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Science 20 July 1984:
Vol. 225. no. 4659, pp. 329 - 331
DOI: 10.1126/science.6330890
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Articles

Science, Vol 225, Issue 4659, 329-331
Copyright © 1984 by American Association for the Advancement of Science

articles

Cytochrome a3 structure in carbon monoxide-bound cytochrome oxidase

PV Argade, YC Ching, and DL Rousseau

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 a3 is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five- and six-coordinate cytochrome a3 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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Simultaneous Resonance Raman Detection of the Heme a3-Fe-CO and CuB-CO Species in CO-bound ba3-Cytochrome c Oxidase from Thermus thermophilus: EVIDENCE FOR A CHARGE TRANSFER CuB-CO TRANSITION.
E. Pinakoulaki, T. Ohta, T. Soulimane, T. Kitagawa, and C. Varotsis (2004)
J. Biol. Chem. 279, 22791-22794
   Abstract »    Full Text »    PDF »
The Role of the Cross-link His-Tyr in the Functional Properties of the Binuclear Center in Cytochrome c Oxidase.
E. Pinakoulaki, U. Pfitzner, B. Ludwig, and C. Varotsis (2002)
J. Biol. Chem. 277, 13563-13568
   Abstract »    Full Text »    PDF »
The Heme Complex of Hmu O, a Bacterial Heme Degradation Enzyme from Corynebacterium diphtheriae. STRUCTURE OF THE CATALYTIC SITE.
G. C. Chu, T. Tomita, F. D. Sonnichsen, T. Yoshida, and M. Ikeda-Saito (1999)
J. Biol. Chem. 274, 24490-24496
   Abstract »    Full Text »    PDF »
The Heme Environment in Barley Hemoglobin.
T. K. Das, H. C. Lee, S. M. G. Duff, R. D. Hill, J. Peisach, D. L. Rousseau, B. A. Wittenberg, and J. B. Wittenberg (1999)
J. Biol. Chem. 274, 4207-4212
   Abstract »    Full Text »    PDF »
Cyanide-binding Site of bd-type Ubiquinol Oxidase from Escherichia coli.
M. Tsubaki, H. Hori, T. Mogi, and Y. Anraku (1995)
J. Biol. Chem. 270, 28565-28569
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