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Electron tunneling in protein crystals.

F A Tezcan¹, B R Crane, J R Winkler

¹Beckman Institute, MC 139-74, California Institute of Technology, Pasadena, CA 91125, USA.

Proceedings of the National Academy of Sciences of the United States of America

|April 11, 2001

Summary

Electron tunneling rates between proteins in crystals match intraprotein transfer, revealing van der Waals and hydrogen bonds facilitate electron flow across interfaces.

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Area of Science:

Biophysics
Protein Crystallography
Electron Transfer

Background:

Understanding electron tunneling through proteins is limited by fixed donor-acceptor systems.
Factors controlling interprotein electron flow are unclear due to structural uncertainties.

Purpose of the Study:

To investigate electron transfer kinetics between proteins in a crystalline environment.
To resolve structural ambiguities in interprotein electron transfer.

Main Methods:

Studied oxidation-reduction reactions in protein crystals.
Measured electron transfer rates between native and Zn-substituted tuna cytochrome c (cyt c) in crystals of known structure.

Main Results:

Electron transfer rates between Zn-cyt c and Fe(III)-cyt c (320 s⁻¹) and Fe(II)-cyt c and Zn-cyt c⁺ (2000 s⁻¹) were measured.

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Observed rates over a 24.1 Å distance closely matched intraprotein electron tunneling rates.

Identified van der Waals interactions and water-mediated hydrogen bonds as effective coupling elements.

Conclusions:

Protein crystals provide a method to overcome structural ambiguities in studying interprotein electron transfer.
Van der Waals forces and hydrogen bonds facilitate electron tunneling across protein-protein interfaces.