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Literature summary for 7.1.1.9 extracted from

  • Wang, K.; Geren, L.; Zhen, Y.; Ma, L.; Ferguson-Miller, S.; Durham, B.; Millett, F.
    Mutants of the CuA site in cytochrome c oxidase of Rhodobacter sphaeroides: II. Rapid kinetic analysis of electron transfer (2002), Biochemistry, 41, 2298-2304.
    View publication on PubMed
Search for more literature for 7.1.1.9

Protein Variants

Protein Variants Comment Organism
H260N mutant of CuA center, the rate constant for the intramolecular electron transfer from heme c to CuA is decreased from 40000 per s for the wild-type enzyme to 11000 for the mutant enzyme, the rate constant for intracomplex electron transfer from CuA to heme a is decreased from 90000 per s for wild-type enzyme to 45 per s for the mutant. The rate constant for the reverse reaction, heme A to CuA, is 180 per s for the mutant enzyme, compared to 17000 for the wild-type enzyme. The redox potential of CuA is increased by 90 mV relative to hemeA Cereibacter sphaeroides
M263L mutant of CuA center, the rate constant for the intramolecular electron transfer from heme c to CuA is decreased from 40000 per s for the wild-type enzyme to 16000 for the mutant enzyme, the rate constant for intracomplex electron transfer from CuA to heme a is decreased from 90000 per s for wild-type enzyme to 4000 per s for the mutant. The rate constant for the reverse reaction, hemeA to CuA, is 66000 per s for the mutant enzyme, compared to 17000 for the wild-type enzyme. The redox potential of CuA is increased by 120 mV relative to hemeA Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
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Synonyms

Synonyms Comment Organism
CCO
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 Cereibacter sphaeroides