Possible Role of the Iron Coordination Sphere in Hemoprotein Electron Transfer Self-Exchange: (1)H NMR Study of the Cytochrome c-PMe(3) Complex.
The rates of self-exchange electron transfer in the trimethylphosphine complex of cytochrome c have been measured by an NMR technique over a large range of ionic strengths. The rate constant is 1.56 x 10(4) M(-)(1) s(-)(1) at 23 degrees C (&mgr; = 0.34 M) at pH 6.9. Dependence on ionic strength of the rate constant is treated by van Leeuwen theory. Extrapolation of the rate constant to infinite ionic strength gives a rate constant of 3.9 x 10(5) M(-)(1) s(-)(1). This rate constant is compared with others reported for myoglobin and cytochrome b(5)(). The values for these systems range over 2 orders of magnitude with myoglobin-PMe(3) << cytochrome b(5)() < cytochrome c-PMe(3) < cytochrome c. Analysis of the data in terms of Marcus theory gives a reorganization energy, lambda, for self-exchange of 0.75 eV mol(-)(1) for cytochrome c-PMe(3). Substitution of Met-80 by PMe(3) appears to influence only weakly the rearrangement barrier to electron transfer.
Legrand
Nathalie
N
Laboratoire de Chimie Organométallique et Biologique, URA CNRS 415, Université de Rennes 1, Campus de Beaulieu, Rennes, France.
Bondon
Arnaud
A
Simonneaux
Gérard
G