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Published November 15, 1982 | Published
Journal Article Open

Preparation and characterization of a pentaammineruthenium(III) derivative of horse heart ferricytochrome c

Abstract

A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)3+/2+, 0.15 V (vs. normal hydrogen electrode).

Additional Information

© 1982 by the National Academy of Sciences. Contributed by Harry B. Gray, August 23, 1982. Our research on cytochrome c derivatives has been aided greatly by numerous discussions with Dick Dickerson, Walther Ellis, John Hopfield, Bo Malmstrom, Rudy Marcus, Chuck Root, Norman Sutin, Henry Taube, and Henrique Toma. NMR spectra were obtained at the Stanford University NMR Laboratory (supported by National Science Foundation Grant GP23633 and National Institutes of Health Grant RR 00711). Research at California Institute of Technology was supported by National Science Foundation Grant CHE80-24863 (K.M.Y., E.B., and H.B.G.) and by National Institutes of Health Grant HL 02558 (J.B.S., J.R.S., and W.A.S.). Research at Rutgers University was supported by National Institutes of Health Grant GM 26324 (S.S.1.). S.S.I. acknowledges a National Institutes of Health Career Development Award (AM 00734) (1980-1985) and a Camille and Henry Dreyfus Teacher-Scholar Award. This is contribution no. 6706 from the Arthur Amos Noyes Laboratory. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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August 22, 2023
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