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

DOI: 10.1039/C7CC02591B DOI Help

Authors: Philip A. Ash (University of Oxford) , Stephen B. Carr (Research Complex at Harwell; University of Oxford) , Holly A. Reeve (University of Oxford) , Aiste Skorupskaite (University of Oxford) , Jack Rowbotham (University of Oxford) , Rebecca Shutt (University of Oxford) , Mark Frogley (Diamond Light Source) , Rhiannon Mari Evans (University of Oxford) , Gianfelice Cinque (Diamond Light Source) , Fraser A Armstrong (University of Oxford) , Kylie A Vincent (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chem. Commun.

State: Published (Approved)
Published: May 2017
Diamond Proposal Number(s): 13879

Abstract: We describe an approach to generating and verifying well-defined redox states in metalloprotein single crystals by combining electrochemical control with synchtroton 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.

Subject Areas: Chemistry

Instruments: B22-Multimode InfraRed imaging And Microspectroscopy

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