EC Number   |
BRENDA No.  |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
|---|
    7.1.1.3 | 713612 |
Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli |
Acta Crystallogr. Sect. D |
56 |
1076-1078 |
2000 |
Escherichia coli |
10944359 |
| 7.1.1.3 | 713612 |
Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli |
Acta Crystallogr. Sect. D |
56 |
1076-1078 |
2000 |
Escherichia coli GO105 |
10944359 |
| 7.1.1.3 | 714129 |
Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity |
Biochemistry |
31 |
6917-6924 |
1992 |
Escherichia coli |
1322173 |
| 7.1.1.3 | 714129 |
Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity |
Biochemistry |
31 |
6917-6924 |
1992 |
Escherichia coli RG145 |
1322173 |
| 7.1.1.3 | 714130 |
Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity |
Biochemistry |
32 |
10923-10928 |
1993 |
Escherichia coli |
8399242 |
| 7.1.1.3 | 714130 |
Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity |
Biochemistry |
32 |
10923-10928 |
1993 |
Escherichia coli GL101 |
8399242 |
| 7.1.1.3 | 714131 |
Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center |
Biochemistry |
32 |
11173-11180 |
1993 |
Escherichia coli |
8218180 |
| 7.1.1.3 | 714131 |
Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center |
Biochemistry |
32 |
11173-11180 |
1993 |
Escherichia coli GL101 |
8218180 |
| 7.1.1.3 | 714132 |
Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands |
Biochemistry |
32 |
11524-11529 |
1993 |
Escherichia coli |
8218219 |
| 7.1.1.3 | 714132 |
Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands |
Biochemistry |
32 |
11524-11529 |
1993 |
Escherichia coli GLlOl |
8218219 |
