1H-n.m.r. Investigation of the Interaction Between Cytochrome C and Cytochrome B5

Overview

Journal Biochem J

Specialty Biochemistry

Date 1983 Oct 1

PMID 6312971

Citations 10

Authors

C G Eley

G R MOORE

Affiliations

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Abstract

The interaction between eukaryotic cytochrome c and the tryptic fragment of bovine liver microsomal cytochrome b5 was studied by 1H-n.m.r. spectroscopy, and a procedure was developed that may be generally applicable to the study of macromolecular interactions by n.m.r. At pH6.3 (27 degrees C, I approx. 0.04) the two ferricytochromes were found to form a 1:1 complex with an association constant of approx. 10(3) M -1. The protein--protein-interaction region was found to encompass the region of the surface of horse cytochrome c that includes Ile-81, Phe-82, Ala-83 and Ile-85, and Lys-13 and Lys-72 of horse cytochrome c were suggested to be involved in two important intermolecular interactions. Me3Lys-72 of Candida krusei cytochrome c was shown to be involved in the interaction.

Citing Articles

Kinetic and Structural Characterization of the Effects of Membrane on the Complex of Cytochrome b and Cytochrome c.

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Characterization and calculation of a cytochrome c-cytochrome b5 complex using NMR data.

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The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK.

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A further investigation of the cytochrome b5-cytochrome c complex.

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Effects of charged amino-acid mutation on the solution structure of cytochrome b(5) and binding between cytochrome b(5) and cytochrome c.

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