A previously obtained photomodified cytochrome c is analyzed in order to characterize the first coordination sphere of the heme iron. Electron spin resonance and electrochemical measurements show that iron is exa-coordinated in the photomodified cytochrome as well as in the native one and are in favour of tyrosine-67 being the sixth heme ligand. An investigation on the photoredox behaviour of cytochrome C551(Pseudomonas aerugnnosa is also reported. The results obtained are discussed on the basis of the difference in the heme environment with respect to cytochrome c, so obtaining further confirmation of the conclusions drawn in the case of the mitochondrial protein. © 1986.
Photoredox reactions in Cytochrome c and cytochrome c551
MALDOTTI, Andrea;BARTOCCI, Carlo;CARASSITI, Vittorio;FERRI, Albertino;BORTOLOTTI, Fabrizio
1986
Abstract
A previously obtained photomodified cytochrome c is analyzed in order to characterize the first coordination sphere of the heme iron. Electron spin resonance and electrochemical measurements show that iron is exa-coordinated in the photomodified cytochrome as well as in the native one and are in favour of tyrosine-67 being the sixth heme ligand. An investigation on the photoredox behaviour of cytochrome C551(Pseudomonas aerugnnosa is also reported. The results obtained are discussed on the basis of the difference in the heme environment with respect to cytochrome c, so obtaining further confirmation of the conclusions drawn in the case of the mitochondrial protein. © 1986.I documenti in SFERA sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
