Laser flash photolysis studies of electron transfer between semiquinone and fully reduced free flavins and horse heart cytochrome c.
AUTOR(ES)
Ahmad, I
RESUMO
Laser flash photolysis has been used to determine the second-order rate constants for the reduction of horse heart cytochrome c by the semiquinone and fully reduced forms of various flavin analogs. We find that substitution in the dimethylbenzene ring of the flavin causes appreciable changes in the rate constants, whereas substitutions at the N-10 position do not. Placing a charged phosphate group in the N-10 ribityl side chain leads to only small ionic strength effects on the rate constants, whereas a charged group attached to the dimethylbenzene ring produces a large ionic strength effect. These results can be accounted for by assuming that a productive collision between flavin and cytochrome involves an orientation that positions the aromatic ring--N-5 region of the flavin toward the heme crevice and the N-10--pyrimidine ring region away from it. Our observations have implications for mechanistic understanding of biological electron transfer reactions and are discussed in this context.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=349122Documentos Relacionados
- Metalloprotein electron transfer reactions: analysis of reactivity of horse heart cytochrome c with inorganic complexes.
- Kinetics of electron transfer between cardiac cytochromes c1 and c.
- Electron transfer between hemes in mammalian cytochrome c oxidase
- Mechanism of electron transfer in the cytochrome b/f complex of algae: evidence for a semiquinone cycle.
- Direct measurements of intramolecular electron transfer rates between cytochrome c and cytochrome c peroxidase: effects of exothermicity and primary sequence on rate.
