Dithiolato- and halogenido-bridged nickel–iron complexes related to the active site of [NiFe]-H2ases: preparation, structures, and electrocatalytic H2 production

2017 ◽  
Vol 46 (30) ◽  
pp. 10003-10013 ◽  
Author(s):  
Li-Cheng Song ◽  
Xiao-Feng Han ◽  
Wei Chen ◽  
Jia-Peng Li ◽  
Xu-Yong Wang

A new series of [NiFe]-H2ase mimics (5a,b–7a,b) has been prepared and structurally characterized; particularly, they have been found to be pre-catalysts for H2 production from Cl2CHCO2H under CV conditions.

2017 ◽  
Vol 53 (27) ◽  
pp. 3818-3821 ◽  
Author(s):  
Li-Cheng Song ◽  
Xi-Yue Yang ◽  
Meng Cao ◽  
Xiu-Yun Gao ◽  
Bei-Bei Liu ◽  
...  

While the first NiFe-based μ-hydroxo model [3]+ can be prepared by reaction of a dicarbonyl model [1]2+ with Me3NO·2H2O, the functional modeling of H2 activation catalyzed by the Ni-SIa state gives the t-hydride model [2]+ in high yield.


Author(s):  
Raheman Shakeelur ◽  
Rupali S. Mane ◽  
Higgins Wilson ◽  
Neetu Jha

In the world of photocatalytic hydrogen (H2) evolution two-dimensional (2D) nanomaterials have attracted widespread attention owing to their high surface area, abundant active site, and excellent photogenerated charge separation properties....


2019 ◽  
Author(s):  
Moritz Senger ◽  
Viktor Eichmann ◽  
Konstantin Laun ◽  
Jifu Duan ◽  
Florian Wittkamp ◽  
...  

Hydrogenases are metalloenzymes that catalyse the interconversion of protons and molecular hydrogen, H2. [FeFe]-hydrogenases show particularly high rates of hydrogen turnover and have inspired numerous compounds for biomimetic H2 production. Two decades of research on the active site cofactor of [FeFe]-hydrogenases have put forward multiple models of the catalytic proceedings. In comparison, understanding of the catalytic proton transfer is poor. We were able to identify the amino acid residues forming a proton transfer pathway between active site cofactor and bulk solvent; however, the exact mechanism of catalytic proton transfer remained inconclusive. Here, we employ in situ IR difference spectroscopy on the [FeFe]-hydrogenase from Chlamydomonas reinhardtii evaluating dynamic changes in the hydrogen-bonding network upon catalytic proton transfer. Our analysis allows for a direct, molecular unique assignment to individual amino acid residues. We found that transient protonation changes of arginine and glutamic acid residues facilitate bidirectional proton transfer in [FeFe]-hydrogenases.<br>


2018 ◽  
Vol 37 (6) ◽  
pp. 1050-1061 ◽  
Author(s):  
Li-Cheng Song ◽  
Xiu-Yun Gao ◽  
Wen-Bo Liu ◽  
Hong-Tao Zhang ◽  
Meng Cao
Keyword(s):  

Author(s):  
Shuzhong Zhan ◽  
Dong Guo ◽  
Chunwei Yuan ◽  
Ping Li
Keyword(s):  

2002 ◽  
Vol 41 (17) ◽  
pp. 4417-4423 ◽  
Author(s):  
Christian Stadler ◽  
Antonio L. de Lacey ◽  
Belén Hernández ◽  
Víctor M. Fernández ◽  
Jose C. Conesa

2007 ◽  
Vol 692 (19) ◽  
pp. 4177-4181 ◽  
Author(s):  
Vijendran Vijaikanth ◽  
Jean-François Capon ◽  
Frédéric Gloaguen ◽  
François Y. Pétillon ◽  
Philippe Schollhammer ◽  
...  
Keyword(s):  

2014 ◽  
Vol 43 (21) ◽  
pp. 8062-8071 ◽  
Author(s):  
Li-Cheng Song ◽  
Fu-Qiang Hu ◽  
Miao-Miao Wang ◽  
Zhao-Jun Xie ◽  
Kai-Kai Xu ◽  
...  

The first four acylmethyl/ester group-disubstituted pyridine-containing models for [Fe]-hydrogenase have been synthesized and crystallographically characterized.


2009 ◽  
Vol 131 (20) ◽  
pp. 6942-6943 ◽  
Author(s):  
Bryan E. Barton ◽  
C. Matthew Whaley ◽  
Thomas B. Rauchfuss ◽  
Danielle L. Gray
Keyword(s):  

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