NDLI: X-ray absorption edge studies on oxidized and reduced cytochrome c oxidase.

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X-ray absorption edge studies on oxidized and reduced cytochrome c oxidase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chan, S. I. Hu, V. W. Brown, G. S.
Abstract	The x-ray absorption edge spectra of the Cu and Fe-centers in oxidized and reduced cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase: EC 1.9.3.1) have been obtained using synchrotron radiation from the SPEAR storage ring at the Stanford Linear Accelerator Center. In addition, oxidized and reduced plastocyanin as well as a number of model copper compounds in various oxidation states were also examined. A comparison of the absorption edge fine structure of cytochrome oxidase with those of the models indicates that one of the two coopers in the oxidized protein is in the +1 oxidation state. Upon reduction of the protein with dithionite, the second copper becomes Cu(I). The shift in the Fe K-edge of cytochrome oxidase upon reduction is small (about 2 e V or 3 times 10(-19 J) and is comparable to that previously observed for the reduction of the heme iron of cytochrome c.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	74
Language	English
Publisher	National Academy of Sciences
Publisher Date	1977-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Electron Transport Complex IV Animals Chick Embryo Copper Cytochrome c Group Myocardium Enzymology Oxidation-Reduction Plastocyanin Spectrum Analysis X-Rays Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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