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

Hydrogenases are microbial metalloenzymes capable of catalyzing the reversible
interconversion between molecular hydrogen and protons with high efficiency, and have …

Hydrogenases are enzymes of great biotechnological relevance because they catalyse the
interconversion of H2, water (protons) and electricity using non-precious metal catalytic …

Escherichia coli uptake hydrogenase 2 (Hyd-2) catalyzes the reversible oxidation of H2 to
protons and electrons. Hyd-2 synthesis is strongly upregulated during growth on glycerol or …

Under anaerobic conditions, Escherichia coli is able to metabolize molecular hydrogen via
the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically …

During mixed‐acid fermentation Escherichia coli produces formate, which is initially
excreted out the cell. Accumulation of formate, and drop** extracellular pH, leads to …

Microbial Ni2+ homeostasis underpins the virulence of several clinical pathogens. Ni2+ is
an essential cofactor in urease and [NiFe]-hydrogenases involved in colonization and …

[NiFe]-hydrogenases (Hyds) comprise a small and a large subunit. The latter harbors the
biologically unique [NiFe](CN) 2 CO active-site cofactor. The maturation process includes …

The HypC and HypD maturases are required for the biosynthesis of the Fe (CN) 2CO
cofactor in the large subunit of [NiFe]-hydrogenases. Using infrared spectroscopy we …

Metalloenzymes catalyze complex and essential processes, such as photosynthesis,
respiration, and nitrogen fixation. For example, bacteria and archaea use [NiFe] …