Issue 40, 2014
From the journal:

Chemical Communications

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

Jie Gu,a   Soyeun Yang,a   Alexander J. Rajic,b   Igor V. Kurnikov,c   Tatiana R. Prytkovab  and  Ekaterina V. Pletneva*a  

* Corresponding authors

a Department of Chemistry, Dartmouth College, Hanover, NH 03755, USA
E-mail: ekaterina.pletneva@dartmouth.edu
Tel: +1-603-646-0933

b Schmid College of Science & Technology, Chapman University, Orange, CA 92866, USA

c Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA 15213, USA

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

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Article information

DOI
https://doi.org/10.1039/C3CC47943A
Article type
Communication
Submitted
15 Here 2013
Accepted
16 Ker. 2013
First published
16 Ker. 2013

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

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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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