Cytochrome a3 structure in carbon monoxide-bound cytochrome oxidase

P. V. Argade, Y. C. Ching, Denis L. Rousseau

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm-1, respectively. The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a 3 is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five-and six-coordinate cytochrome 03 is strained; and that the carbon monoxide and the proximal histidine each have characteristic, well-defined orientations in all molecules. These data can account for the binding affinities of carbon monoxide and dioxygen under physiological conditions.

Original languageEnglish (US)
Pages (from-to)329-331
Number of pages3
JournalScience
Volume225
Issue number4659
StatePublished - 1984
Externally publishedYes

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Cytochromes a3
Electron Transport Complex IV
Carbon Monoxide
Iron
Histidine
Oxygen
Cytochromes
Heme
Carbon

ASJC Scopus subject areas

  • General

Cite this

Cytochrome a3 structure in carbon monoxide-bound cytochrome oxidase. / Argade, P. V.; Ching, Y. C.; Rousseau, Denis L.

In: Science, Vol. 225, No. 4659, 1984, p. 329-331.

Research output: Contribution to journalArticle

Argade, PV, Ching, YC & Rousseau, DL 1984, 'Cytochrome a3 structure in carbon monoxide-bound cytochrome oxidase', Science, vol. 225, no. 4659, pp. 329-331.
Argade, P. V. ; Ching, Y. C. ; Rousseau, Denis L. / Cytochrome a3 structure in carbon monoxide-bound cytochrome oxidase. In: Science. 1984 ; Vol. 225, No. 4659. pp. 329-331.
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