Cytochrome c: A Thermodynamic Study of the Relationship among Oxidation State, Ion‐Binding and Structural Parameters Cation Binding to Horse‐Heart Ferrocytochrome c

Rimona MARGALIT*, Abel SCHEJTER

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability constants are in the range of 5–8 mM−1, and the number of binding sites per protein molecule are 1 to 2. The temperature dependence of the stability constant for the Mg2+‐ferrocytochrome system was measured. The thermodynamic parameters were found to be: ΔH0obs=+ 12 kcal/mol, ΔG0obs, (25°C) =−5.6 kcal/mol and ΔS0obs=+ 57 cal × mob1× K−1.

Original languageEnglish
Pages (from-to)387-391
Number of pages5
JournalEuropean Journal of Biochemistry
Volume46
Issue number2
DOIs
StatePublished - Jul 1974

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