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2-heptyl-4-hydroxyquinoline N-oxide
-
i.e. HQNO, binds stoichiometrically to the enzyme and prevents formation of the ubisemiquinone at the QH-site, but does not displace the ubiquinone-8 bound at the QH-site, enzyme binding kineticss, overview
2-Heptyl-4-hydroxyquinoline-N-oxide
-
2-hydroxybenzhydroxamic acid
-
competitive inhibitor towards ubiquinol
5-chloro-3-[(2E)-3,7-dimethylocta-2,6-dienyl]-2,4-dihydroxy-6-methylbenzaldehyde
an ascofuranone derivative
5-chloro-3-[(2E,6E)-8-hydroxy-3,7-dimethylnona-2,6-dienyl]-2,4-dihydroxy-6-methylbenzaldehyde
an ascofuranone derivative
antimycin A
56% residual activity at 0.005 mg/ml; 56% residual activity at 0.005 mg/ml
aurachin C 1-10
15% residual activity at 0.005 mg/ml; 15% residual activity at 0.005 mg/ml
aurachin C1-10
-
prevents formation of the ubisemiquinone at the QH-site, but appears to compete for quinol binding at the QL-site, enzyme binding kineticss, overview
aurachin D
16% residual activity at 0.005 mg/ml; 16% residual activity at 0.005 mg/ml
Gramicidin S
67% residual activity at 0.005 mg/ml; 67% residual activity at 0.005 mg/ml
LL-Z1272gamma
69% residual activity at 0.005 mg/ml; 69% residual activity at 0.005 mg/ml
Piericidin A
14% residual activity at 0.005 mg/ml; 14% residual activity at 0.005 mg/ml
Salicylhydroxamic acid
-
-
ubiquinol-1
-
substrate inhibition
ubiquinol-2
-
substrate inhibition
ubiquinone-1
-
product inhibition, an excess amount of ubiquinol-2 is unable to suppress product inhibition with ubiquinone-1 therefore, the inhibition mode may not be competitive
ubiquinone-2
-
product inhibition
ascofuranone

-
almost complete inhibition at 10 nM
ascofuranone
-
almost complete inhibition at 10 nM
ascofuranone
an antibiotic
ascofuranone
-
specifically inhibits the quinol oxidase activity of TAO
cyanide

-
cyanide
quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration; quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration
n-octyl gallate

-
the enzyme is fully sensitive to 0.001 mM octyl gallate
n-octyl gallate
-
the enzyme is fully sensitive to 0.001 mM octyl gallate
n-propyl gallate

-
-
octyl gallate

-
-
ubiquinol

-
AOX is inactivated by its product ubiquinol during catalysis, this inhibition is prevented in the presence of pyruvate. The inhibition can be reversed by a reductive process, achieved by high levels of reduction of the ubiquinone-pool or by dithiothreitol
ubiquinol
-
AOX is inactivated by its product ubiquinol during catalysis, this inhibition is prevented in the presence of pyruvate. The inhibition can be reversed by a reductive process, achieved by high levels of reduction of the ubiquinone-pool or by dithiothreitol
additional information

-
the enzyme is cyanide- and antimycin-resistant
-
additional information
-
not inhibited by cyanide
-
additional information
-
presence of high affinity inhibitors, 2-heptyl-4-hydroxyquinoline N-oxide and aurachin C1ā10, does not displace ubiquinone-8 from the QH site
-
additional information
-
not inhibited by ascofuranone; not inhibited by ascofuranone
-
additional information
not inhibited by ascofuranone; not inhibited by ascofuranone
-
additional information
-
CIO activity is much more resistant to cyanide, compared with Escherichia coli cytochrome bd, but sensitive to azide
-
additional information
-
not inhibited by myxothiazol
-
additional information
-
insensitive to cyanide
-
additional information
-
the respiratory activity exhibited by mitochondria containing the wild type AOX is partially resistant to antimycin A (about 18% of the NADH-dependent rate)
-
additional information
-
the enzyme is cyanide- and antimycin-resistant
-
additional information
inhibitor binding induces the ligation of a histidine residue in the active site, inhibitor binding site and structures, overview
-
additional information
-
inhibitor binding induces the ligation of a histidine residue in the active site, inhibitor binding site and structures, overview
-
additional information
-
insensitive to cyanide
-
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0.013
2-Heptyl-4-hydroxyquinoline-N-oxide
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5)
0.00000048
5-chloro-3-[(2E,6E)-8-hydroxy-3,7-dimethylnona-2,6-dienyl]-2,4-dihydroxy-6-methylbenzaldehyde
Trypanosoma brucei
pH and temperature not specified in the publication
0.017
antimycin A
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5)
0.00004
aurachin C 1-10
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5)
0.82
azide
Gluconobacter oxydans
-
pH 6.5, 25°C
0.04
Gramicidin S
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5)
0.013
LL-Z1272gamma
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5)
0.00007 - 0.0001
octyl gallate
0.0007
Piericidin A
Gluconobacter oxydans
at 25°C in 50 mM potassium phosphate (pH 6.5)
0.00036 - 0.00044
propyl gallate
0.042 - 0.194
Salicylhydroxamic acid
0.008
cyanide

Gluconobacter oxydans
quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration with the IC50 of 0.008 mM (relative amplitude, 21%) and 0.013 mM (79%), at 25°C in 50 mM potassium phosphate (pH 6.5)
13
cyanide
Gluconobacter oxydans
quinol oxidase activity of the membranes from the wild type shows a biphasic dependence on the cyanide concentration with the IC50 of 0.008 mM (relative amplitude, 21%) and 13 mM (79%), at 25°C in 50 mM potassium phosphate (pH 6.5)
0.00007
octyl gallate

Sauromatum venosum
mutant Y299F, pH and temperature not specified in the publication
0.00008
octyl gallate
Sauromatum venosum
mutants C172A and T179A, pH and temperature not specified in the publication
0.00009
octyl gallate
Sauromatum venosum
wild-type enzyme, pH and temperature not specified in the publication
0.0001
octyl gallate
Sauromatum venosum
mutant Y253F, pH and temperature not specified in the publication
0.00036
propyl gallate

Arabidopsis thaliana
-
mutant enzyme F215L, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.00039
propyl gallate
Arabidopsis thaliana
-
mutant enzyme M219V, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.00039
propyl gallate
Arabidopsis thaliana
-
wild type enzyme, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.00042
propyl gallate
Arabidopsis thaliana
-
mutant enzyme M219I, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.00044
propyl gallate
Arabidopsis thaliana
-
mutant enzyme G303E, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.042
Salicylhydroxamic acid

Arabidopsis thaliana
-
wild type enzyme, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.057
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme M219I, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.069
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme F215L, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.073
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme M219V, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.194
Salicylhydroxamic acid
Arabidopsis thaliana
-
mutant enzyme G303E, in 50 mM potassium phosphate, 10 mM KCl, 5 mM MgCl , 1 mM 2 EDTA, 5 mM pyruvate, pH 7.0, at 25°C
0.012
sialic acid

Sauromatum venosum
mutant T179A, pH and temperature not specified in the publication
0.016
sialic acid
Sauromatum venosum
wild-type enzyme, pH and temperature not specified in the publication
0.018
sialic acid
Sauromatum venosum
mutant Y299F, pH and temperature not specified in the publication
0.019
sialic acid
Sauromatum venosum
mutant C172A, pH and temperature not specified in the publication
0.02
sialic acid
Sauromatum venosum
mutant Y253F, pH and temperature not specified in the publication
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malfunction
-
transgenic plant cells lacking mitochondrial alternative oxidase have increased susceptibility to mitochondria-dependent and -independent pathways of programmed cell death and show higher sensitivity to treatment with hydrogen peroxide, salicylic acid and cantharidin as compared to the wild type enzyme
evolution

the cytochrome ba3 oxidase belongs to the family B of the heme-copper containing terminal oxidases, heme-copper oxidases use either c-type cytochromes or quinols as electron donors
evolution
-
the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis
evolution
the enzyme is found in mitochondria of all higher plants studied to date
evolution
-
the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis
metabolism

-
the alternative oxidase actively competes with the cytochrome pathway for reducing equivalents and contributes up to 24% to the overall respiratory activity
metabolism
-
alternative oxidase is a key enzyme for cyanide-resistant respiration
physiological function

-
AppBC alleviates the accumulation of electrons in the quinone pool during respiratory stress via electroneutral ubiquinol oxidation
physiological function
AOX is a diiron carboxylate protein that catalyzes the four-electron reduction of dioxygen to water by ubiquinol. AOX plays a critical role in the survival of the parasite in its bloodstream form
physiological function
-
cytochrome bo3 oxidase catalyzes the 2-electron oxidation of ubiquinol-8 and the 4-electron reduction of dioxygen to water
physiological function
the alternative oxidase (AOX) is a non-protonmotive ubiquinol oxidase
physiological function
-
ubiquinol-10 molecules are reoxidized by cytochrome bo3 and CIO, terminal oxidases of the respiratory chain. In the Gluconobacter oxydans respiratory chain, CIO may have a physiological role in compensation for lower activity of cytochrome bo3 under low growth pH to maintain rapid substrate oxidation
physiological function
-
enzyme signaling regulates the greening process
physiological function
-
plastid signals enhance plant cold stress tolerance mainly through the induction of the gene AOX1a
physiological function
-
the alternative oxidase pathway plays an important role in the sodium nitroprusside-elevated resistance of Medicago to salt stress
physiological function
-
the enzyme is central for metabolic heat-production
physiological function
the enzyme is required for the N gene-mediated resistance to Tobacco mosaic virus
physiological function
-
the expression of AOX1a in Saccharomyces cerevisiae enhances its respiratory tolerance which, in turn, maintains cellular redox homeostasis and protects from oxidative damage
physiological function
-
ubiquinol-10 molecules are reoxidized by cytochrome bo3 and CIO, terminal oxidases of the respiratory chain. In the Gluconobacter oxydans respiratory chain, CIO may have a physiological role in compensation for lower activity of cytochrome bo3 under low growth pH to maintain rapid substrate oxidation
physiological function
-
AppBC alleviates the accumulation of electrons in the quinone pool during respiratory stress via electroneutral ubiquinol oxidation
additional information

-
analysis of a one-site Q-site model and a two-site Q-site model, overview
additional information
putative ubiquinol binding cavities, overview. The nonheme diiron carboxylate active site is buried within a four-helix bundle. The active site is ligated solely by four glutamate residues in its oxidized inhibitor-free state. Highly conserved Tyr220 iswithin 4 A of the active site and is critical for catalytic activity. The enzyme is a homodimer with two hydrophobic cavities per monomer. Both cavities bind ubiquinol and along with Tyr220 are required for the catalytic cycle for O2 reduction, but also inhibitors bind to one cavity and Tyr220, respectively. A second cavity interacts with the inhibitor-binding cavity at the diiron center. The active site, which is located in a hydrophobic environment deep inside the enzyme molecule, is composed of the diiron center and four glutamate (E123, E162, E213, and E266) and two histidine residues (H165 and H269), all of which are completely conserved
additional information
-
putative ubiquinol binding cavities, overview. The nonheme diiron carboxylate active site is buried within a four-helix bundle. The active site is ligated solely by four glutamate residues in its oxidized inhibitor-free state. Highly conserved Tyr220 iswithin 4 A of the active site and is critical for catalytic activity. The enzyme is a homodimer with two hydrophobic cavities per monomer. Both cavities bind ubiquinol and along with Tyr220 are required for the catalytic cycle for O2 reduction, but also inhibitors bind to one cavity and Tyr220, respectively. A second cavity interacts with the inhibitor-binding cavity at the diiron center. The active site, which is located in a hydrophobic environment deep inside the enzyme molecule, is composed of the diiron center and four glutamate (E123, E162, E213, and E266) and two histidine residues (H165 and H269), all of which are completely conserved
additional information
the enzyme can be reduced by ubiquinol, but it alone can also be reduced by decylubiquinol and N,N,N',N'-tetramethyl-4-phenylenediamine/ascorbate in the presence of cyanide
additional information
-
the enzyme can be reduced by ubiquinol, but it alone can also be reduced by decylubiquinol and N,N,N',N'-tetramethyl-4-phenylenediamine/ascorbate in the presence of cyanide
additional information
-
the purified CIO shows an extraordinary high ubiquinol-1 oxidase activity. The enzyme shows a modified ping-pong bi-bi mechanism
additional information
-
the purified CIO shows an extraordinary high ubiquinol-1 oxidase activity. The enzyme shows a modified ping-pong bi-bi mechanism
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C127S
-
the substitution prevents oxidative inactivation of alternative oxidase and renders the protein insensitive to pyruvate activation, the mutated protein is instead activated specifically by succinate
C78A
-
the mutant shows significant (418%) stimulation by 5 mM succinate and little response to 5 mM pyruvate
C78D
-
the mutant is significantly stimulated (28%) by 5 mM succinate, pyruvate has no significant effect on the mutant enzyme activity
C78E
-
the mutant is significantly stimulated (37%) by 5 mM succinate
C78K
-
the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
C78R
-
the mutant is insensitive to pyruvate or succinate but more active than the wild type without pyruvate
C78S
-
the mutant is significantly (489%) stimulated by 5 mM succinate
F215L
-
the mutant exhibits 1.6fold resistance to salicylhydroxamic acid compared to the wild type enzyme
G303E
-
the mutant exhibits 4.6fold resistance to salicylhydroxamic acid compared to the wild type enzyme
M219I
-
the mutant exhibits 1.4fold resistance to salicylhydroxamic acid compared to the wild type enzyme
M219V
-
the mutant exhibits 1.7fold resistance to salicylhydroxamic acid compared to the wild type enzyme
D188A
-
site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme, The mutant oxidase is not able to support aerobic growth when expressed in a strain of Escherichia coli without a genomically encoded respiratory oxidase
D188N
-
site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme
D75E
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows similar activity compared to the wild-type enzyme
D75H
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
D75N
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
D75R
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
H98N
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
H98T
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
Q101N
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R257Q
-
site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme. The mutant oxidase is not able to support aerobic growth when expressed in a strain of Escherichia coli without a genomically encoded respiratory oxidase
R71D
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71D/D75R
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71K
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
R71Q
-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
WI36A
-
site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme
C99S
-
the substitution prevents oxidative inactivation of alternative oxidase and renders the protein insensitive to pyruvate activation, the mutated protein is instead activated specifically by succinate
C172A
site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme
E217A
-
the mutation results in the loss of AOX activity
E270N
-
the mutation results in the loss of AOX activity
T179A
site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme
W206F
site-directed mutagenesis, inactive mutant
W206Y
site-directed mutagenesis, inactive mutant
Y275F
-
the mutant exhibits barely detectable mitochondrial antimycin-resistant respiratory activity
Y299F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H261A
-
the mutant shows 5% activity compared to the wild type enzyme
N247Q
-
the mutant shows 96% activity compared to the wild type enzyme
Q242N
-
the mutant shows 6% activity compared to the wild type enzyme
R262K
-
the mutant shows 6% activity compared to the wild type enzyme
S256T
-
the mutant shows 7% activity compared to the wild type enzyme
Y253A
-
the mutant shows 28% activity compared to the wild type enzyme
Y253F
-
the mutant shows 61% activity compared to the wild type enzyme
H261A
-
the mutant shows 5% activity compared to the wild type enzyme
N247Q
-
the mutant shows 96% activity compared to the wild type enzyme
Q242N
-
the mutant shows 6% activity compared to the wild type enzyme
Y253A
-
the mutant shows 28% activity compared to the wild type enzyme
Y253F
-
the mutant shows 61% activity compared to the wild type enzyme
A216L
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
A216N
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
E213A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
E215A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
L122A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
L122N
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
R118A
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
R118Q
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
T219V
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
Y220F
site-directed mutagenesis, the mutation results in almost complete loss of ubiquinol oxidizing activity
Y246A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H98S

-
site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme
H98S
-
site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-100 compared to the wild-type enzyme
Y253F

site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y253F
-
the mutant exhibits a mitochondrial antimycin-resistant respiratory activity that is comparable with that of the wild type
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Kido, Y.; Shiba, T.; Inaoka, D.K.; Sakamoto, K.; Nara, T.; Aoki, T.; Honma, T.; Tanaka, A.; Inoue, M.; Matsuoka, S.; Moore, A.; Harada, S.; Kita, K.
Crystallization and preliminary crystallographic analysis of cyanide-insensitive alternative oxidase from Trypanosoma brucei brucei
Acta Crystallogr. Sect. F
66
275-278
2010
Trypanosoma brucei brucei, Trypanosoma brucei brucei FN102
brenda
Hoefnagel, M.H.; Wiskich, J.T.
Activation of the plant alternative oxidase by high reduction levels of the Q-pool and pyruvate
Arch. Biochem. Biophys.
355
262-270
1998
Arum italicum, Glycine max
brenda
Umbach, A.L.; Siedow, J.N.
The cyanide-resistant alternative oxidases from the fungi Pichia stipitis and Neurospora crassa are monomeric and lack regulatory features of the plant enzyme
Arch. Biochem. Biophys.
378
234-245
2000
Neurospora crassa, Scheffersomyces stipitis
brenda
Berthold, D.A.
Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol:oxygen oxidoreductase) resistant to salicylhydroxamic acid
Biochim. Biophys. Acta
1364
73-83
1998
Arabidopsis thaliana
brenda
Siedow, J.N.; Umbach, A.L.
The mitochondrial cyanide-resistant oxidase: structural conservation amid regulatory diversity
Biochim. Biophys. Acta
1459
432-439
2000
Arabidopsis thaliana
brenda
Umbach, A.L.; Gonzalez-Meler, M.A.; Sweet, C.R.; Siedow, J.N.
Activation of the plant mitochondrial alternative oxidase: insights from site-directed mutagenesis
Biochim. Biophys. Acta
1554
118-128
2002
Arabidopsis thaliana
brenda
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
brenda
Albury, M.S.; Elliott, C.; Moore, A.L.
Ubiquinol-binding site in the alternative oxidase: mutagenesis reveals features important for substrate binding and inhibition
Biochim. Biophys. Acta
1797
1933-1939
2010
Schizosaccharomyces pombe, Schizosaccharomyces pombe Sp.011
brenda
Siedow, J.N.; Umbach, A.L.; Moore. A.L.
The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center
FEBS Lett.
362
10-14
1995
Sauromatum venosum
brenda
Djajanegara, I.; Holtzapffel, R.; Finnegan, P.M.; Hoefnagel, M.H.; Berthold, D.A.; Wiskich, J.T.; Day, D.A.
A single amino acid change in the plant alternative oxidase alters the specificity of organic acid activation
FEBS Lett.
454
220-224
1999
Arabidopsis thaliana, Glycine max
brenda
Mogi, T.; Ano, Y.; Nakatsuka, T.; Toyama, H.; Muroi, A.; Miyoshi, H.; Migita, C.T.; Ui, H.; Shiomi, K.; Omura, S.; Kita, K.; Matsushita, K.
Biochemical and spectroscopic properties of cyanide-insensitive quinol oxidase from Gluconobacter oxydans
J. Biochem.
146
263-271
2009
Gluconobacter oxydans, Gluconobacter oxydans (Q5FU84), Gluconobacter oxydans 621H (Q5FU84), Gluconobacter oxydans NBRC 3172
brenda
Moore, A.L.; Umbach, A.L.; Siedow, J.N.
Structure-function relationships of the alternative oxidase of plant mitochondria: a model of the active site
J. Bioenerg. Biomembr.
27
367-377
1995
Arum maculatum, Sauromatum venosum
brenda
Albury, M.S.; Dudley, P.; Watts, F.Z.; Moore, A.L.
Targeting the plant alternative oxidase protein to Schizosaccharomyces pombe mitochondria confers cyanide-insensitive respiration
J. Biol. Chem.
271
17062-17066
1996
Sauromatum venosum
brenda
Affourtit, C.; Albury, M.S.; Krab, K.; Moore, A.L.
Functional expression of the plant alternative oxidase affects growth of the yeast Schizosaccharomyces pombe
J. Biol. Chem.
274
6212-6218
1999
Sauromatum venosum
brenda
Albury, M.S.; Affourtit, C.; Crichton, P.G.; Moore, A.L.
Structure of the plant alternative oxidase. Site-directed mutagenesis provides new information on the active site and membrane topology
J. Biol. Chem.
277
1190-1194
2002
Sauromatum venosum
brenda
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.
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