Numerous recent developments in the biochemistry, molecular biology, and physiology of
formate and H2 metabolism and of the [NiFe]-hydrogenase (Hyd) cofactor biosynthetic …

Iron/sulfur clusters are key cofactors in proteins involved in a large number of conserved
cellular processes, including gene expression, DNA replication and repair, ribosome …

Abstract [NiFe]-hydrogenases have a bimetallic NiFe (CN) 2CO cofactor in their large,
catalytic subunit. The 136 Da Fe (CN) 2CO group of this cofactor is preassembled on a …

We report the decomposition of formic acid to hydrogen and carbon dioxide, catalysed by a
NiRu complex originally developed as a [NiFe] hydrogenase model. This is the first example …

Molecular hydrogen (H2) can be produced in green microalgae by [FeFe]‐hydrogenases as
a direct product of photosynthesis. The Chlamydomonas reinhardtii hydrogenase HYDA 1 …

Abstract [NiFe]-hydrogenases (Hyd) are redox-active metalloenzymes that catalyze the
reversible oxidation of molecular hydrogen to protons and electrons. These enzymes are …

Escherichia coli is a Gram-negative bacterium that is a workhorse for biotechnology. The
organism naturally performs a mixed-acid fermentation under anaerobic conditions where it …

Iron sulfur (Fe-S) clusters are important biological cofactors present in proteins with crucial
biological functions, from photosynthesis to DNA repair, gene expression, and bioenergetic …

Fermentatively growing Escherichia coli cells have three active [NiFe]-hydrogenases (Hyd),
two of which, Hyd-1 and Hyd-2, contribute to H2 oxidation while Hyd-3 couples formate …

The selenate reductase in Escherichia coli is a multi-subunit enzyme predicted to bind Fe–S
clusters. In this study, we examined the iron–sulfur cluster biosynthesis genes that are …