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Cytochrome P-450cam and putidaredoxin interaction during electron transfer.

J A Peterson, D M Mock

Acta Biologica Et Medica Germanica

|January 1, 1979

Summary

The reduction of cytochrome P-450cam by putidaredoxin follows first-order kinetics, indicating rapid bimolecular complex formation. This complex formation is crucial for activating molecular oxygen in this bacterial monooxygenase reaction.

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Area of Science:

Biochemistry
Enzymology
Electron Transfer

Background:

Cytochrome P-450cam catalyzes camphor hydroxylation, requiring two electrons for oxygen activation.
Putidaredoxin serves as the physiological electron donor for cytochrome P-450cam.
The electron transfer occurs in two distinct one-electron steps.

Purpose of the Study:

To investigate the kinetics of cytochrome P-450cam reduction by putidaredoxin.
To elucidate the mechanism of electron transfer between these two proteins.
To provide direct evidence for the formation of a protein-protein complex during the reaction.

Main Methods:

Kinetic analysis of cytochrome P-450cam reduction.
Spectroscopic methods including UV-Vis absorbance and Electron Paramagnetic Resonance (EPR).
Freeze-quenching technique to capture transient intermediates.

Main Results:

The reaction exhibits first-order kinetics with a rate constant of 33 s⁻¹ at 25°C.
Evidence for rapid bimolecular complex formation between reduced putidaredoxin and Fe(III) cytochrome P-450cam.
Direct EPR observation of complex formation, showing loss of Fe(III) cytochrome P-450cam signal and decay of reduced putidaredoxin signal.

Conclusions:

The reduction of cytochrome P-450cam by putidaredoxin proceeds via a pre-equilibrium bimolecular complex.
Complex formation is a key step in the electron transfer pathway for camphor hydroxylation.
Further studies are needed to understand the conformational changes in cytochrome P-450cam upon complexation.

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