ArticleChemical communications (Cambridge, England)2017
Generating single metalloprotein crystals in well-defined redox states: electrochemical control combined with infrared imaging of a NiFe hydrogenase crystal.
Article in Chemical communications (Cambridge, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Crystallise, poise, capture: a multimodal platform for correlated structural and spectroscopic characterisation of redox enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Lessons, connections, hypotheses and predictions from protein film electrochemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Review
- Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis.Current opinion in structural biology · 2021Review
- The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase.Chemical science · 2021Article
- Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies.Molecules (Basel, Switzerland) · 2021Review
- Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes.Angewandte Chemie (International ed. in English) · 2021Article
Corrections and comments
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Authors and funding
11 authors.
Funding
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.
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Registered trials
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