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Interaction between adrenodoxin and cytochrome c.

L M Geren, F Millett

The Journal of Biological Chemistry

|May 25, 1981

Summary

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Horse heart ferricytochrome c reduction by reduced adrenodoxin follows second-order kinetics. Specific lysine residues near the heme crevice are crucial for this protein-protein interaction.

Area of Science:

Biochemistry
Protein-protein interactions
Electron transfer reactions

Background:

Cytochrome c and adrenodoxin are key electron transfer proteins.
Understanding their interaction is vital for cellular respiration and metabolic pathways.

Purpose of the Study:

To elucidate the kinetics and mechanism of horse heart ferricytochrome c reduction by reduced adrenodoxin.
To identify the specific residues involved in the electrostatic interactions between these two proteins.

Main Methods:

Stopped-flow spectroscopy to determine reaction kinetics.
Temperature dependence studies to calculate activation parameters.
Chemical modification of lysine residues on cytochrome c to assess their role in the interaction.

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Main Results:

The reaction follows second-order kinetics with a rate constant of 7.8 x 10^6 M^-1 s^-1.
Activation parameters indicate a specific transition state.
Lysine residues 13, 27, 72, and 79 surrounding the heme crevice significantly impact the reaction rate, suggesting a defined interaction domain.

Conclusions:

Electrostatic interactions, particularly involving specific lysine residues near the heme crevice of cytochrome c, are critical for the reduction by adrenodoxin.
A semi-empirical model accurately describes the electrostatic interactions governing this electron transfer process.