scholarly journals Coordination and conformational isomers in mononuclear iron complexes with pertinence to the [FeFe] hydrogenase active site

2014 ◽  
Vol 43 (11) ◽  
pp. 4537-4549 ◽  
Author(s):  
Andreas Orthaber ◽  
Michael Karnahl ◽  
Stefanie Tschierlei ◽  
Daniel Streich ◽  
Matthias Stein ◽  
...  
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Iron Complexes ◽  
Computational Studies ◽  
Mononuclear Iron ◽  
Conformational Isomers ◽  
Ligand Modification ◽  
Fe Complexes ◽  
Ir Spectroscopic

6 Fe complexes of the type [Fe(X-bdt)(PR2NPh2)(CO)] were prepared and the possibility to tune their electronic properties by ligand modification was demonstrated. IR spectroscopic and computational studies suggest that the compounds exist as a mixture of isomers in solution.

A shared mechanistic pathway for pyridoxal phosphate–dependent arginine oxidases

2021 ◽  
Vol 118 (40) ◽  
pp. e2012591118
Author(s):  
Elesha R. Hoffarth ◽  
Kersti Caddell Haatveit ◽  
Eugene Kuatsjah ◽  
Gregory A. MacNeil ◽  
Simran Saroya ◽  
...  
Keyword(s):  
Active Site ◽  
Evolutionary History ◽  
Pyridoxal Phosphate ◽  
Computational Studies ◽  
Single Electron Transfer ◽  
Oxidation Reactions ◽  
Unified Framework ◽  
Precise Positioning ◽  
X Ray ◽  
Mechanistic Pathway

The mechanism by which molecular oxygen is activated by the organic cofactor pyridoxal phosphate (PLP) for oxidation reactions remains poorly understood. Recent work has identified arginine oxidases that catalyze desaturation or hydroxylation reactions. Here, we investigate a desaturase from the Pseudoalteromonas luteoviolacea indolmycin pathway. Our work, combining X-ray crystallographic, biochemical, spectroscopic, and computational studies, supports a shared mechanism with arginine hydroxylases, involving two rounds of single-electron transfer to oxygen and superoxide rebound at the 4′ carbon of the PLP cofactor. The precise positioning of a water molecule in the active site is proposed to control the final reaction outcome. This proposed mechanism provides a unified framework to understand how oxygen can be activated by PLP-dependent enzymes for oxidation of arginine and elucidates a shared mechanistic pathway and intertwined evolutionary history for arginine desaturases and hydroxylases.

Selective hydrosiloxane synthesis via dehydrogenative coupling of silanols with hydrosilanes catalysed by Fe complexes bearing a tetradentate PNNP ligand

2018 ◽  
Vol 47 (47) ◽  
pp. 17004-17010 ◽  
Author(s):  
Tomohiro Takeshita ◽  
Kazuhiko Sato ◽  
Yumiko Nakajima
Keyword(s):  
Iron Complexes ◽  
Dehydrogenative Coupling ◽  
Fe Complexes

Iron complexes bearing PNNP efficiently catalyse dehydrogenative coupling of silanols with silanes to selectively form various hydrosiloxanes.

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.

Insights from the computational studies on the oxidized as-isolated state of [NiFeSe] hydrogenase from D. vulgaris Hildenborough

2015 ◽  
Vol 17 (32) ◽  
pp. 20677-20686 ◽  
Author(s):  
Swaminathan Angeline Vedha ◽  
Gunasekaran Velmurugan ◽  
Rajangam Jagadeesan ◽  
Ponnambalam Venuvanalingam
Keyword(s):  
Density Functional Theory ◽  
Active Site ◽  
Density Functional ◽  
Computational Studies ◽  
Density Functional Theory Study ◽  
Functional Theory ◽  
Site Structure ◽  
Active Site Structure

A density functional theory study of the active site structure and features of the oxygen tolerant [NiFeSe] Hase in the oxidized as-isolated state of the enzyme D. vulgaris Hildenborough (DvH) is reported here.

The Electronic Properties of a Model Active Site for Blue Copper Proteins as Probed by Stark Spectroscopy

2002 ◽  
Vol 106 (11) ◽  
pp. 3007-3012 ◽  
Author(s):  
Arindam Chowdhury ◽  
Linda A. Peteanu ◽  
Patrick L. Holland ◽  
William B. Tolman
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Stark Spectroscopy ◽  
Blue Copper

Molecular and Electronic Structures of Mononuclear Iron Complexes Using Strongly Electron-Donating Ligands and their Oxidized Forms

2008 ◽  
Vol 47 (15) ◽  
pp. 6804-6824 ◽  
Author(s):  
Julia B. H. Strautmann ◽  
Serena DeBeer George ◽  
Eberhard Bothe ◽  
Eckhard Bill ◽  
Thomas Weyhermüller ◽  
...  
Keyword(s):  
Electronic Structures ◽  
Iron Complexes ◽  
Mononuclear Iron

Targeting metallo-carbapenemases via modulation of electronic properties of cephalosporins

2014 ◽  
Vol 464 (2) ◽  
pp. 271-279 ◽  
Author(s):  
Hao Yang ◽  
Heather Young ◽  
Sophia Yu ◽  
Larry Sutton ◽  
Michael W. Crowder
Keyword(s):  
Electronic Properties ◽  
Residence Time ◽  
Active Site

We demonstrate that the residence time of intermediates formed in the active site of NDM-1 can be tuned by substituents on cephalosporin scaffolds; compounds that reside for long times in the active site could be inhibitors of metallo-β-lactamases.

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