Aug 25, 2014 · In this work, genetic tools are reported that allow the facile isolation of FHL in a single chromatographic step. The core complex is shown to comprise HycE (a [NiFe] hydrogenase component termed Hyd-3), FdhF (the molybdenum-dependent formate dehydrogenase-H), and three iron-sulfur proteins: HycB, HycF, and HycG.

May 10, 2017 · FHL comprises a formate dehydrogenase (encoded by fdhF) linked directly to [NiFe]-hydrogenase-3 (Hyd-3), and formate is the only natural substrate known for proton reduction by this hydrogenase. In this work, the possibility of engineering an alternative electron donor for hydrogen production has been explored.

Sep 26, 2017 · Escherichia coli cells have three formate dehydrogenases (FDHs), FDH-H, FDN-N and FDH-O. All three FDHs contain selenocysteine and the molybdenum (Mo) cofactor, which are required for their formate dehydrogenase activities. FDH-N complex and FDH-O complex are localized in inner membrane, oxidize formate into CO 2 and reduce quinone to quinol.

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Jun 24, 1997 · By in vitro selection, novel RNA sequences ("aptamers"), which can interact tightly and specifically with SelB, were isolated from an RNA library. The library was comprised of mutagenized variants of the wild-type fdhF mRNA hairpin. One-half of the selected sequences contained the apical stem-loop of the fdhF mRNA hairpin highly conserved.

Analogous mutants, termed fdhD and fdhE, have been isolated in Escherichia coli. We used gene fusions between fdnG, the structural gene for the large subunit of formate dehydrogenase-N, and lacZ, the structural gene for beta-galactosidase, to examine E. coli fdnGHI operon expression in fdhD and fdhE insertion mutants.

Nov 23, 2011 · IscS is one of the three Escherichia colil -cysteine desulfurases. It interacts with FdhD, a protein essential for the activity of formate dehydrogenases (FDHs), which are iron/molybdenum/selenium-containing enzymes. Here, we address the role played by this interaction in the activity of FDH-H (FdhF) in E. coli.

Formate is an important and widespread electron donor available to bacteria in anaerobic environments. During anaerobic growth with nitrate, E. coli can express a membrane-bound formate dehydrogenase (FdhN), which oxidizes formate in the periplasmic compartment and for which a high-resolution structure has been determined.

Feb 26, 2008 · Repressed by oxygen, nitrate, nitrite, and other electron acceptors. Consists of two separable enzymatic activities: a formate dehydrogenase component (FDH-H) and …

Genome analysis of Clostridium bovifaecis revealed that it contains almost the complete genes of the Wood-Ljungdahl pathway but lacks the gene encoding formate dehydrogenase, which catalyzes the reduction of CO 2 to formate as the first step of the methyl branch of the Wood-Ljungdahl pathway.