Hydrogenases (H 2 ases) are metalloproteins. The great majority of them contain iron-sulfur
clusters and two metal atoms at their active center, either a Ni and an Fe atom, the [NiFe]-H 2 …

Hydrogenases (H2ases) catalyze the reversible oxidation of molecular hydrogen and play a
central role in microbial energy metabolism. Most of these enzymes are found in Archaea …

Hydrogenases are metalloenzymes subdivided into two classes that contain iron-sulfur
clusters and catalyze the reversible oxidation of hydrogen gas (H 2⇆ 2H++ 2e−). Two metal …

Most methanogenic archaea reduce CO2 with H2 to CH4. For the activation of H2, they use
different [NiFe]-hydrogenases, namely energy-converting [NiFe]-hydrogenases …

Methanogenic archaea are known to contain two types of [NiFe] hydrogenases designated
F420‐reducing hydrogenase and F420‐non‐reducing hydrogenase. We report here that …

The activation of molecular hydrogen is of interest both from a chemical and biological
viewpoint. The covalent bond of H2 is strong (436 kJ mol− 1). Its cleavage is catalyzed by …

The iron-sulfur cluster-free hydrogenase (Hmd) from methanogenic archaea harbors an iron-
containing cofactor of yet unknown structure. X-ray absorption spectroscopy of the active, as …

Abstract [Fe] hydrogenase (iron–sulfur-cluster-free hydrogenase) catalyzes the reversible
reduction of methenyltetrahydromethanopterin (methenyl-H 4 MPT+) with H 2 to methylene …

H2‐forming methylenetetrahydromethanopterin dehydrogenase (Hmd) is an unusual
hydrogenase present in many methanogenic archaea. The homodimeric enzyme dubbed …

Background The realization of hydrogenase-based technologies for renewable H2
production is presently limited by the need for scalable and high-yielding methods to supply …