6g94
From Proteopedia
Structure of E. coli hydrogenase-1 C19G variant in complex with cytochrome b
Structural highlights
Function[MBHS_ECOLI] This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. [CYBH_ECOLI] Probable b-type cytochrome. [MBHL_ECOLI] This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. Publication Abstract from PubMedThe crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni-Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype. X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe-4S] cluster.,Volbeda A, Mouesca JM, Darnault C, Roessler MM, Parkin A, Armstrong FA, Fontecilla-Camps JC Chem Commun (Camb). 2018 Jun 11. doi: 10.1039/c8cc02896f. PMID:29888350[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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