bo3 severely reduced the growth rate and the cell yield
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
-
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 bo-type ubiquinol oxidase is functioning as a proton pump
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
-
cytochrome bo3 might be a rate-limiting factor of the respiratory chain
physiological function
-
the enzyme contributes to oxidative stress resistance and dioxygen tolerance
physiological function
-
the enzyme is important during murine infection, required for the intracellular growth in air, essential for aerobic respiration and intracellular replication and confers resistance to reactive nitrogen species
physiological function
-
the enzyme is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress
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
-
overexpression of cytochrome c ScyA facilitates growth despite nitrite inhibition by enhancing nitrite resistance of the cbb3 oxidase. ScyA either increases electron flow to the cbb3 oxidase;, or ScyA promotes nitrite resistance of the cbb3 oxidase, possibly by direct interaction
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
-
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 bd-II-mediated quinol oxidation prevents the accumulation of NADH, whereas GABA synthesis/antiport maintains the proton motive force for ATP production
-
physiological function
-
the enzyme contributes to oxidative stress resistance and dioxygen tolerance
-
physiological function
-
the enzyme is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress
-
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
-
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D135E
-
the mutant shows 45% activity compared to the wild type enzyme
D135K
-
the mutant is deficient in proton pumping (23% activity compared to the wild type enzyme)
D36V
-
the mutant of subunit III shows 160% activity compared to the wild type enzyme
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
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
F112L
-
the mutation does not affect the in vivo activity
F113L
-
the mutation does not affect the in vivo activity
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
F208L
-
the mutation does not affect the in vivo activity
F295L
-
the mutation does not affect the in vivo activity
F29I
-
the mutant of subunit III shows 115% activity compared to the wild type enzyme
F336L
-
the mutation does not affect the in vivo activity
F347L
-
the mutation does not affect the in vivo activity
F348L
-
4.8% activity compared to the wild type enzyme
F391L
-
the mutation does not affect the in vivo activity
F415W
-
the mutation does not affect the in vivo activity
F420L
-
the mutation does not affect the in vivo activity
F93A
-
the mutant shows 37% activity with ubiquinol-1 and 102% activity with ubiquinol-2 compared to the wild type enzyme
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
G132R
-
the mutant shows wild type proton-translocation activity
H333C
-
nonfunctional enzyme
H333L
-
the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
H333N
-
nonfunctional enzyme
H333Q
-
nonfunctional enzyme
H334L
-
the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
H334M
-
nonfunctional enzyme
H98F
mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials
H98S
-
2% activity compared to the wild type enzyme
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
K362D/Dl35K
-
the mutant is devoid of redox activity
K362L
-
catalytically inactive
K362M
-
catalytically inactive
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
M353A
-
the mutant shows substantial activity
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
P358A
-
the mutant shows substantial activity
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)
Q101E
-
the mutant shows 55% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
Q101M
-
the mutant shows 51% activity with ubiquinol-1 and 72% activity with ubiquinol-2 compared to the wild type enzyme
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
R481L
-
nonfunctional mutant
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
R71L
the mutation inhibits activity by 99%
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
T352A
-
catalytically inactive
T352N
-
the mutant shows substantial activity
T352S
-
the mutant shows substantial activity
T359A
-
catalytically inactive
T359S
-
the mutant shows almost wild type activity
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
W147L
-
the mutation does not affect the in vivo activity
W156A
-
the mutant of subunit III shows 70% activity compared to the wild type enzyme
W280L
-
67% activity compared to the wild type enzyme
W282F
-
the mutation does not affect the in vivo activity
W331L
-
19% 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
Y288L
-
0.3% activity compared to the wild type enzyme
Y61F
-
the mutation does not affect the in vivo activity
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
-
D135N
-
the mutant shows 45% activity compared to the wild type enzyme, with proton pumping decoupled from the electron-transfer activity
-
D256N
-
the mutant shows 25% activity compared to the wild type enzyme
-
D407N
-
the mutant shows 31% activity compared to the wild type enzyme
-
E286Q
-
the mutant shows 69% activity compared to the wild type enzyme
-
K362M
-
catalytically inactive
-
K362Q
-
catalytically inactive
-
T352A
-
catalytically inactive
-
T352N
-
the mutant shows substantial activity
-
T359A
-
catalytically inactive
-
H333C
-
nonfunctional enzyme
-
H333L
-
the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
-
H333N
-
nonfunctional enzyme
-
H333Q
-
nonfunctional enzyme
-
H334L
-
the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
-
E286D
-
the mutant retains 31% of the wild type activity
-
E286Q
-
the mutant shows 4% activity compared to the wild type enzyme and is unable to bind azide ions
-
F113L
-
the mutation does not affect the in vivo activity
-
F295L
-
the mutation does not affect the in vivo activity
-
F347L
-
the mutation does not affect the in vivo activity
-
F420L
-
the mutation does not affect the in vivo activity
-
Y61F
-
the mutation does not affect the in vivo activity
-
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
-
D407N
-
the mutation affects the CO-binding by the heme-copper binuclear center
-
E286Q
-
the mutations specifically eliminates the CuB center from the oxidase complex
-
K55Q
-
the mutant possesses 100% copper and 73% cytochrome o compared to the wild type enzyme
-
R80Q
-
the mutation causes loss of a diagnostic peak for low-spin heme b in the 77 K redox difference spectrum
-
Y173F
-
the mutant possesses 91% copper and 108% cytochrome o compared to the wild type enzyme
-
additional information
-
plasmid-based overexpression of cyoBACD leads to increased growth rates and growth yields, both in the wild-type and the DELTAcyoBACD mutant, suggesting that cytochrome bo3 might be a rate-limiting factor of the respiratory chain
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
D188N
-
the mutant shows 53% activity compared to the wild type enzyme
D256N
-
the mutant possesses 103% copper and 74% cytochrome o compared to the wild type enzyme
D256N
-
the mutant shows 25% activity compared to the wild type enzyme
D407N
-
the mutant shows 31% activity compared to the wild type enzyme
D407N
-
the mutation affects the CO-binding by the heme-copper binuclear center
D75E
-
135% activity compared to the wild type enzyme
D75E
-
the mutant shows 48% activity with ubiquinol-1 and 88% activity with ubiquinol-2 compared to the wild type enzyme
D75H
-
4% activity compared to the wild type enzyme
D75H
mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials
D75N
-
inactive
D75N
the mutation inhibits activity by 99%
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
E286D
-
the mutant retains 31% of the wild type activity
E286Q
-
the mutant shows 4% activity compared to the wild type enzyme and is unable to bind azide ions
E286Q
-
the mutant shows 69% activity compared to the wild type enzyme
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
-
1% activity compared to the wild type enzyme
H98N
the mutation inhibits activity by 97%
H98N
-
the mutant shows 3% activity with ubiquinol-1 and 10% activity with ubiquinol-2 compared to the wild type enzyme
H98T
-
1% activity 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
-
catalytically inactive
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
-
5% activity compared to the wild type enzyme
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 is fully functional
R481Q
-
the mutant possesses 91% copper and 73% cytochrome o compared to the wild type enzyme
R71Q
-
inactive
R71Q
the mutation inhibits activity by 99%
R71Q
-
the mutant shows 3% activity with ubiquinol-1 and 8% activity with ubiquinol-2 compared to the wild type enzyme
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