Issue 43, 2017

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

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

Supplementary files

Article information

Article type
Communication
Submitted
04 Apr 2017
Accepted
09 May 2017
First published
09 May 2017
This article is Open Access
Creative Commons BY license

Chem. Commun., 2017,53, 5858-5861

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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