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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.

SUBMITTER: Ash PA 

PROVIDER: S-EPMC5708527 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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

Ash P A PA   Carr S B SB   Reeve H A HA   Skorupskaitė A A   Rowbotham J S JS   Shutt R R   Frogley M D MD   Evans R M RM   Cinque G G   Armstrong F A FA   Vincent K A KA  

Chemical communications (Cambridge, England) 20170501 43

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. ...[more]

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