Cytochrome c: A Thermodynamic Study of Relationships among Oxidation State, Ion‐Binding and Structural Parameters: 2. Ion‐Binding Linked to Oxidation State

Rimona Margalit; Abel SCHEJTER

doi:10.1111/j.1432-1033.1973.tb02634.x

Cytochrome c: A Thermodynamic Study of Relationships among Oxidation State, Ion‐Binding and Structural Parameters: 2. Ion‐Binding Linked to Oxidation State

Rimona Margalit^*, Abel SCHEJTER

^*Corresponding author for this work

Biochemistry Molecular Biology

Research output: Contribution to journal › Article › peer-review

Abstract

The specific binding of anions to oxidized horse‐heart cytochrome c has been studied by two methods: measuring the effect of ion concentration on the redox potential, and directly by gel nitration. The anions investigated were: chloride, phosphate, ADP and sulfanilate. The binding constants estimated are in the range of 1–10 mM⁻¹, and the number of sites per protein molecule are 1 to 2. The specificity of anion binding to the oxidized protein is demonstrated.

Original language	English
Pages (from-to)	500-505
Number of pages	6
Journal	European Journal of Biochemistry
Volume	32
Issue number	3
DOIs	https://doi.org/10.1111/j.1432-1033.1973.tb02634.x
State	Published - Feb 1973

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AB - The specific binding of anions to oxidized horse‐heart cytochrome c has been studied by two methods: measuring the effect of ion concentration on the redox potential, and directly by gel nitration. The anions investigated were: chloride, phosphate, ADP and sulfanilate. The binding constants estimated are in the range of 1–10 mM−1, and the number of sites per protein molecule are 1 to 2. The specificity of anion binding to the oxidized protein is demonstrated.

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Cytochrome c: A Thermodynamic Study of Relationships among Oxidation State, Ion‐Binding and Structural Parameters: 2. Ion‐Binding Linked to Oxidation State

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