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Information on EC 1.10.3.12 - menaquinol oxidase (H+-transporting) for references in articles please use BRENDA:EC1.10.3.12Word Map on EC 1.10.3.12
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The enzyme appears in viruses and cellular organisms
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menaquinol oxidase (H+-transporting)
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2 menaquinol + O2 = 2 menaquinone + 2 H2O
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menaquinol:O2 oxidoreductase (H+-transporting)
Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.The enzyme also pumps protons across the membrane bilayer, generating a proton motive force.
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cytochrome aa3-600 menaquinol oxidase
cytochrome aa3-600 oxidase
cytochrome aa3-type menaquinol oxidase
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cytochrome bd terminal oxidase
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cytochrome bd-type respiratory oxidase
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menaquinol oxidase (aa3-600)
menaquinol:O2 oxidoreductase
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cyt aa3-600
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cytochrome aa3
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cytochrome aa3-600
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cytochrome aa3-600 menaquinol oxidase
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cytochrome aa3-600 menaquinol oxidase
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cytochrome aa3-600 oxidase
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cytochrome aa3-600 oxidase
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cytochrome aa3-600 oxidase
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cytochrome bd oxidase
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cytochrome bd oxidase
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cytochrome bd oxidase
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cytochrome bd oxidase
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menaquinol oxidase (aa3-600)
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menaquinol oxidase (aa3-600)
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Qox
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metabolism
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the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cyo, Cyd and Nar contribute to the proton motive force that drives ATP formation. oxygen-dependent cytochrome oxidases, cytochrome bo3 (Cyo) and cytochrome bd (Cyd) oxidase, sustain up to 67% (Cyd) and 78% (Cyo) of HemG activity in the absence of ubiquinone, indicating a tight association of the quinones with the enzyme complexes during preparation
physiological function
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cytochrome aa3 is the most important terminal oxidase contributing to proton motive force generation in exponentially growing cells
physiological function
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cytochrome aas-600 is the major terminal oxidase in lopgh ase cells
physiological function
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the enzyme is important during murine infection
physiological function
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cytochrome aa3 is the most important terminal oxidase contributing to proton motive force generation in exponentially growing cells; cytochrome aas-600 is the major terminal oxidase in lopgh ase cells
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2,3-dimethyl-1,4-naphthoquinol + O2
2,3-dimethyl-1,4-naphthoquinone + H2O
2,3-dimethyl-1,4-naphthoquinone + O2
2,3-dimethyl-1,4-naphthoquinol + H2O
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?
dimethylnitrosamine + O2
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duroquinol + O2
duroquinone + H2O
ferricytochrome c + O2
ferrocytochrome c + H2O
menadiol + O2
menadione + H2O
menaquinol + O2
menaquinone + H2O
additional information
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2,3-dimethyl-1,4-naphthoquinol + O2
2,3-dimethyl-1,4-naphthoquinone + H2O
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best substrate
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?
2,3-dimethyl-1,4-naphthoquinol + O2
2,3-dimethyl-1,4-naphthoquinone + H2O
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best substrate
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?
dimethylnitrosamine + O2
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dimethylnitrosamine + O2
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duroquinol + O2
duroquinone + H2O
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?
duroquinol + O2
duroquinone + H2O
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ferricytochrome c + O2
ferrocytochrome c + H2O
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low activity
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?
ferricytochrome c + O2
ferrocytochrome c + H2O
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low activity
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menadiol + O2
menadione + H2O
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?
menadiol + O2
menadione + H2O
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?
menaquinol + O2
menaquinone + H2O
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menaquinol + O2
menaquinone + H2O
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cyt aa3-600 is strictly a menaquinol oxidase
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menaquinol + O2
menaquinone + H2O
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menaquinol + O2
menaquinone + H2O
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menaquinol + O2
menaquinone + H2O
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menaquinol + O2
menaquinone + H2O
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additional information
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cytochrome aa3-600 is a proton-pumping terminal oxidase
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additional information
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no activity with 1,4-naphthoquinol, N,N,N',N'-tetramethyl-1,4-phenylenediamine plus ascorbate or reduced cytochrome c
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additional information
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the enzyme does not oxidize 1,4-naphthoquinol, 2,3-dimethoxy-5-methyl-6-(n-nonyl)-1,4-benzoquinol, and 2,3-dimethoxy-5-methyl- 1,4-benzoquinol
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additional information
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cytochrome aa3-600 is a proton-pumping terminal oxidase
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additional information
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the enzyme does not oxidize 1,4-naphthoquinol, 2,3-dimethoxy-5-methyl-6-(n-nonyl)-1,4-benzoquinol, and 2,3-dimethoxy-5-methyl- 1,4-benzoquinol
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additional information
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no activity with 1,4-naphthoquinol, N,N,N',N'-tetramethyl-1,4-phenylenediamine plus ascorbate or reduced cytochrome c
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menaquinol + O2
menaquinone + H2O
menaquinol + O2
menaquinone + H2O
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?
menaquinol + O2
menaquinone + H2O
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cyt aa3-600 is strictly a menaquinol oxidase
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menaquinol + O2
menaquinone + H2O
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menaquinol + O2
menaquinone + H2O
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menaquinol + O2
menaquinone + H2O
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cytochrome
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the isolated enzyme contains 0.0053 mM cytochrome aa 3 per gram of protein and negligible amounts of cytochrome b and c
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cytochrome
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the enzyme contains 7 mol cytochrome aa 3 per g protein which corresponds to 2 mol heme A per mol enzyme
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heme
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cytochrome aa3-600 contains cytochrome a and cytochrome a3
heme
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the enzyme contains a binuclear heme iron-copper site
heme
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cytochrome aa3-600 is a member of the heme-copper superfamily of oxygen reductases
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copper
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cytochrome aa3-600 contains CuB
copper
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the enzyme contains a binuclear heme iron-copper site with only one copper CuB, while the Cu A center is lacking
Cu2+
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contains copper
Cu2+
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cytochrome aa3-600 is a member of the heme-copper superfamily of oxygen reductases
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2-(n-heptyl)-4-hydroxyquinoline-N-oxide
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antimycin A
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 39% residual activity at 0.01 mM
Myxothiazol
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 45% residual activity at 0.01 mM
Stigmatellin
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 39% residual activity at 0.01 mM
cyanide
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more than 90% of activity is inhibited by 0.01 mM cyanide
cyanide
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47% residual activity at 0.5 mM
cyanide
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the enzyme is easily inhibited by cyanide
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0.3
2,3-dimethyl-1,4-naphthoquinone
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in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
0.055 - 0.089
dimethylnitrosamine
0.055
dimethylnitrosamine
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mutant enzyme R70H, at pH 6.8 and 25°C
0.089
dimethylnitrosamine
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wild type enzyme, at pH 6.8 and 25°C
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61 - 65
2,3-dimethyl-1,4-naphthoquinone
180 - 227
dimethylnitrosamine
61
2,3-dimethyl-1,4-naphthoquinone
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in 50 mM Tris, pH 7.0, at 25°C
65
2,3-dimethyl-1,4-naphthoquinone
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in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
180
dimethylnitrosamine
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wild type enzyme, at pH 6.8 and 25°C
227
dimethylnitrosamine
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mutant enzyme R70H, at pH 6.8 and 25°C
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13686
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
15000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
20000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
22670
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
33640
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
54000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
57000
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the preparation consists of two major (57000 Da and 36000 Da) polypeptides
73834
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
144000
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calculated from sequence of cDNA
36000
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the preparation consists of two major (57000 Da and 36000 Da) polypeptides
36000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
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heterotetramer
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA; 1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
heterotetramer
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA; 1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
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DEAE-Sepharose column chromatography and chromatofocusing
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Ni-NTA column chromatography, 1.25 equivalents of menaquinone-7 co-purify with the enzyme
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Ni2+-chelating-Sepharose column chromatography
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expressed in Bacillus subtilis strain LUW143 lacking both the aa3-600 menaquinol oxidase and caa3-type cytochrome c oxidase
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expressed in Bacillus subtilis strain LUW20
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expressed in Escherichia coli XL10-Gold cells
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R70H
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the mutant shows reduced activity compared to the wild type enzyme
R70H
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the mutant shows reduced activity compared to the wild type enzyme
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A0A1Y0XDY6_BACAM
122
13484
TrEMBL
A0A072NPY0_BACAZ
97
10561
TrEMBL
A0A072P1E3_BACAZ
649
73060
TrEMBL
S9QP02_9RHOB
191
20234
TrEMBL
A0A0S4MF82_STACP
662
75279
TrEMBL
A0A0D0Q0N4_9RHOB
186
20215
TrEMBL
A0A1Y0YLF8_BACLI
121
13142
TrEMBL
A0A1Y0YLA8_BACLI
204
22886
TrEMBL
A0A0H4L7W3_9RHOB
198
21351
TrEMBL
V9W8Y3_9BACL
206
23108
TrEMBL
A0A1E3L9R2_9BACL
658
74726
TrEMBL
A0A0U1EF66_STACP
201
22943
TrEMBL
S6FQQ5_9BACI
649
73633
TrEMBL
A0A2X0Q2R4_BROTH
204
23004
TrEMBL
A0A2W0CUF1_9BACL
656
74775
TrEMBL
A0A072NPA7_BACAZ
198
22151
TrEMBL
A0A1Y0X0N1_BACLI
649
73838
TrEMBL
A0A2L1U6F7_9BACL
206
23108
TrEMBL
A0A1Y0XHM1_BACAM
649
73702
TrEMBL
A0A1Y0XX34_BACLI
649
73754
TrEMBL
W8TQJ7_STAAU
662
75243
TrEMBL
A0A2X0R854_BROTH
336
37808
TrEMBL
W2ECJ1_9BACL
206
23108
TrEMBL
S6G2Y1_9BACI
204
22636
TrEMBL
M1Z7E5_9FIRM
[Clostridium] ultunense Esp
203
22442
TrEMBL
A0A1Q9FRQ1_BACLI
204
22672
TrEMBL
A0A1Y0XDU9_BACAM
204
22666
TrEMBL
A0A075RBT1_BRELA
198
22521
TrEMBL
A0A2L1THY2_9BACL
106
11669
TrEMBL
V9WCP1_9BACL
106
11669
TrEMBL
M1ZIC0_9FIRM
[Clostridium] ultunense Esp
653
74453
TrEMBL
A0A2X0Q7T2_BROTH
204
23046
TrEMBL
A0A2X0QZM3_BROTH
663
74879
TrEMBL
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Lemma, E.; Schagger, H.; Kroger, A.
The menaquinol oxidase of Bacillus subtilis W23
Arch. Microbiol.
159
574-578
1993
Bacillus subtilis, Bacillus subtilis W23
brenda
Lemma, E.; Simon, J.; Schagger, H.; Kroger, A.
Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis
Arch. Microbiol.
163
432-438
1995
Bacillus subtilis, Bacillus subtilis W23
brenda
Mattatall, N.R.; Cameron, L.M.; Hill, B.C.
Transient-state reduction and steady-state kinetic studies of menaquinol oxidase from Bacillus subtilis, cytochrome aa3-600 nm. Spectroscopic characterization of the steady-state species
Biochemistry
40
13331-13341
2001
Bacillus subtilis
brenda
Powers, L.; Lauraeus, M.; Reddy, K.S.; Chance, B.; Wikstroem, M.
Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis
Biochim. Biophys. Acta
1183
504-512
1994
Bacillus subtilis
brenda
Winstedt, L.; Frankenberg, L.; Hederstedt, L.; von Wachenfeldt, C.
Enterococcus faecalis V583 contains a cytochrome bd-type respiratory oxidase
J. Bacteriol.
182
3863-3866
2000
Enterococcus faecalis
brenda
Winstedt, L.; von Wachenfeldt, C.
Terminal oxidases of Bacillus subtilis strain 168: one quinol oxidase, cytochrome aa3 or cytochrome bd, is required for aerobic growth
J. Bacteriol.
182
6557-6564
2000
Bacillus subtilis, Bacillus subtilis 168
brenda
Lauraeus, M.; Wikstroem, M.
The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties
J. Biol. Chem.
268
11470-11473
1993
Bacillus subtilis 168, Bacillus subtilis
brenda
Yi, S.M.; Narasimhulu, K.V.; Samoilova, R.I.; Gennis, R.B.; Dikanov, S.A.
Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis
J. Biol. Chem.
285
18241-18251
2010
Bacillus subtilis
brenda
Moebius, K.; Arias-Cartin, R.; Breckau, D.; Haennig, A.L.; Riedmann, K.; Biedendieck, R.; Schroeder, S.; Becher, D.; Magalon, A.; Moser, J.; Jahn, M.; Jahn, D.
Heme biosynthesis is coupled to electron transport chains for energy generation
Proc. Natl. Acad. Sci. USA
107
10436-10441
2010
Escherichia coli
brenda
Bossis, F.; De Grassi, A.; Palese, L.L.; Pierri, C.L.
Prediction of high- and low-affinity quinol-analogue-binding sites in the aa3 and bo3 terminal oxidases from Bacillus subtilis and Escherichia coli
Biochem. J.
461
305-314
2014
Bacillus subtilis
brenda
Yi, S.M.; Taguchi, A.T.; Samoilova, R.I.; OMalley, P.J.; Gennis, R.B.; Dikanov, S.A.
Plasticity in the high affinity menaquinone binding site of the cytochrome aa3-600 menaquinol oxidase from Bacillus subtilis
Biochemistry
54
5030-5044
2015
Bacillus subtilis 1A1, Bacillus subtilis
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
e00354-17
2017
Listeria monocytogenes
brenda
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