Resolution of cytochrome oxidase into two component complexes.
AUTOR(ES)
Fry, M
RESUMO
Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC 1.9.3.1) has been resolved into a pair of complexes of unequal molecular weight. The larger complex (electron transfer complex) contains exclusively the oxidation-reduction proteins characteristic of cytochrome oxidase; the smaller complex (ion transfer complex) shows exclusively the capability for cation-dependent induction of the fluorescence of 8-anilino-1-naphthalenesulfonic acid--a capability demonstrable in preparations of cytochrome oxidase. The duplex nature of cytochrome oxidase has important implications for the mechanism of energy coupling.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=393085Documentos Relacionados
- Resolution of complex III of the mitochondrial electron transfer chain into two component complexes.
- An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes.
- Ion-channel component of cytochrome oxidase.
- Resolution of the electronic transitions of cytochrome c oxidase: evidence for two conformational states of ferrous cytochrome alpha.
- Component A3 of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum delta H: resolution into two components.