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• W617349056 abstract "A cytochrome c haem ligand, methionine-80, was photo-oxidized to methionine sulphoxide and the subsequent changes in redox properties and ligand binding were monitored kinetically. Isoelectric focusing of the product showed the presence of a single oxidized species, capable of binding CO when reduced. The binding of CO to the reduced protein was followed in stopped-flow experiments, which revealed the presence of two binding processes, at neutral pH, with rate constants of K+1 = 3.4 × 10(3)M-1-S-1 and k+2 = 5.80 × 10(2)M-1-S-1. When CO was photolytically dissociated from the reduced protein two recombination processes were observed with rates almost identical with those observed in the stopped-flow experiments (k+1 = 3.3 × 10(3)M-1-S-1 and k+2 = 6.0 × 10(2)M-1-S-1). These findings provide evidence of two reduced forms of the protein. The reduction of [methionine sulphoxide]cytochrome c by Cr2+ at neutral pH in stopped-flow experiments showed the presence of a single second-order reduction process (k = 7.2 × 10(3)M-1-S-1, activation energy = 44kJ/mol) and one first-order process. This protein was compared with some other chemically modified cytochromes." @default.
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• W617349056 date "1976-12-01" @default.
• W617349056 modified "2023-10-18" @default.
• W617349056 title "Kinetic studies on [methionine sulphoxide] cytochrome c" @default.
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• W617349056 doi "https://doi.org/10.1042/bj1590621" @default.
• W617349056 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1164161" @default.
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