EC Number   |
BRENDA No. |
Title |
Journal |
Volume  |
Pages |
Year |
Organism |
PubMed ID |
|---|
    7.1.1.3 | 743792 |
The cytochrome bd-type quinol oxidase is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress |
Sci. Rep. |
5 |
10333 |
2015 |
Mycolicibacterium smegmatis |
26015371 |
| 7.1.1.3 | 743792 |
The cytochrome bd-type quinol oxidase is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress |
Sci. Rep. |
5 |
10333 |
2015 |
Mycolicibacterium smegmatis mc(2)155 |
26015371 |
| 7.1.1.3 | 741935 |
Q-band electron-nuclear double resonance reveals out-of-plane hydrogen bonds stabilize an anionic ubisemiquinone in cytochrome bo3 from Escherichia coli |
Biochemistry |
55 |
5714-5725 |
2016 |
Escherichia coli |
27622672 |
| 7.1.1.3 | 742510 |
Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site |
FEBS Lett. |
588 |
1537-1541 |
2014 |
Escherichia coli |
24681096 |
| 7.1.1.3 | 752188 |
The terminal oxidase cytochrome bd promotes sulfide-resistant bacterial respiration and growth |
Sci. Rep. |
6 |
23788 |
2016 |
Escherichia coli |
27030302 |
| 7.1.1.3 | 741616 |
Susceptibility of Mycobacterium tuberculosis cytochrome bd oxidase mutants to compounds targeting the terminal respiratory oxidase, cytochrome c |
Antimicrob. Agents Chemother. |
61 |
e01338-17 |
2017 |
Mycobacterium tuberculosis |
28760899 |
| 7.1.1.3 | 741616 |
Susceptibility of Mycobacterium tuberculosis cytochrome bd oxidase mutants to compounds targeting the terminal respiratory oxidase, cytochrome c |
Antimicrob. Agents Chemother. |
61 |
e01338-17 |
2017 |
Mycobacterium tuberculosis H37Rv |
28760899 |
| 7.1.1.3 | 749941 |
Spectral-kinetic analysis of recombination reaction of heme centers of bd-type quinol oxidase from Escherichia coli with carbon monoxide |
Biochemistry |
82 |
1354-1366 |
2017 |
Escherichia coli |
29223162 |
| 7.1.1.3 | 716735 |
Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site |
Proc. Natl. Acad. Sci. USA |
102 |
3657-3662 |
2005 |
Escherichia coli |
15728392 |
| 7.1.1.3 | 716735 |
Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site |
Proc. Natl. Acad. Sci. USA |
102 |
3657-3662 |
2005 |
Escherichia coli GO105 |
15728392 |
