Cytochrome a3 structure in carbon monoxide-bound cytochrome oxidase

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

Research output: Contribution to journalArticlepeer-review

65 Scopus citations


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
Issue number4659
StatePublished - 1984
Externally publishedYes

ASJC Scopus subject areas

  • General


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