Occurrence, Classification, and Biological Function of Hydrogenases:  An Overview

Catalytic Hydrogen Evolution by Fe(II) Carbonyls Featuring a Dithiolate and a Chelating Phosphine

“…Liaw and coworkers demonstrated the synthesis of a pentacoordinate, 16-electron Fe(II) complex [Fe(CO) 2 (CN)(S,NH-C 6 H 4 )] -and showed that it readily reacted to form hexacoordinate complexes or dimers. 22 They did not, however, investigate the catalytic activity of this compound.…”

“…Darensbourg and coworkers have also produced pentacoordinate iron dicarbonyls using the strongly π-donating, redox noninnocent ligand 2-amido-thiophenylate as models for the mononuclear Fe-containing hydrogenases. 23,24 Particularly relevant to this work, Sellmann and coworkers employed the benzene-1,2-dithiolate (bdt) ligand to construct [Fe(bdt)(PMe 3 ) 2 (CO) 2 ] and noted that it had an unexpected tendency to lose CO to form a 16 electron complex. 25 Rauchfuss and coworkers used that work as an inspiration to create (Et 4 N) 2 [Fe(bdt)(CN) 2 (CO)], as a spectroscopic model of the enzyme active site.…”

“…23,24 Particularly relevant to this work, Sellmann and coworkers employed the benzene-1,2-dithiolate (bdt) ligand to construct [Fe(bdt)(PMe 3 ) 2 (CO) 2 ] and noted that it had an unexpected tendency to lose CO to form a 16 electron complex. 25 Rauchfuss and coworkers used that work as an inspiration to create (Et 4 N) 2 [Fe(bdt)(CN) 2 (CO)], as a spectroscopic model of the enzyme active site. 26 Only recently did Ott and coworkers report complexes of bdt together with a chelating phosphine to create coordinatively unsaturated monocarbonyl models of the distal iron site of [FeFe]-hydrogenases and to show that these compounds are active in electrocatalytic proton reduction.…”

HydF as a scaffold protein in [FeFe] hydrogenase H‐cluster biosynthesis

“…The [FeFe] and [NiFe] hydrogenases catalyze hydrogen oxidation and proton reduction and function either to couple hydrogen oxidation to energy yielding processes or to regenerate reduced electron carriers accumulated during fermentation [1]. Although phylogenetically unrelated, these enzymes share biologically unique sites containing iron with both cyanide and carbon monoxide ligands [2].…”

Ferric ion (hydr)oxo clusters in the “Venus flytrap” cleft of FbpA: Mössbauer, calorimetric and mass spectrometric studies

“…In general, proteins having non-heme polynuclear iron sites play important roles in a plethora of important physiological reactions including oxygen transport, oxygenases and hydrogenases [11][12][13][14][15][16][17]. Recently it has been shown that a phosphate uptake and transfer protein (Pho U)…”