Nickel–thiolate and iron–thiolate cyanocarbonyl complexes: Modeling the nickel and iron sites of [NiFe] hydrogenase

Chiou, Tzung-Wen; Liaw, Wen‐Feng

doi:10.1016/j.crci.2008.04.003

Cited by 12 publications

(11 citation statements)

References 73 publications

(44 reference statements)

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“…These reports include the discrete Ni(II) homoleptic thiolate complexes, [Ni 2 (SR) 4 ] 2– ; , mononuclear mixed ligand Ni(II) complexes of the type [Ni(SR) 2 PMe 2 Ph) 2 ] (L = PMe 2 Ph), [Ni(SR) 2 (Ph 2 PCH 2 CH 2 PPh 2 )], , [Ni(SR)L 1 L 2 ] 1+ , [Ni(SR) 2 L] (L 1 = t BuNC, L 2 = 1,2-bis(diisopropylphosphino)ethane), [Ni(SR)L] (L is a bidentate β-diketiminate (“nacnac”) ligand), and [Ni(SR)L] 1+ (L = (Ph 2 PCH 2 CH 2 ) 2 PPh); , thiolate bridged dimeric Ni(II) complexes; ,, and various thiolate bridged multinuclear Ni(II) complexes such as the recently reported trinuclear T-shaped Ni 3 S 8 complex, [Ni 3 (SCH 2 CH 2 CH 2 S) 4 ] 2– , which promotes the electrocatalytic reduction of N 2 to hydrazine. Several mononuclear nickel–thiolate complexes have been explored for the intramolecular proton transfer between nickel and coordinated thiolate, ,, while some nickel–pyridine thiolate complexes have been studied for ligand noninnocence and photocatalytic production of hydrogen. , On the other hand, a majority of research involving heterometallic nickel thiolate/sulfide compounds has been directed toward the model chemistry of nickel containing enzymes, such as [NiFe]-hydrogenases − and [NiFe]-carbon monoxide dehydrogenases/acetyl coenzyme A synthase. ,,− The synthesis of mononuclear nickel complexes in different ligand systems − and interactions of some of these complexes with CO 2 and CO in relation with the active site of the aforementioned enzymes have also been studied for a long time.…”

Section: Introductionmentioning

confidence: 99%

Thiolate Coordination vs C–S Bond Cleavage of Thiolates in Dinickel(II) Complexes

2021

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A detailed study for the synthesis of dinickel(II)–thiolate and dinickel(II)–hydrosulfide complexes and the complete characterization of the relevant intermediates involved in the C–S bond cleavage of thiolates are presented. Hydrated Ni(II) salts mediate the hydrolytic C–S bond cleavage of thiolates (NaSR/RSH; R = Me, Et, n Bu, t Bu), albeit inefficiently, to yield a mixture of a dinickel(II)–hydrosulfide complex, [Ni2(BPMP)(μ-SH)(DMF)2]2+ (1), and the corresponding dinickel(II)–thiolate complexes, such as [Ni2(BPMP)(μ-SEt)(ClO4)]1+ (2) (HBPMP is 2,6-bis[[bis(2-pyridylmethyl)amino]methyl]-4-methylphenol). A systematic study for the reactivity of thiolates with Ni(II) was therefore pursued which finally yielded 1 as a pure product which has been characterized in comparison with the dinickel(II)–dichloride complex, [Ni2(BPMP)(Cl)2(MeOH)2]1+ (3). While the reaction of thiolates with anhydrous Ni(OTf)2 in dry conditions could only yield [Ni2(BPMP)(OTf)2]1+ (5) instead of the expected dinickel(II)–thiolate compound, the C–S bond cleavage could be suppressed by the use of a chelating thiol, such as PhCOSH, to yield [Ni2(BPMP)(SCOPh)2]1+ (6). Finally, with the suitable choice of a monodentate thiol, a dinickel(II)–monothiolate complex, [Ni2(BPMP)(SPh)(DMF)(MeOH)(H2O)]2+ (7), was isolated as a pure product within 1 h of reaction, which after a longer time of reaction yielded 1 and PhOH. Complex 7 may thus be regarded as the intermediate that precedes the C–S bond cleavage and is generated by the reaction of a thiolate with an initially formed dinickel(II)–solvento complex, [Ni2(BPMP)(MeOH)2(H2O)2]3+(4). Selected dinickel(II) complexes were explored further for the scope of substitution reactions, and the results include the isolation of a dinickel(II)–bis(thiolate) complex, [Ni2(BPMP)(μ-SPh)2]1+ (8).

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Section: Introductionmentioning

confidence: 99%

Thiolate Coordination vs C–S Bond Cleavage of Thiolates in Dinickel(II) Complexes

2021

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“…3,4,11 In contrast, models of the oxygentolerant [NiFe]-hydrogenases are less mature, and comparisons to the enzymatic system are sometimes less applicative. 3,4,12,13 …”

Section: Introductionmentioning

confidence: 99%

“…Hydrogenases are enzymes that catalyze the oxidation of hydrogen and reduction of protons at high rates and low overpotentials, reactions that are potentially useful for clean energy applications. − Hydrogenases are classified into three main families according to the metals in their active site: [Fe]-, [FeFe]-, and [NiFe]-hydrogenases. , These enzymes are oxygen-sensitive but the [NiFe]-hydrogenases can recover from oxygen poisoning. , Model compounds have been useful in elucidating catalytic mechanisms or atom identity, notably with [FeFe]-hydrogenases. , [FeFe]-hydrogenase models are fairly advanced and have strong resemblance and relevance to the enzymatic system. ,, In contrast, models of the oxygen-tolerant [NiFe]-hydrogenases are less mature, and comparisons to the enzymatic system are sometimes less applicative. ,,, …”

Section: Introductionmentioning

confidence: 99%

Models of the Ni-L and Ni-SI_a States of the [NiFe]-Hydrogenase Active Site

Chambers

Huynh

et al. 2015

Inorg. Chem.

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A new class of synthetic models for the active site of [NiFe]-hydrogenases are described. The NiI/II(SCys)2 and FeII(CN)2CO sites are represented with (RC5H4)NiI/II and FeII(diphos)(CO) modules, where diphos = 1,2-C2H4(PPh2)2(dppe) or cis-1,2-C2H2(PPh2)2(dppv). The two bridging thiolate ligands are represented by CH2(CH2S)22− (pdt2−), Me2C(CH2S)22− (Me2pdt2−), and (C6H5S)22−. The reaction of Fe(pdt)(CO)2(dppe) and [(C5H5)3Ni2]BF4 affords [(C5H5)Ni(pdt)Fe(dppe)-(CO)]BF4 ([1a]BF4). Monocarbonyl [1a]BF4 features an S = 0 NiIIFeII center with five-coordinated iron, as proposed for the Ni-SIa state of the enzyme. One-electron reduction of [1a]+ affords the S = 1/2 derivative [1a]0, which, according to density functional theory (DFT) calculations and electron paramagnetic resonance and Mössbauer spectroscopies, is best described as a NiIFeII compound. The NiIFeII assignment matches that for the Ni-L state in [NiFe]-hydrogenase, unlike recently reported NiIIFeI-based models. Compound [1a]0 reacts with strong acids to liberate 0.5 equiv of H2 and regenerate [1a]+, indicating that H2 evolution is catalyzed by [1a]0. DFT calculations were used to investigate the pathway for H2 evolution and revealed that the mechanism can proceed through two isomers of [1a]0 that differ in the stereochemistry of the Fe(dppe)CO center. Calculations suggest that protonation of [1a]0 (both isomers) affords NiIII–H–FeII intermediates, which represent mimics of the Ni-C state of the enzyme.

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“…The nickel atom functions in redox reactions while the iron atom is consistently in a Fe (II) coordination state. [22]. However, they were identified as two carbon monoxide (C≡O) molecules and one cyanide ( -C≡N) molecule.…”

Section: Structure Of [Nife] Hydrogenasesmentioning

confidence: 99%

“…(3)The CO-inhibitory state CO, is one of the inhibitory factor that bind directly to the Ni metal ion at the active site of the enzyme changing it configuration or conformation to form Ni-Sco, Because Ni-C is photo sensor when illuminated at 100k, forms the Ni-Co state in the presence of CO. [22]…”

Section: Mechanism Of the [Nife] Hydrogenasementioning

confidence: 99%

The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)

Saidu¹,

Tijani²,

Hindatu³

et al. 2014

BIO

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Sulfate-reducing bacteria are categories of bacteria and archaea that can obtain energy by oxidizing organic compounds or molecular hydrogen (H 2) while reducing sulfate (SO 4 2−) to hydrogen sulfide (H 2 S). By analysis, these organisms "respire" sulfate rather than oxygen, a form of anaerobic respiration, the oxidation of hydrogen by the primary genus of Sulfate Reducing Bacteria (Desulfovibrio, Desulfovibrio desulfuricans) is catalyzed by enzymes called Hydrogenases. Three basic types of hydrogenases have been widely isolated from the primary genus of sulfate-reducing bacteria Desulfobibrio which differ in their structural subunits, metal compositions, physico-chemical characteristics, amino acid sequences, immunological activities, structural gene configuration and their catalytic properties. Broadly, hydrogenases can be considered as 'iron containing hydrogenases and nickel-containing hydrogenases. The iron-sulfurcontaining hydrogenase enzyme contains two ferredoxin-type (4Fe-4S) clusters and typical iron-sulfur center believed to be involved in the activation of H 2 yet it is the most sensitive domain to CO and NO 2 − .eventhough it is not featured in all species of genus Desulfovibrio. The nickel-(iron-sulfur)-containing hydrogenases, [NiFe] hydrogenase posses two 4Fe-4S centers and one 3Fe-xS cluster in addition to nickel and have been found in all species of Desulfovibrio with strong resistance to CO and NO 2 so far investigated. The genes encoding the large and small subunits of a periplasmic and membrane-bound species of the [NiFe] hydrogenase have been cloned in Escherichia coli and sequenced, however the functional complexity of the hydrogenase system remained unexplored as a result of the metabolic diversity in Desulfovibrio spp. The [NiFe] hydrogenase plays an important role in the energy metabolism of Desulfovibrio spp. Thus, the expression of the encoded structural genes would be an excellent marker for the metabolic functionalities under specific inducible environment.

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Nickel–thiolate and iron–thiolate cyanocarbonyl complexes: Modeling the nickel and iron sites of [NiFe] hydrogenase

Cited by 12 publications

References 73 publications

Thiolate Coordination vs C–S Bond Cleavage of Thiolates in Dinickel(II) Complexes

Thiolate Coordination vs C–S Bond Cleavage of Thiolates in Dinickel(II) Complexes

Models of the Ni-L and Ni-SI_a States of the [NiFe]-Hydrogenase Active Site

The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)

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Nickel–thiolate and iron–thiolate cyanocarbonyl complexes: Modeling the nickel and iron sites of [NiFe] hydrogenase

Cited by 12 publications

References 73 publications

Thiolate Coordination vs C–S Bond Cleavage of Thiolates in Dinickel(II) Complexes

Thiolate Coordination vs C–S Bond Cleavage of Thiolates in Dinickel(II) Complexes

Models of the Ni-L and Ni-SIa States of the [NiFe]-Hydrogenase Active Site

The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)

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Models of the Ni-L and Ni-SI_a States of the [NiFe]-Hydrogenase Active Site