Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6702
Title: Time-resolved raman detection of v(Fe-O) in an early intermediate in the reduction of O2 by cytochrome oxidase
Authors: Woodruff, William
Babcock, Gerald
Varotsis, Constantinos 
Keywords: Cytochrome oxidase
Oxygen
Photochemistry
Cytochromes
Enzymes
Raman spectroscopy
Issue Date: 1989
Publisher: ACS Publications
Source: Journal of the american chemical society, 1989, Volume 111, Issue 16, Pages 6439-6440
Abstract: Cytochrome oxidase contains four redox-active centers per functional unit: cytochromes a and a3 and the copper atoms, CuA and Cue. Cytochrome c, the physiological substrate of cytochrome oxidase, transfers electrons to the cyt a and CuA sites. These reducing equivalents are transferred to the binuclear cyt a3-CuB center, which binds O2 and reduces it to H20. Although the reaction between O2 and cytochrome oxidase occurs too quickly to be studied by conventional stopped-flow techniques, Gibson and Greenwood' showed that photolysis of the cytochrome a32+-CO complex of the enzyme in the presence of O2 could be used to circumvent this limitation. Babcock et adopted this approach and used time-resolved resonance Raman spectroscopy to study
URI: http://ktisis.cut.ac.cy/handle/10488/6702
ISSN: 0002-7863 (print)
1520-5126 (online)
DOI: 10.1021/ja00198a075
Rights: © 1989 American Chemical Society
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