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Cytochrome oxidase heme-protein dynamics: a transient Raman study of carbon monoxide photolysis from cytochrome a

Journal Article · · J. Am. Chem. Soc.; (United States)
DOI:https://doi.org/10.1021/ja00331a059· OSTI ID:6462637

Data are reported on results of initial efforts to probe the mechanism of cytochrome oxidase function by utilizing time-resolved resonance Raman spectroscopy. Preparation of the reduced beef-heart cytochrome oxidase sample and cytochrome oxidase-CO sample is described. At the laser powers and concentrations employed, the reduced cytochrome oxidase-CO sample underwent almost complete photolysis during the laser pulse. Principal conclusions drawn from spectral analysis are that time-resolved resonance Raman investigation of the transient heme species generated by ligand photolysis is a viable technique for the study of heme-ligand dynamics in proteins other than hemoglobin. A transient proximal geometry leading to a strengthened iron-histidine bond is present in these. The interplay of porphyrin core size, pi electron density, and Fe-His bonding as modulated by heme-protein dynamics is different for the ligand binding sites of hemoglobin and cytochrome oxidase. 17 references, 1 figure.

Research Organization:
Univ. of New Mexico, Albuquerque
OSTI ID:
6462637
Journal Information:
J. Am. Chem. Soc.; (United States), Journal Name: J. Am. Chem. Soc.; (United States) Vol. 106:19; ISSN JACSA
Country of Publication:
United States
Language:
English

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