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Issue 43, 2017
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Generating single metalloprotein crystals in well-defined redox states: electrochemical control combined with infrared imaging of a NiFe hydrogenase crystal

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Abstract

We describe an approach to generating and verifying well-defined redox states in metalloprotein single crystals by combining electrochemical control with synchrotron infrared microspectroscopic imaging. For NiFe hydrogenase 1 from Escherichia coli we demonstrate fully reversible and uniform electrochemical reduction from the oxidised inactive to the fully reduced state, and temporally resolve steps during this reduction.

Graphical abstract: Generating single metalloprotein crystals in well-defined redox states: electrochemical control combined with infrared imaging of a NiFe hydrogenase crystal

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Article information


Submitted
04 Apr 2017
Accepted
09 May 2017
First published
09 May 2017

This article is Open Access

Chem. Commun., 2017,53, 5858-5861
Article type
Communication

Generating single metalloprotein crystals in well-defined redox states: electrochemical control combined with infrared imaging of a NiFe hydrogenase crystal

P. A. Ash, S. B. Carr, H. A. Reeve, A. Skorupskaitė, J. S. Rowbotham, R. Shutt, M. D. Frogley, R. M. Evans, G. Cinque, F. A. Armstrong and K. A. Vincent, Chem. Commun., 2017, 53, 5858
DOI: 10.1039/C7CC02591B

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