One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

Ever since the discovery of hydrogenases over 90 years ago (Stephenson and Stickland,
1931), their structure and mechanism of action have been intensively investigated. Of the …

Hydrogenases are the most active molecular catalysts for hydrogen production and uptake,,
and could therefore facilitate the development of new types of fuel cell,,. In [FeFe] …

Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-
hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose …

Fe–S clusters are partners in the origin of life that predate cells, acetyl-CoA metabolism,
DNA, and the RNA world. The double helix solved the mystery of DNA replication by base …

[FeFe]-hydrogenases are complex metalloenzymes, key to microbial energy metabolism in
numerous organisms. During anaerobic metabolism, they dissipate excess reducing …

Both photo-and biocatalysis are well-established and intensively studied. The combination
of these two approaches is also an emerging research field, commonly referred to as semi …

Hydrogenases are redox enzymes that catalyze the conversion of protons and molecular
hydrogen (H2). Based on the composition of the active site cofactor, the monometallic [Fe] …

The enzyme FeFe-hydrogenase catalyzes H2 evolution and oxidation at an active site that
consists of a [4Fe-4S] cluster bridged to a [Fe2 (CO) 3 (CN) 2 (azadithiolate)] subsite …

H2 turnover at the [FeFe]-hydrogenase cofactor (H-cluster) is assumed to follow a reversible
heterolytic mechanism, first yielding a proton and a hydrido-species which again is double …