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Kinetics of elementary steps in the cytochrome P-450 reaction sequence. V. Laser temperature-jump investigation of the spin relaxation kinetics of cytochrome P-450 LM2

Ziegler, M.; Blanck, J.; Greschner, S.; Lenz, K.; Lau, A.; Ruckpaul, K.

Biomedica Biochimica Acta 42(6): 641-649

1983

ISSN/ISBN: 0232-766X
PMID: 6639642
Document Number: 213147
The cytochrome P-450 LM2 spin state relaxation kinetics has been resolved by means of laser temperature-jump techniques. The first order rate constants amount to about 10(6) S-1 in the substrate-free and the substrate-bound protein, respectively. Evidence is provided that the spin equilibrium preequilibrates the P-450 reduction but is not rate-limiting. Additional capacitor discharge temperature-jump studies elucidate substrate dependent perturbations.

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