Many microorganisms can use molecular hydrogen as a source of electrons or generate it
by reducing protons. These reactions are catalysed by metalloenzymes of two types: NiFe …

The iron− sulfur-cluster-free hydrogenase Hmd (H2-forming
methylenetetrahydromethanopterin dehydrogenase) from methanogenic archaea has …

Enzymes possessing the capacity to oxidize molecular hydrogen have developed
convergently three class of enzymes leading to:[FeFe]-,[NiFe]-, and [FeS]-cluster-free …

Thirty sequenced microbial hydrogenases are classified into six classes according to
sequence homologies, metal content and physiological function. The first class contains …

The distribution of [Fe]-hydrogenases was once thought to be limited to a small number of
bacteria and a few peculiar hydrogen-producing anaerobic eukaryotes. However, it is now …

The iron–sulphur cluster-free hydrogenase (Hmd, EC 1.12. 98.2) from methanogenic
archaea is a novel type of hydrogenase that tightly binds an iron-containing cofactor. The …

Abstract [NiFe]‐hydrogenases catalyze the oxidation of H2 to protons and electrons. This
reversible reaction is based on a complex interplay of metal cofactors including the Ni–Fe …

Recent physiological and ecological studies have challenged the long-held belief that
microbial metabolism of molecular hydrogen (H2) is a niche process. To gain a broader …

Most hydrogenases (H 2 ases), the enzymes that produce or oxidize dihydrogen, possess
dimetallic active sites and belong to either one of two phylogenetically distinct classes, the …

Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic,
or sulfate-reducing bacteria, metabolize hydrogen.[1, 2a] Hydrogen activation is mediated by …