PMID: 2158816Feb 20, 1990

Kinetics of cyanide binding to Chromatium vinosum ferricytochrome c'

Biochemistry
M MotieM A Cusanovich

Abstract

The kinetics of the reversible binding of cyanide by the ferric cytochrome c' from Chromatium vinosum have been studied over the pH range 6.9-9.6. The reaction is extremely slow at neutral pH compared to the reactions of other high-spin ferric heme proteins with cyanide. The observed bimolecular rate constant at pH 7.0 is 2.25 X 10(-3) M-1 s-1, which is approximately 10(7)-fold slower than that for peroxidases, approximately 10(5)-fold slower than those for hemoglobin and myoglobin, and approximately 10(2)-fold to approximately 10(3)-fold slower than that recently reported for the Glycera dibranchiata hemoglobin, which has anomalously slow cyanide rate constants of 4.91 X 10(-1), 3.02 X 10(-1), and 1.82 M-1 s-1 for components II, III, and IV, respectively [Mintorovitch, J., & Satterlee, J. D. (1988) Biochemistry 27, 8045-8050; Mintorovitch, J., Van Pelt, D., & Satterlee, J. D. (1989) Biochemistry 28, 6099-6104]. The unusual ligand binding property of this cytochrome c' is proposed to be associated with a severely hindered heme coordination site. Cyanide binding is also characterized by a nonlinear cyanide concentration dependence of the observed rate constant at higher pH values, which is interpreted as involving a change in th...Continue Reading

References

Jan 8, 1991·Biochimica Et Biophysica Acta·M MotieM A Cusanovich
Jun 16, 2012·The Journal of Biological Chemistry·Célia Caillet-SaguyAnne Lecroisey
Sep 15, 1996·European Journal of Biochemistry·J A ZahnA A Dispirito
Mar 5, 2008·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Rastislav Varhac, Marián Antalík
Jun 24, 2009·Biophysical Chemistry·Rastislav VarhacErik Sedlák
May 23, 1991·Biochimica Et Biophysica Acta·R J Kassner
Dec 29, 2007·The Journal of Biological Chemistry·Célia Caillet-SaguyAnne Lecroisey

Citations

May 1, 1976·Quarterly Reviews of Biophysics·M M Maltempo
Apr 19, 1977·Biochemistry·J RawlingsM D KAMEN
Nov 25, 1977·Biochimica Et Biophysica Acta·M H EmptageW H Orme-Johnson
Jul 14, 1987·Biochemistry·M Ikeda-Saito
Sep 20, 1985·Biochimica Et Biophysica Acta·R J KassnerM A Cusanovich
Jul 22, 1965·Biochimica Et Biophysica Acta·A Ehrenberg, M D KAMEN
Apr 11, 1974·Biochimica Et Biophysica Acta·M M MaltempoM A Cusanovich
Dec 1, 1970·Archives of Biochemistry and Biophysics·M A CusanovichM D KAMEN
Nov 1, 1968·Biochemistry·D DolmanM Morrison
Jul 17, 1980·Nature·P C WeberF R Salemme
Nov 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·R P AmblerJ Van Beeumen
Apr 1, 1961·Biochimica Et Biophysica Acta·T HORIO, M D KAMEN
Aug 13, 1963·Biochimica Et Biophysica Acta·S TANIGUCHI, M D KAMEN
Feb 1, 1952·The Biochemical Journal·P GEORGE, C L TSOU

Related Concepts

Ligand Binding
Chromatium
Peroxidases
Isocyanides
Cytochrome c Group
Plasma Protein Binding Capacity
Potassium Cyanide (K(C(15)N))
Hemoglobin Measurement
Hemeproteins
Myoglobin

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