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 language | English (US) |
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Pages (from-to) | 329-331 |
Number of pages | 3 |
Journal | Science |
Volume | 225 |
Issue number | 4659 |
DOIs | |
State | Published - 1984 |
Externally published | Yes |
ASJC Scopus subject areas
- General