The Third Hydrogenase: A Ferracyclic Carbamoyl with Close Structural Analogy to the Active Site of Hmd

Turrell, Peter J.; Wright, Joseph A.; Peck, Jamie N. T.; Oganesyan, Vasily S.; Pickett, Christopher J.

doi:10.1002/anie.201004189

Cited by 100 publications

(78 citation statements)

References 17 publications

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“…The oxidation state of the Fe center in Hmd has been of recurring interest, 40 but the issue should now be considered settled in light of this and related modeling work on acyl-containing models. 26,27 …”

Section: Discussionmentioning

confidence: 99%

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

et al. 2010

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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.

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Section: Discussionmentioning

confidence: 99%

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

et al. 2010

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“…Synthetic investigations into 2-pyridylcarbamoyl 405,406 and pyridylacyl complexes have afforded models closely resembling the CO-inhibited [Fe]-H 2 ase active site. Indeed, this motif has been incorporated into complexes of the form [Fe(CO) 2 (2-pyridinethiolate)(2-pyridylacetyl)] ([ 54 – 56 ], Figure 53), which feature donors resembling the native ligands, with an additional N-donor.…”

Section: [Fe]-h2asesmentioning

confidence: 99%

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

et al. 2016

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Hydrogenase enzymes efficiently process H2 and protons at organometallic FeFe, NiFe, or Fe active sites. Synthetic modeling of the many H2ase states has provided insight into H2ase structure and mechanism, as well as afforded catalysts for the H2 energy vector. Particularly important are hydride-bearing states, with synthetic hydride analogues now known for each hydrogenase class. These hydrides are typically prepared by protonation of low-valent cores. Examples of FeFe and NiFe hydrides derived from H2 have also been prepared. Such chemistry is more developed than mimicry of the redox-inactive monoFe enzyme, although functional models of the latter are now emerging. Advances in physical and theoretical characterization of H2ase enzymes and synthetic models have proven key to the study of hydrides in particular, and will guide modeling efforts toward more robust and active species optimized for practical applications.

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“…The iron carbonyl bromide starting salt [Fe(CO) 4 (Br) 2 ] was prepared by modification of a previously reported procedure. [9] The overall synthetic and reactivity scheme is summarized in Scheme 2. In the context of other synthetic approaches, Darensbourg and co-workers performed metalations of monodentate ligands (carbenes, py, PPh 3 ) and bidentate ligands (bpy, 2-pyridone) with [Fe(CO) 4 I 2 ] in hexane at room temperature; [23] no bisligated products were reported in these cases, except for PMe 3 , which afforded the complex [Fe(CO) 2 (PMe 3 ) 2 I 2 ] under certain conditions.…”

Section: Syntheses and Reactivitymentioning

confidence: 99%

Mononuclear Iron(II) Dicarbonyls Derived from NNS Ligands – Structural Models Related to a “Pre‐Acyl” Active Site of Mono‐Iron (Hmd) Hydrogenase

et al. 2015

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The Third Hydrogenase: A Ferracyclic Carbamoyl with Close Structural Analogy to the Active Site of Hmd

Cited by 100 publications

References 17 publications

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

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

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

Mononuclear Iron(II) Dicarbonyls Derived from NNS Ligands – Structural Models Related to a “Pre‐Acyl” Active Site of Mono‐Iron (Hmd) Hydrogenase

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