Mechanisms of the Reactions of Cytochrome c
作者： Norman Sutin , John K. Yandell
DOI: 10.1016/S0021-9258(19)44675-9
关键词: Ionic strength 、 Equilibrium constant 、 Cytochrome c 、 Stereochemistry 、 Pyridine 、 Chemistry 、 Azide 、 Imidazole 、 Reaction rate constant 、 Kinetics 、 Medicinal chemistry 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: Abstract Kinetic and equilibrium data for the binding of azide, imidazole, pyridine to horse heart ferricytochrome c have been obtained by conventional spectrophotometric stopped flow techniques. The stability constants 1:1 complexes formed between ligands are: 4.5 m-1; 15.3 pyridine, 2.4 m-1, at 25°, pH 7, 1.0 m ionic strength. These measurements are consistent with a model in which added bind iron displacing coordinated methionine-80. kinetic indicate rate constant about 60 s-1 rupture iron-sulfur bond.
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sci-hub.st 参考文章(20)
P. George, C. L. Tsou, Reaction between hydrocyanic acid, cyanide ion and ferricytochrome c Biochemical Journal. ,vol. 50, pp. 440- 448 ,(1952) , 10.1042/BJ0500440
Arthur Kowalsky, A study of the mechanism of electron transfer in cytochrome c. Chromium as a probe. Journal of Biological Chemistry. ,vol. 244, pp. 6619- 6625 ,(1969) , 10.1016/S0021-9258(18)63451-9
Colin Greenwood, Graham Palmer, Evidence for the Existence of Two Functionally Distinct Forms of Cytochrome c Monomer at Alkaline pH Journal of Biological Chemistry. ,vol. 240, pp. 3660- 3663 ,(1965) , 10.1016/S0021-9258(18)97195-4
Richard E. Dickerson, Tsunehiro Takano, David Eisenberg, Olga B. Kallai, Lalli Samson, Angela Cooper, E. Margoliash, Ferricytochrome c: I. GENERAL FEATURES OF THE HORSE AND BONITO PROTEINS AT 2.8 A RESOLUTION Journal of Biological Chemistry. ,vol. 246, pp. 1511- 1535 ,(1971) , 10.1016/S0021-9258(19)77002-1
Douglas E. Goldsack, Wolfgang S. Eberlein, Robert A. Alberty, Temperature Jump Studies of Sperm Whale Metmyoglobin III. EFFECT OF HEME-LINKED GROUPS ON LIGAND BINDING Journal of Biological Chemistry. ,vol. 241, pp. 2653- 2660 ,(1965) , 10.1016/S0021-9258(18)96589-0
Philip George, Stanley C. Glauser, A. Schejter, The Reactivity of Ferricytochrome c with Ionic Ligands Journal of Biological Chemistry. ,vol. 242, pp. 1690- 1695 ,(1967) , 10.1016/S0021-9258(18)96056-4
Karl G. Brandt, Paul C. Parks, Georg H. Czerlinski, George P. Hess, On the elucidation of the pH dependence of the oxidation-reduction potential of cytochrome c at alkaline pH. Journal of Biological Chemistry. ,vol. 241, pp. 4180- 4185 ,(1966) , 10.1016/S0021-9258(18)99768-1
S.K. Chan, E. Margoliash, Properties and Primary Structure of the Cytochrome c from the Flight Muscles of the Moth, Samia cynthia Journal of Biological Chemistry. ,vol. 241, pp. 335- 348 ,(1966) , 10.1016/S0021-9258(18)96922-X
Michael H. Klapper, Hiroshi Uchida, Nonequivalent Binding to Human Methemoglobin THERMODYNAMIC AND KINETIC COMPARISON Journal of Biological Chemistry. ,vol. 246, pp. 6849- 6854 ,(1971) , 10.1016/S0021-9258(19)45924-3
E. Margoliash, Nehamah Frohwirt, Edith Wiener, A study of the cytochrome c haemochromogen Biochemical Journal. ,vol. 71, pp. 559- 570 ,(1959) , 10.1042/BJ0710559