Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.14279/2183
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Woodruff, William | en |
dc.contributor.author | Babcock, Gerald | en |
dc.contributor.author | Varotsis, Constantinos | - |
dc.contributor.other | Βαρώτσης, Κωνσταντίνος | - |
dc.date.accessioned | 2013-01-25T08:28:24Z | en |
dc.date.accessioned | 2013-05-16T06:25:31Z | - |
dc.date.accessioned | 2015-12-02T09:18:11Z | - |
dc.date.available | 2013-01-25T08:28:24Z | en |
dc.date.available | 2013-05-16T06:25:31Z | - |
dc.date.available | 2015-12-02T09:18:11Z | - |
dc.date.issued | 1989 | en |
dc.identifier.citation | Journal of the american chemical society, 1989, Volume 111, Issue 16, Pages 6439-6440 | en |
dc.identifier.issn | 0002-7863 (print) | en |
dc.identifier.issn | 1520-5126 (online) | en |
dc.identifier.uri | https://hdl.handle.net/20.500.14279/2183 | - |
dc.description.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 | en |
dc.language.iso | en | en |
dc.rights | © 1989 American Chemical Society | en |
dc.subject | Cytochrome oxidase | en |
dc.subject | Oxygen | en |
dc.subject | Photochemistry | en |
dc.subject | Cytochromes | en |
dc.subject | Enzymes | en |
dc.subject | Raman spectroscopy | en |
dc.title | Time-resolved raman detection of v(Fe-O) in an early intermediate in the reduction of O2 by cytochrome oxidase | en |
dc.type | Article | en |
dc.affiliation | Michigan State University | en |
dc.identifier.doi | 10.1021/ja00198a075 | en |
dc.dept.handle | 123456789/54 | en |
item.openairetype | article | - |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en | - |
item.fulltext | No Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.grantfulltext | none | - |
crisitem.author.dept | Department of Chemical Engineering | - |
crisitem.author.faculty | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.orcid | 0000-0003-2771-8891 | - |
crisitem.author.parentorg | Faculty of Geotechnical Sciences and Environmental Management | - |
Appears in Collections: | Άρθρα/Articles |
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