Heme-heme communication during the alkaline-induced structural transition in cytochrome c oxidase

Journal of Inorganic Biochemistry
Hong JiSyun-Ru Yeh

Abstract

Alkaline-induced conformational changes at pH 12.0 in the oxidized as well as the reduced state of cytochrome c oxidase have been systematically studied with time-resolved optical absorption and resonance Raman spectroscopies. In the reduced state, the heme a(3) first converts from the native five-coordinate configuration to a six-coordinate bis-histidine intermediate as a result of the coordination of one of the Cu(B) ligands, H290 or H291, to the heme iron. The coordination state change in the heme a(3) causes the alteration in the microenvironment of the formyl group of the heme a(3) and the disruption of the H-bond between R38 and the formyl group of the heme a. This structural transition, which occurs within 1min following the initiation of the pH jump, is followed by a slower reaction, in which Schiff base linkages are formed between the formyl groups of the two hemes and their nearby amino acid residues, presumably R38 and R302 for the heme a and a(3), respectively. In the oxidized enzyme, a similar Schiff base modification on heme a and a(3) was observed but it is triggered by the coordination of the H290 or H291 to heme a(3) followed by the breakage of the native proximal H378-iron and H376-iron bonds in heme a and a(3...Continue Reading

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Citations

Oct 3, 2008·Journal of Bioenergetics and Biomembranes·Martyn A Sharpe, Shelagh Ferguson-Miller
Nov 3, 2011·Chembiochem : a European Journal of Chemical Biology·Toni KühlDiana Imhof
Jan 28, 2014·Biochemistry. Biokhimii︠a︡·A V DyubaA A Konstantinov

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