Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.14279/2183
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 |
metadata.dc.contributor.other: | Βαρώτσης, Κωνσταντίνος | Keywords: | Cytochrome oxidase;Oxygen;Photochemistry;Cytochromes;Enzymes;Raman spectroscopy | Issue Date: | 1989 | 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: | https://hdl.handle.net/20.500.14279/2183 | ISSN: | 0002-7863 (print) 1520-5126 (online) |
DOI: | 10.1021/ja00198a075 | Rights: | © 1989 American Chemical Society | Type: | Article | Affiliation: | Michigan State University |
Appears in Collections: | Άρθρα/Articles |
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