Pub No:
118
Title:
Proton Activities for Three States of Cytochrome P-450cam
Authors:
David Dolphin, James, B.R., and Welborn, H.C.
Journal:
Biochem. Biophys. Res. Commun.
Year:
1979
Pages:
88, 415-421
Abstract:
Changes in proton concentration during the binding of O2, CO, and in the exchange of O2 by CO at ferrocytochrome P 450cam were measured by direct titration Insufficient proton release was observed to support protonation-deprotonation of an axial cysteinyl S donor as a mechanism for generation of hyper spectra in only the carbonylated ferrous state. Measurement of the pCO2 required to convert 1/2 of the cytochrome to the CO-bound form as a function of pH (the CO Bohr effect) confirmed the direct titration data.

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