4jjg
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Crystal structure of FE-hydrogenase from methanothermobacter marburgensis in complex with toluenesulfonylmethylisocyanide
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Structural highlights
FunctionHMD_METTM Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT. Publication Abstract from PubMedInhibition mechanism: Isocyanides strongly inhibit [Fe]-hydrogenase. X-ray crystallography and X-ray absorption spectroscopy revealed that the isocyanide binds to the trans position, versus the acyl carbon of the Fe center, and is covalently bound to the pyridinol hydroxy oxygen. These results also indicated that the hydroxy group is essential for H2 activation. Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H -Activation Site.,Tamura H, Salomone-Stagni M, Fujishiro T, Warkentin E, Meyer-Klaucke W, Ermler U, Shima S Angew Chem Int Ed Engl. 2013 Jul 22. doi: 10.1002/anie.201305089. PMID:23873755[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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