X-Ray Absorption Edge Studies on Oxidized and Reduced Cytochrome c Oxidase
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 an...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 74; no. 9; pp. 3821 - 3825 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
National Academy of Sciences of the United States of America
01.09.1977
National Acad Sciences |
Subjects | |
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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 coppers 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 eV or 3 × 10-19J) and is comparable to that previously observed for the reduction of the heme iron of cytochrome c. |
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AbstractList | 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. 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 coppers 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 eV or 3 × 10-19J) and is comparable to that previously observed for the reduction of the heme iron of cytochrome c. |
Author | Hu, Valerie W. Chan, Sunney I. Brown, George S. |
Author_xml | – sequence: 1 givenname: Valerie W. surname: Hu fullname: Hu, Valerie W. – sequence: 2 givenname: Sunney I. surname: Chan fullname: Chan, Sunney I. – sequence: 3 givenname: George S. surname: Brown fullname: Brown, George S. |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/198807$$D View this record in MEDLINE/PubMed |
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SubjectTerms | Absorption spectra Animals Atoms Cattle Chick Embryo Copper Cytochrome c Group Cytochromes Dogs Electron Transport Complex IV Energy levels Iron Ligands Myocardium - enzymology Oxidases Oxidation Oxidation-Reduction Plastocyanin Spectrum Analysis Synchrotron radiation X ray spectrum X-Rays |
Title | X-Ray Absorption Edge Studies on Oxidized and Reduced Cytochrome c Oxidase |
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