Information on EC 1.10.3.10 - ubiquinol oxidase (H+-transporting)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.10.3.10
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RECOMMENDED NAME
GeneOntology No.
ubiquinol oxidase (H+-transporting)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 ubiquinol + O2 + n H+[side 1] = 2 ubiquinone + 2 H2O + n H+[side 2]
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-lactate to cytochrome bo oxidase electron transfer
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glycerol-3-phosphate to cytochrome bo oxidase electron transfer
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NADH to cytochrome bo oxidase electron transfer I
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NADH to cytochrome bo oxidase electron transfer II
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proline to cytochrome bo oxidase electron transfer
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pyruvate to cytochrome bo oxidase electron transfer
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succinate to cytochrome bo oxidase electron transfer
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oxidative phosphorylation
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SYSTEMATIC NAME
IUBMB Comments
ubiquinol:O2 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, while for the bd-II oxidase it is 1. cf. EC 1.10.3.14, ubiquinol oxidase (electrogenic, non H+-transporting).
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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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
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
decylubiquinol + O2 + H+/in
decylubiquinone + H2O + H+/out
show the reaction diagram
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?
duroquinol + O2 + H+/in
duroquinone + H2O + H+/out
show the reaction diagram
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-
?
menaquinol + O2 + H+[side 1]
menaquinone + H2O + H+[side 2]
show the reaction diagram
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?
N,N,N',N'-tetramethylphenylene diamine + O2
?
show the reaction diagram
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?
ubiquinol + O2 + H+/in
ubiquinone + H2O + H+/out
show the reaction diagram
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
ubiquinol-1 + O2
ubiquinone-1 + H2O
show the reaction diagram
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?
ubiquinol-1 + O2 + H+/in
ubiquinone-1 + H2O + H+/out
show the reaction diagram
ubiquinol-1 + O2 + H+[side 1]
ubiquinone-1 + H2O + H+[side 2]
show the reaction diagram
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?
ubiquinol-2 + O2 + H+[side 1]
ubiquinone-2 + H2O + H+[side 2]
show the reaction diagram
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-
?
ubiquinol-8 + O2 + H+/in
ubiquinone-8 + H2O + H+/out
show the reaction diagram
ubiquinol-8 + O2 + H+[side 1]
ubiquinone-8 + H2O + H+[side 2]
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
menaquinol + O2 + H+[side 1]
menaquinone + H2O + H+[side 2]
show the reaction diagram
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?
ubiquinol + O2 + H+[side 1]
ubiquinone + H2O + H+[side 2]
show the reaction diagram
ubiquinol-8 + O2 + H+[side 1]
ubiquinone-8 + H2O + H+[side 2]
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome
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the oxidase contains cytochrome b, cytochrome o
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ubiquinol-8
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ubiquinone-8
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
Cu
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copper-containing enzyme
Fe
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the pure four-subunit enzyme contains two equivalents of iron (19.5 ng/mg)
additional information
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the enzyme contains no zinc. The equivalent of CuA of the aa3-type cytochrome c oxidases is absent in this quinol oxidase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-heptyl-4-hydroxyquinoline N-oxide
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2-n-heptyl-4-hydroxyquinoline N-oxide
AC1-10
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aurachin C1-10
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competitive inhibitor
nitric oxide
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reversible inhibition
Sulfide
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low-micromolar levels of sulfide directly inhibit the proton-pumping cytochrome bo oxidase, but not cytochrome bd oxidase
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphatidyl glycerol
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activates the enzyme with the optimum concentration at 0.04 mg/ml
liponox DCH
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the activity is saturated at 0.01-0.02% (v/v) Liponox DCH
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n-dodecyl octaethyleneglycol monoether
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effective activator
N-lauroylsarcosine
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effective activator
Zwittergent 3-14
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effective activator
additional information
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the enzyme is not activated by sodium cholate, phosphatidyl glycerol, phosphatidyl ethanolamine and soybean phospholipids
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.2
ubiquinol-1
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
300 - 341
ubiquinol-1
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00074
2-heptyl-4-hydroxyquinoline N-oxide
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wild type enzyme, at 37°C, pH 7.0
0.0007
2-n-heptyl-4-hydroxyquinoline N-oxide
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wild type enzyme, at pH 7.0 and 25°C
0.000005
AC1-10
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wild type enzyme, at pH 7.0 and 25°C
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0.000012 - 0.000025
aurachin C1-10
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032
2-n-heptyl-4-hydroxyquinoline N-oxide
Vibrio alginolyticus
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n 25 mM potassium phosphate (pH 7.5), at 30°C
0.0064
KCN
Vibrio alginolyticus
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in 25 mM potassium phosphate (pH 7.5), at 30°C
0.0001
nitric oxide
Escherichia coli
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pH and temperature not specified in the publication
0.005
Sulfide
Escherichia coli
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cytochrome bo oxidase, at pH 7.0 and 25°C
0.0034
ZnSO4
Vibrio alginolyticus
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in 25 mM potassium phosphate (pH 7.5), at 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
960
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at 37°C, pH not specified in the publication
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
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1 * 79000 + 1 * 36000 + 1 * 13000, SDS-PAGE
17000
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1 * 58000 + 1 * 33000 + 1 * 22000 + 1 * 17000, SDS-PAGE
22000
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1 * 58000 + 1 * 33000 + 1 * 22000 + 1 * 17000, SDS-PAGE
33000
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1 * 58000 + 1 * 33000 + 1 * 22000 + 1 * 17000, SDS-PAGE
36000
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1 * 79000 + 1 * 36000 + 1 * 13000, SDS-PAGE
58000
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1 * 58000 + 1 * 33000 + 1 * 22000 + 1 * 17000, SDS-PAGE
79000
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1 * 79000 + 1 * 36000 + 1 * 13000, SDS-PAGE
320000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
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1 * 79000 + 1 * 36000 + 1 * 13000, SDS-PAGE
heterotetramer
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
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hanging drop vapor diffusion method, using 9-10% (w/v) PEG 1500, 100 mM NaCl, 100 mM MgCl2 and 5% (v/v) ethanol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephacel gel filtration, DEAE-5PW gel filtration, and Sephacryl S-300 gel filtration
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DEAE-Sepharose column chromatography
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Ni-NTA column chromatography
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Ni-Sepharose column chromatography
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Ni2+-NTA column chromatography and MonoQ column chromatography
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Ni2+-NTA-agarose column chromatography, gel filtration
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ProBond Ni-IDA column chromatography and Superdex 200 gel filtration
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recombinant C-terminally His6-tagged on subunit II Cyt-bo3 from Escherichia coli strain C43 by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43 BL21(DE3) cells
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expressed in Escherichia coli C43(DE3) cells
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expressed in Escherichia coli RG 129 cells
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expressed in Escherichia coli RG129 cells
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D135E
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the mutant shows 45% activity compared to the wild type enzyme
D135K
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the mutant is deficient in proton pumping (23% activity compared to the wild type enzyme)
D36V
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the mutant of subunit III shows 160% activity compared to the wild type enzyme
D75H
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4% activity compared to the wild type enzyme
D75R
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inactive
E164A
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the mutant of subunit I shows 28% activity compared to the wild type enzyme
E164K
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the mutant of subunit I shows 54% activity compared to the wild type enzyme
E259A
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the mutant of subunit II shows 135% activity compared to the wild type enzyme
E259K
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the mutant of subunit II shows 97% activity compared to the wild type enzyme
E286A
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inactive
E445A
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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
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the mutation affects the CO-binding by the heme-copper binuclear center
F112L
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the mutation does not affect the in vivo activity
F113L
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the mutation does not affect the in vivo activity
F138G
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the mutant shows 63% proton-translocating activity compared to the wild type enzyme
F138R
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the mutant shows 55% proton-translocating activity compared to the wild type enzyme
F165A
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the mutant of subunit I shows 37% activity compared to the wild type enzyme
F208L
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the mutation does not affect the in vivo activity
F295L
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the mutation does not affect the in vivo activity
F29I
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the mutant of subunit III shows 115% activity compared to the wild type enzyme
F336L
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the mutation does not affect the in vivo activity
F347L
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the mutation does not affect the in vivo activity
F348L
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4.8% activity compared to the wild type enzyme
F391L
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the mutation does not affect the in vivo activity
F415W
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the mutation does not affect the in vivo activity
F420L
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the mutation does not affect the in vivo activity
F93A
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the mutant shows 37% activity with ubiquinol-1 and 102% activity with ubiquinol-2 compared to the wild type enzyme
F93Y
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the mutant shows 81% activity with ubiquinol-1 and 107% activity with ubiquinol-2 compared to the wild type enzyme
G132A
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the mutant shows wild type proton-translocation activity (113% activity compared to the wild type enzyme)
G132D/D135N
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the mutant shows 66% proton-translocating activity compared to the wild type enzyme
G132R
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the mutant shows wild type proton-translocation activity
H333C
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nonfunctional enzyme
H333L
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the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
H333N
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nonfunctional enzyme
H333Q
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nonfunctional enzyme
H334L
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the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
H334M
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nonfunctional enzyme
H98S
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2% activity compared to the wild type enzyme
K25L
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the mutant of subunit III shows75 % activity compared to the wild type enzyme
K362D/Dl35K
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the mutant is devoid of redox activity
K362L
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catalytically inactive
K362M
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catalytically inactive
K55Q
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the mutant possesses 100% copper and 73% cytochrome o compared to the wild type enzyme
L160W
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the mutant shows 58% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
L171A
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the mutant of subunit I shows 79% activity compared to the wild type enzyme
M353A
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the mutant shows substantial activity
N124D
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the mutant is deficient in proton pumping (56% activity compared to the wild type enzyme)
N124D/D135N
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the mutant shows 21% proton-translocating activity compared to the wild type enzyme
N124H
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the mutant is deficient in proton pumping (16% activity compared to the wild type enzyme)
N142D
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the mutant is deficient in proton pumping (48% activity compared to the wild type enzyme)
N142D/D135N
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the mutant shows 33% proton-translocating activity compared to the wild type enzyme
N142Q
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the mutant shows wild type proton-translocation activity (109% activity compared to the wild type enzyme)
N142V
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the mutant is deficient in proton pumping (22% activity compared to the wild type enzyme)
N157V
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the mutant shows 23% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
P128A
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the mutant shows wild type proton-translocation activity (115% activity compared to the wild type enzyme)
P128D/D135N
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inactive
P139E/D135N
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the mutant shows 95% proton-translocating activity compared to the wild type enzyme
P358A
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the mutant shows substantial activity
Pl39A
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the mutant shows wild type proton-translocation activity (67% activity compared to the wild type enzyme)
Pl39E
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the mutant shows wild type proton-translocation activity (46% activity compared to the wild type enzyme)
Q101A
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the mutant shows 26% activity with ubiquinol-1 and 82% activity with ubiquinol-2 compared to the wild type enzyme
Q101E
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the mutant shows 55% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
Q101L
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the mutant shows 11% activity with ubiquinol-1 and 58% activity with ubiquinol-2 compared to the wild type enzyme
Q101M
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the mutant shows 51% activity with ubiquinol-1 and 72% activity with ubiquinol-2 compared to the wild type enzyme
Q101T
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the mutant shows 27% activity with ubiquinol-1 and 62% activity with ubiquinol-2 compared to the wild type enzyme
Q167A
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the mutant of subunit I shows 57% activity compared to the wild type enzyme
Q167K
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the mutant of subunit I shows 75% activity compared to the wild type enzyme
Q195L
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the mutant of subunit I shows 119% activity compared to the wild type enzyme
Q82A
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the mutant shows 88% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme
R134P
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the mutant shows 112% proton-translocating activity compared to the wild type enzyme
R176A
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the mutant of subunit III shows 70% activity compared to the wild type enzyme
R257Q
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the mutations specifically eliminates the CuB center from the oxidase complex
R481L
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nonfunctional mutant
R482Q
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the mutant possesses 82% copper and 100% cytochrome o compared to the wild type enzyme
R71D
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inactive
R71D/D75R
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inactive
R71K
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inactive
R71L
the mutation inhibits activity by 99%
R80Q
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the mutation causes loss of a diagnostic peak for low-spin heme b in the 77 K redox difference spectrum
S177A
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the mutant of subunit I shows 91% activity compared to the wild type enzyme
T168A
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the mutant of subunit I shows 118% activity compared to the wild type enzyme
T247V
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the mutant of subunit I shows 173% activity compared to the wild type enzyme
T352A
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catalytically inactive
T352N
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the mutant shows substantial activity
T352S
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the mutant shows substantial activity
T359A
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catalytically inactive
T359S
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the mutant shows almost wild type activity
W136A
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the mutant of subunit II shows 89% activity compared to the wild type enzyme
W136K
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the mutant of subunit II shows 105% activity compared to the wild type enzyme
W147L
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the mutation does not affect the in vivo activity
W156A
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the mutant of subunit III shows 70% activity compared to the wild type enzyme
W280L
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67% activity compared to the wild type enzyme
W282F
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the mutation does not affect the in vivo activity
W331L
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19% activity compared to the wild type enzyme
Y173F
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the mutant possesses 91% copper and 108% cytochrome o compared to the wild type enzyme
Y288F
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the mutations specifically eliminates the CuB center from the oxidase complex
Y288L
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0.3% activity compared to the wild type enzyme
Y61F
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the mutation does not affect the in vivo activity
E286C
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the mutant shows 3% activity compared to the wild type enzyme as a result of the inhibition of proton transfer from the D-channel
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D135N
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the mutant shows 45% activity compared to the wild type enzyme, with proton pumping decoupled from the electron-transfer activity
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D256N
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the mutant shows 25% activity compared to the wild type enzyme
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D407N
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the mutant shows 31% activity compared to the wild type enzyme
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E286A
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inactive
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E286Q
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the mutant shows 69% activity compared to the wild type enzyme
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K362M
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catalytically inactive
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K362Q
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catalytically inactive
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T352A
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catalytically inactive
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T352N
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the mutant shows substantial activity
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T359A
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catalytically inactive
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H333C
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nonfunctional enzyme
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H333L
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the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
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H333N
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nonfunctional enzyme
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H333Q
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nonfunctional enzyme
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H334L
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the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme
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E286A
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inactive
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E286D
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the mutant retains 31% of the wild type activity
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E286Q
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the mutant shows 4% activity compared to the wild type enzyme and is unable to bind azide ions
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F113L
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the mutation does not affect the in vivo activity
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F295L
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the mutation does not affect the in vivo activity
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F347L
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the mutation does not affect the in vivo activity
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F420L
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the mutation does not affect the in vivo activity
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Y61F
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the mutation does not affect the in vivo activity
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E445A
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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
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D407N
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the mutation affects the CO-binding by the heme-copper binuclear center
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E286Q
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the mutations specifically eliminates the CuB center from the oxidase complex
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K55Q
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the mutant possesses 100% copper and 73% cytochrome o compared to the wild type enzyme
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R80Q
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the mutation causes loss of a diagnostic peak for low-spin heme b in the 77 K redox difference spectrum
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Y173F
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the mutant possesses 91% copper and 108% cytochrome o compared to the wild type enzyme
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additional information
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (833 entries)
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