Spectral identification of intermediates generated during the reaction of dioxygen with the wild-type and EQ(I-286) mutant of Rhodobacter sphaeroides cytochrome c oxidase.

@article{Szundi2012SpectralIO,
  title={Spectral identification of intermediates generated during the reaction of dioxygen with the wild-type and EQ(I-286) mutant of Rhodobacter sphaeroides cytochrome c oxidase.},
  author={Istv{\'a}n Szundi and Chie Funatogawa and Jennifer A. Cassano and William Alasdair Mcdonald and Jayashree Ray and Carrie Beth Hiser and Shelagh M Ferguson-Miller and Robert B Gennis and {\'O}l{\"o}f Einarsd{\'o}ttir},
  journal={Biochemistry},
  year={2012},
  volume={51 46},
  pages={
          9302-11
        }
}
Cytochrome c oxidase from Rhodobacter sphaeroides is frequently used to model the more complex mitochondrial enzyme. The O(2) reduction in both enzymes is generally described by a unidirectional mechanism involving the sequential formation of the ferrous-oxy complex (compound A), the P(R) state, the oxyferryl F form, and the oxidized state. In this study we investigated the reaction of dioxygen with the wild-type reduced R. sphaeroides cytochrome oxidase and the EQ(I-286) mutant using the CO… CONTINUE READING
BETA