Coordination Chemistry of a Model for the GP Cofactor in the Hmd Hydrogenase:  Hydrogen-Bonding and Hydrogen-Transfer Catalysis

Royer, Aaron M.; Rauchfuss, Thomas B.; Wilson, Scott R.

doi:10.1021/ic7018692

Cited by 51 publications

(24 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…All solvents were dried and degassed prior to use. Literature procedures afforded the following reagents: 2-diphenylphosphinobenzoic acid, 41 2,6-dimesitylphenylthiol, 2,4,6-triisopropylthiol, 42 2-hydroxy-4-methylpyridine-6-acetic acid, 43 [H(Et 2 O)]BAr F 4 , 44 and Fe(bda)(CO) 3 . 45 Benzenethiol, 2-methyl-2-propanethiol, ethanethiol, TsCH 2 NC, and Et 4 NCN were purchased from Sigma-Aldrich.…”

Section: Methodsmentioning

confidence: 99%

Iron Acyl Thiolato Carbonyls: Structural Models for the Active Site of the [Fe]-Hydrogenase (Hmd)

et al. 2010

Self Cite

View full text Add to dashboard Cite

Phosphine-modified thioester derivatives are shown to serve as efficient precursors to phosphine-stabilized ferrous acyl thiolato carbonyls via the reaction of phosphine thioesters and sources of Fe(0). The reaction generates both Fe(SPh)(Ph2PC6H4CO)(CO)3 (1) and the diferrous diacyl Fe2(SPh)2(CO)3(Ph2PC6H4CO)2, which carbonylates to give 1. For the extremely bulky arylthioester Ph2PC6H4C(O)SC6H4-2,6-(2,4,6-trimethylphenyl)2, oxidative addition is arrested and the Fe(0) adduct of the phosphine is obtained. Complex 1 reacts with cyanide to give Et4N[Fe(SPh)(Ph2PC6H4CO)(CN)(CO)2] (Et4N[2]). 13C and 31P NMR spectra indicate that substitution is stereospecific and cis to P. The IR spectrum of [2]− in CH2Cl2 solution very closely matches that for HmdCN. XANES and EXAFS measurements also indicate close structural and electronic similarity of Et4N[2] to the active site of wild-type Hmd. Complex 1 also stereospecifically forms a derivative with TsCH2NC, but the adduct is more labile than Et4N[2]. Tricarbonyl 1 was found to reversibly protonate to give a thermally labile derivative, IR measurements of which indicate that the acyl and thiolate ligands are probably not protonated in Hmd.

show abstract

Section: Methodsmentioning

confidence: 99%

Iron Acyl Thiolato Carbonyls: Structural Models for the Active Site of the [Fe]-Hydrogenase (Hmd)

et al. 2010

Self Cite

View full text Add to dashboard Cite

show abstract

“…[41] Artificial H 2 ases inspired by Hmd are just appearing. [42,43] As with the other artificial H 2 ases, phosphine ligands are useful as illustrated by the most advanced model, which features a phosphine-stabilized Fe-acyl thiolate carbonyl center. [44] Both the structural biology and literature precedents suggest that the pyridone group is mechanistically important (Scheme 1), but such modules have not yet been installed into catalytic systems.…”

Section: Artificial [Fe]-h2asesmentioning

confidence: 99%

Artificial hydrogenases

Barton

Olsen

Rauchfuss

2010

Current Opinion in Biotechnology

View full text Add to dashboard Cite

Decades of biophysical study on the hydrogenase (H 2 ase) enzymes have yielded sufficient information to guide the synthesis of analogues of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-, [NiFe]-, and [Fe]-H 2 ases, all of which feature iron centers bound to both CO and thiolate. Artificial H 2 ases effect the oxidation of H 2 of H 2 and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H 2 towards biomimetic H 2 ases.

show abstract

“…Interestingly, all diferreous complexes which have been characterized are stabilized by a bridging or semibridging carbonyl, a feature also observed in the enzyme active site [97]. the coordination chemistry of the pyridone cofactor has been explored using 6-(carboxymethyl)-4-methyl-2-hydroxypyridine as a surrogate [98]. Prior to the report of the crystal structure of the active site, Pickett and coworkers reported the iron complex 13, which exhibits infrared spectra similar to that of the enzyme active site [99].…”

mentioning

confidence: 99%