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Publication Abstract from PubMed

The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce H(2) during fermentation, its reversibility, allowing H(2)-dependent CO(2) reduction, and its evolutionary link to respiratory complex I. FHL has been studied for over a century, but its atomic structure remains unknown. Here we report cryo-EM structures of FHL in its aerobically and anaerobically isolated forms at resolutions reaching 2.6 A. This includes well-resolved density for conserved loops linking the soluble and membrane arms believed to be essential in coupling enzymatic turnover to ion translocation across the membrane in the complex I superfamily. We evaluate possible structural determinants of the bias toward hydrogen production over its oxidation and describe an unpredicted metal-binding site near the interface of FdhF and HycF subunits that may play a role in redox-dependent regulation of FdhF interaction with the complex.

Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli.,Steinhilper R, Hoff G, Heider J, Murphy BJ Nat Commun. 2022 Sep 14;13(1):5395. doi: 10.1038/s41467-022-32831-x. PMID:36104349^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.