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Issue 40, 2014
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Control of cytochrome c redox reactivity through off-pathway modifications in the protein hydrogen-bonding network

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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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Publication details

The article was received on 15 Oct 2013, accepted on 16 Dec 2013 and first published on 16 Dec 2013


Article type: Communication
DOI: 10.1039/C3CC47943A
Citation: 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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