Determination of iron-ligand bond lengths in ferric and ferrous horse heart cytochrome c using multiple-scattering analyses of XAFS data
Cytochrome c (cyt c) is a small heme protein (MW 12 384) that functions as a biological electron-transfer agent. It consists of a single polypeptide chain and a prosthetic heme group and provides a pathway for the transfer of electrons from cyt c reductase to cyt c oxidase in the mitochondrial respiratory chain (oxidative phosphorylation). The protein participates in oxidation-reduction reactions with the heme iron alternating between the oxidized (ferric, Fe{sup III}) state and the reduced (ferrous, Fe{sup II}) state. X-ray absorption fine structure (XAFS) data were obtained from frozen aqueous solutions (10 K) of horse heart ferri- and ferrocyt c. Models of the structure about the Fe center were refined to optimize the fit between the observed XAFS in the range 0 {le} k {le} 16.3 {angstrom}{sup {minus}1} and the XAFS calculated using both single-scattering (SS) and multiple-scattering (MS) calculations. The bond lengths obtained are more accurate and precise than those determined previously for cyt c from various species using X-ray crystallography. The Fe-N bond lengths are 1.98--1.99 {angstrom} for both oxidation states of cyt c. The Fe-S bond of derricyt c (2.33 {angstrom}) is significantly longer than that of ferrocyt c (2.29 {angstrom}). The small changes in the bond lengths are consistent with the small reorganizational energy required for the fast electron-transfer reaction of cyt c.
- Research Organization:
- Univ. of Sydney, New South Wales (AU)
- OSTI ID:
- 20013076
- Journal Information:
- Inorganic Chemistry, Vol. 38, Issue 25; Other Information: PBD: 13 Dec 1999; ISSN 0020-1669
- Country of Publication:
- United States
- Language:
- English
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