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Fast Consecutive Intramolecular Processes Involving Protein and Fe(III) in Ferri‐Cytochrome‐c in Aqueous Solution
Author(s) -
Lichtin N.N.,
Ogdan J.,
Stein G.
Publication year - 1971
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197100079
Subject(s) - chemistry , intramolecular force , moiety , aqueous solution , reaction rate constant , cytochrome c , nanosecond , photochemistry , radiolysis , absorption spectroscopy , crystallography , stereochemistry , kinetics , laser , biochemistry , physics , quantum mechanics , optics , mitochondrion
The reaction of H atoms (produced by nanosecond pulse radiolysis) with ferri‐cytochrome‐c in aqueous solution results in the second order formation of an absorption spectrum due to the addition of H atoms to the enzyme protein. This spectrum is not specific to the iron moiety. The rate constant of the addition is 1×10 10 M −1 sec −1 . This is followed by two first order intramolecular processes with specific rates of ∼ 1×10 5 sec −1 and ∼ 2×10 4 sec −1 . In these processes, specific spectra related to the α and β bands of ferro‐cytochrome‐c appear. The results are interpreted to show reduction equivalent transfer through the protein to the iron moiety.