Dithiolato-bridged nickel–iron complexes as models for the active site of [NiFe]-hydrogenases

2017 ◽  
Vol 53 (27) ◽  
pp. 3818-3821 ◽  
Author(s):  
Li-Cheng Song ◽  
Xi-Yue Yang ◽  
Meng Cao ◽  
Xiu-Yun Gao ◽  
Bei-Bei Liu ◽  
...  
Keyword(s):  
Active Site ◽  
Iron Complexes ◽  
High Yield ◽  
Functional Modeling ◽  
Nickel Iron

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.

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
Keyword(s):  
Active Site ◽  
Iron Complexes ◽  
H2 Production ◽  
Nickel Iron

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.

Synthesis, Characterization, and Reactions of Functionalized Nickel–Iron Dithiolates Related to the Active Site of [NiFe]-Hydrogenases

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):  
Active Site ◽  
Nickel Iron

Functional modeling of the MnCAT active site with a dimanganese(III) complex of an unsymmetrical polydentate N 3 O 3 ligand

2018 ◽  
Vol 186 ◽  
pp. 10-16 ◽  
Author(s):  
Gabriela N. Ledesma ◽  
Elodie Anxolabéhère-Mallart ◽  
Laurent Sabater ◽  
Christelle Hureau ◽  
Sandra R. Signorella
Keyword(s):  
Active Site ◽  
Functional Modeling

SYNTHESIS AND PROPERTIES OF BINUCLEAR CYANIDE-BRIDGED NICKEL–IRON COMPLEXES

2001 ◽  
Vol 31 (1) ◽  
pp. 57-64 ◽  
Author(s):  
Shuzhong Zhan ◽  
Dong Guo ◽  
Chunwei Yuan ◽  
Ping Li
Keyword(s):  
Iron Complexes ◽  
Nickel Iron

Density Functional Calculations for Modeling the Oxidized States of the Active Site of Nickel−Iron Hydrogenases. 1. Verification of the Method with Paramagnetic Ni and Co Complexes

2002 ◽  
Vol 41 (17) ◽  
pp. 4417-4423 ◽  
Author(s):  
Christian Stadler ◽  
Antonio L. de Lacey ◽  
Belén Hernández ◽  
Víctor M. Fernández ◽  
Jose C. Conesa
Keyword(s):  
Active Site ◽  
Density Functional Calculations ◽  
Density Functional ◽  
Nickel Iron

Carboxy-functionalized dithiolate di-iron complexes related to the active site of Fe-only hydrogenase

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

Synthesis, structural characterization, and some properties of 2-acylmethyl-6-ester group-difunctionalized pyridine-containing iron complexes related to the active site of [Fe]-hydrogenase

2014 ◽  
Vol 43 (21) ◽  
pp. 8062-8071 ◽  
Author(s):  
Li-Cheng Song ◽  
Fu-Qiang Hu ◽  
Miao-Miao Wang ◽  
Zhao-Jun Xie ◽  
Kai-Kai Xu ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Active Site ◽  
Iron Complexes ◽  
Ester Group

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

scholarly journals Synthesis of Human Milk Oligosaccharides: Protein Engineering Strategies for Improved Enzymatic Transglycosylation

Molecules ◽  
2019 ◽  
Vol 24 (11) ◽  
pp. 2033 ◽  
Author(s):  
Birgitte Zeuner ◽  
David Teze ◽  
Jan Muschiol ◽  
Anne S. Meyer
Keyword(s):  
Protein Engineering ◽  
Human Milk ◽  
Active Site ◽  
Enzymatic Synthesis ◽  
Spatial Arrangement ◽  
Glycoside Hydrolases ◽  
High Yield ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides ◽  
Enzyme Active Site

Human milk oligosaccharides (HMOs) signify a unique group of oligosaccharides in breast milk, which is of major importance for infant health and development. The functional benefits of HMOs create an enormous impetus for biosynthetic production of HMOs for use as additives in infant formula and other products. HMO molecules can be synthesized chemically, via fermentation, and by enzymatic synthesis. This treatise discusses these different techniques, with particular focus on harnessing enzymes for controlled enzymatic synthesis of HMO molecules. In order to foster precise and high-yield enzymatic synthesis, several novel protein engineering approaches have been reported, mainly concerning changing glycoside hydrolases to catalyze relevant transglycosylations. The protein engineering strategies for these enzymes range from rationally modifying specific catalytic residues, over targeted subsite −1 mutations, to unique and novel transplantations of designed peptide sequences near the active site, so-called loop engineering. These strategies have proven useful to foster enhanced transglycosylation to promote different types of HMO synthesis reactions. The rationale of subsite −1 modification, acceptor binding site matching, and loop engineering, including changes that may alter the spatial arrangement of water in the enzyme active site region, may prove useful for novel enzyme-catalyzed carbohydrate design in general.

scholarly journals Nickel−Iron Dithiolato Hydrides Relevant to the [NiFe]-Hydrogenase Active Site

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