scholarly journals Heterodinuclear nickel(ii)–iron(ii) azadithiolates as structural and functional models for the active site of [NiFe]-hydrogenases

RSC Advances ◽  
2020 ◽  
Vol 10 (53) ◽  
pp. 32069-32077
Author(s):  
Li-Cheng Song ◽  
Bei-Bei Liu ◽  
Wen-Bo Liu ◽  
Zheng-Lei Tan
Keyword(s):  
General Formula ◽  
Active Site ◽  
Proton Reduction ◽  
Model Complexes ◽  
Functional Models

The first azadithiolato-bridged NiFe model complexes with a general formula [CpNi{(μ-SCH2)2NR}Fe(CO)(diphos)]BF4 have been synthesized, characterized, and for some of them found to be catalysts for proton reduction to H2 under CV conditions.

scholarly journals Site-selective Protonation of the One-electron Reduced Cofactor in [FeFe]-Hydrogenase

2020 ◽  
Author(s):  
Konstantin Laun ◽  
Iuliia Baranova ◽  
Jifu Duan ◽  
Leonie Kertess ◽  
Florian Wittkamp ◽  
...  
Keyword(s):  
Proton Transfer ◽  
Active Site ◽  
Catalytic Mechanism ◽  
Ph Dependence ◽  
H2 Evolution ◽  
Proton Reduction ◽  
Ph Values ◽  
Site Selective ◽  
H2 Oxidation ◽  
Diiron Site

Hydrogenases are microbial redox enzymes that catalyze H2 oxidation and proton reduction (H2 evolution). While all hydrogenases show high oxidation activities, the majority of [FeFe]-hydrogenases are excellent H2 evolution catalysts as well. Their active site cofactor comprises a [4Fe-4S] cluster covalently linked to a diiron site equipped with carbon monoxide and cyanide ligands that facilitate catalysis at low overpotential. Distinct proton transfer pathways connect the active site niche with the solvent, resulting in a non-trivial dependence of hydrogen turnover and bulk pH. To analyze the catalytic mechanism of [FeFe]-hydrogenase, we employ in situ infrared spectroscopy and infrared spectro-electrochemistry. Titrating the pH under H2 oxidation or H2 evolution conditions reveals the influence of site-selective protonation on the equilibrium of reduced cofactor states. Governed by pKa differences across the active site niche and proton transfer pathways, we find that individual electrons are stabilized either at the [4Fe-4S] cluster (alkaline pH values) or at the diiron site (acidic pH values). This observation is discussed in the context of the natural pH dependence of hydrogen turnover as catalyzed by [FeFe]-hydrogenase.<br>

Di-Iron Analogue of [FeFe]-Hydrogenase Active Site as a Molecular Electro-catalyst for Proton Reduction

2020 ◽  
Vol 150 (12) ◽  
pp. 3409-3414
Author(s):  
Xia Zhang ◽  
Lihong Liu ◽  
Weiming Cao ◽  
Dongjun Lv
Keyword(s):  
Active Site ◽  
Proton Reduction

Structural and functional models for the dinuclear copper active site in catechol oxidases

2003 ◽  
Vol 96 (4) ◽  
pp. 443-451 ◽  
Author(s):  
Marta González-Álvarez ◽  
Gloria Alzuet ◽  
Joaquı́n Borrás ◽  
Santiago Garcı́a-Granda ◽  
José Manuel Montejo-Bernardo
Keyword(s):  
Active Site ◽  
Dinuclear Copper ◽  
Functional Models

Binuclear Iron−Sulfur Complexes with Bidentate Phosphine Ligands as Active Site Models of Fe-Hydrogenase and Their Catalytic Proton Reduction

2007 ◽  
Vol 46 (6) ◽  
pp. 1981-1991 ◽  
Author(s):  
Weiming Gao ◽  
Jesper Ekström ◽  
Jianhui Liu ◽  
Changneng Chen ◽  
Lars Eriksson ◽  
...  
Keyword(s):  
Active Site ◽  
Phosphine Ligands ◽  
Proton Reduction ◽  
Iron Sulfur ◽  
Bidentate Phosphine ◽  
Binuclear Iron

Synthetic and Structural Studies of Butterfly Fe/S/P Cluster Complexes Related to the Active Site of [FeFe]-Hydrogenases. Proton Reduction to H2Catalyzed by (η1-Ph2PS-η1)2Fe2(CO)6

2008 ◽  
Vol 27 (15) ◽  
pp. 3714-3721 ◽  
Author(s):  
Li-Cheng Song ◽  
Guang-Huai Zeng ◽  
Shao-Xia Lou ◽  
Hui-Ning Zan ◽  
Jiang-Bo Ming ◽  
...  
Keyword(s):  
Active Site ◽  
Structural Studies ◽  
Proton Reduction ◽  
Cluster Complexes
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