Evidence for the absence of photoreduction of the metal centers of cytochrome C oxidase by X-irradiation.

Gary W Brudvig, D. F. Bocian, R. C. Gamble, S. I. Chan

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Samples of X-irradiated cytochrome c oxidase were examined by electron paramagnetic resonance and optical spectroscopy. Both radiation from the Stanford Synchrotron Radiation Laboratory and a conventional X-ray source (W target) were utilized. The X-ray flux from these sources ranges from 10(9) to 10(13) photons/s. No evidence was found for photoreduction of the metal centers in the enzyme by X-ray photons. These results demonstrate that the integrity of cytochrome c oxidase is maintained using the conditions under which X-ray absorption measurements are presently being made.

Original languageEnglish
Pages (from-to)78-89
Number of pages12
JournalBiochimica et biophysica acta
Volume624
Issue number1
Publication statusPublished - Jul 24 1980

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Electron Transport Complex IV
Cytochromes
Oxidoreductases
Metals
X-Rays
Irradiation
X rays
Photons
X ray absorption
Radiation
Synchrotron radiation
Synchrotrons
Paramagnetic resonance
Electron Spin Resonance Spectroscopy
Fluxes
Spectrum Analysis
Enzymes

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Evidence for the absence of photoreduction of the metal centers of cytochrome C oxidase by X-irradiation. / Brudvig, Gary W; Bocian, D. F.; Gamble, R. C.; Chan, S. I.

In: Biochimica et biophysica acta, Vol. 624, No. 1, 24.07.1980, p. 78-89.

Research output: Contribution to journalArticle

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