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Science 25 November 1983:
Vol. 222. no. 4626, pp. 929 - 931
DOI: 10.1126/science.6415814
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Articles

Science, Vol 222, Issue 4626, 929-931
Copyright © 1983 by American Association for the Advancement of Science

articles

Heme-heme orientation and electron transfer kinetic behavior of multisite oxidation-reduction enzymes

MW Makinen, SA Schichman, SC Hill, and HB Gray

Analysis of the polarized single-crystal absorption spectra of cytochrome cd1 of Pseudomonas aeruginosa shows that the heme c and heme d1 groups in each subunit are oriented perpendicularly to each other in both oxidized and reduced forms of the enzyme. These results, together with those of previous kinetic studies, indicate that a perpendicular heme-heme orientation may be an important factor in specifying kinetically slow steps in a sequential series of electron transfer reactions.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Peroxidation of a Specific Tryptophan of Metmyoglobin by Hydrogen Peroxide.
J. A. DeGray, M. R. Gunther, R. Tschirret-Guth, P. R.O. de Montellano, and R. P. Mason (1997)
J. Biol. Chem. 272, 2359-2362
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Molecular dynamics of a cytochrome c-cytochrome b5 electron transfer complex.
J. Wendoloski, J. Matthew, P. Weber, and F. Salemme (1987)
Science 238, 794-797
   Abstract »    PDF »
Long-range electron transfer in heme proteins.
S. Mayo, W. Ellis Jr, R. Crutchley, and H. Gray (1986)
Science 233, 948-952
   Abstract »    PDF »


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