Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/44470
Title: Generating single metalloprotein crystals in well-defined redox states: electrochemical control combined with infrared imaging of a NiFe hydrogenase crystal.
Authors: Ash, PA
Carr, SB
Reeve, HA
Skorupskaitė, A
Rowbotham, JS
Shutt, R
Frogley, MD
Evans, RM
Cinque, G
Armstrong, FA
Vincent, KA
First Published: 9-May-2017
Publisher: Royal Society of Chemistry
Citation: Chemical Communications, 2017, 53 (43), pp. 5858-5861
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.
DOI Link: 10.1039/c7cc02591b
eISSN: 1364-548X
Links: https://pubs.rsc.org/en/content/articlelanding/2017/CC/C7CC02591B#!divAbstract
http://hdl.handle.net/2381/44470
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2017. This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description: Electronic supplementary information (ESI) available: Crystal preparation; cyclic voltammogram in the experimental cell; position-dependent difference spectra; demonstration of control over all active sites; visible images of a crystal recorded periodically during measurements; time-dependent Nia-R formation. See DOI: 10.1039/c7cc02591b
Appears in Collections:Published Articles, Dept. of Chemistry

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