Issue 40, 2014

Control of cytochrome c redox reactivity through off-pathway modifications in the protein hydrogen-bonding network

Abstract

Measurements of photoinduced Fe2+-to-Ru3+ electron transfer (ET), supported by theoretical analysis, demonstrate that mutations off the dominant ET pathways can strongly influence the redox reactivity of cytochrome c. The effects arise from the change in the protein dynamics mediated by the intraprotein hydrogen-bonding network.

Graphical abstract: Control of cytochrome c redox reactivity through off-pathway modifications in the protein hydrogen-bonding network

Supplementary files

Article information

Article type
Communication
Submitted
15 Oct 2013
Accepted
16 Dec 2013
First published
16 Dec 2013

Chem. Commun., 2014,50, 5355-5357

Control of cytochrome c redox reactivity through off-pathway modifications in the protein hydrogen-bonding network

J. Gu, S. Yang, A. J. Rajic, I. V. Kurnikov, T. R. Prytkova and E. V. Pletneva, Chem. Commun., 2014, 50, 5355 DOI: 10.1039/C3CC47943A

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