Open AccessStepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamics
Author(s) -
Moritz Senger,
Stefan Mebs,
Jifu Duan,
Florian Wittkamp,
UlfPeter Apfel,
Joachim Heberle,
Michael Haumann,
Sven T. Stripp
Publication year - 2016
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1606178113
Subject(s) - hox gene , chemistry , ligand (biochemistry) , photochemistry , carbon monoxide , active site , isotopic labeling , catalysis , cofactor , crystallography , stereochemistry , enzyme , organic chemistry , transcription factor , receptor , biochemistry , gene
Significance [FeFe]-hydrogenases are H2 -forming enzymes with potential in renewable energy applications. Their molecular mechanism of catalysis needs to be understood. A protocol for specific13 CO isotope editing of all carbon monoxide ligands at the six-iron cofactor (H-cluster) was established. Analysis of vibrational modes via quantum chemical calculations implies structural dynamics at the H-cluster in the active-ready state. Site-selective introduction of isotopic reporter groups opens new perspectives to identify intermediates in the catalytic cycle.
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