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

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
 [1]; ;
  1. California Inst. of Tech., Pasadena
+ Show Author Affiliations

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, ozidized 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 x 10/sup -19/ J) and is comparable to that previously observed for the reduction of the heme iron of cytochrome c.

OSTI ID:
6845531
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 74:9; ISSN PNASA
Country of Publication:
United States
Language:
English

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Related Subjects

550200* -- Biochemistry
560111 -- Radiation Effects on Biochemicals-- In Vitro-- (-1987)
59 BASIC BIOLOGICAL SCIENCES
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ABSORPTION SPECTRA
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL EFFECTS
BREMSSTRAHLUNG
CHEMICAL REACTIONS
COPPER
COPPER COMPOUNDS
CYTOCHROME OXIDASE
ELECTROMAGNETIC RADIATION
ELEMENTS
ENZYMES
IRON
KINETICS
METALS
ORGANIC COMPOUNDS
OXIDASES
OXIDOREDUCTASES
PROTEINS
RADIATIONS
REACTION KINETICS
REDUCTION
SPECTRA
SPECTROSCOPY
SYNCHROTRON RADIATION
TRANSITION ELEMENT COMPOUNDS
TRANSITION ELEMENTS
X-RAY SPECTROSCOPY