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Volume 271, Number 16, Issue of April 19, 1996 pp. 9177-9180
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Enzymatic and Electron Transfer Activities in Crystalline Protein Complexes

(Received for publication, December 26, 1995; and in revised form, February 12, 1996)

Angelo Merli ,  Ditlev E. Brodersen ,  Barbara Morini ,  Zhi-wei Chen ,  Rosemary C. E. Durley ,  F. Scott Mathews ,  Victor L. Davidson ,  Gian Luigi Rossi

Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the reduced tryptophan tryptophylquinone (TTQ) cofactor to the copper of amicyanin and to the heme of cytochrome c via amicyanin. The equilibrium distribution of electrons among the cofactors, and the rate of heme reduction after reaction with substrate, are both dependent on pH. The presence of copper in the ternary complex is not absolutely required for electron transfer from TTQ to heme, but its presence greatly enhances the rate of electron flow to the heme.



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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.