Computational Studies of Alkene Oxidation Reactions by Metal-oxo Compounds

ChemInform ◽  
2004 ◽  
Vol 35 (17) ◽  
Author(s):  
Thomas Strassner
Keyword(s):  
Computational Studies ◽  
Oxidation Reactions ◽  
Alkene Oxidation ◽  
Oxo Compounds

Solid-state 17O NMR and computational studies of terminal transition metal oxo compounds

2012 ◽  
Vol 3 (2) ◽  
pp. 391-397 ◽  
Author(s):  
Jianfeng Zhu ◽  
Takuya Kurahashi ◽  
Hiroshi Fujii ◽  
Gang Wu
Keyword(s):  
Solid State ◽  
Transition Metal ◽  
Computational Studies ◽  
17O Nmr ◽  
Oxo Compounds

The Wacker Reaction and Related Alkene Oxidation Reactions

ChemInform ◽  
2003 ◽  
Vol 34 (33) ◽  
Author(s):  
James M. Takacs ◽  
Xun-tian Jiang
Keyword(s):  
Oxidation Reactions ◽  
Alkene Oxidation

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.

Reaction Pathway Discrimination in Alkene Oxidation Reactions by Designed Ti‐Siloxy‐Polyoxometalates

ChemCatChem ◽  
2020 ◽  
Author(s):  
Teng Zhang ◽  
Albert Solé-Daura ◽  
Hugo Fouilloux ◽  
Josep M. Poblet ◽  
Anna Proust ◽  
...  
Keyword(s):  
Reaction Pathway ◽  
Oxidation Reactions ◽  
Alkene Oxidation

ChemInform Abstract: Mechanism of Dihydrogen Cleavage by High-Valent Metal Oxo Compounds: Experimental and Computational Studies.

ChemInform ◽  
2010 ◽  
Vol 33 (1) ◽  
pp. no-no
Author(s):  
James P. Collman ◽  
LeGrande M. Slaughter ◽  
Todd A. Eberspacher ◽  
Thomas Strassner ◽  
John I. Brauman
Keyword(s):  
Computational Studies ◽  
Oxo Compounds ◽  
High Valent

scholarly journals Exploring the Role of Phenylalanine Residues in Modulating the Flexibility and Topography of the Active Site in the Peroxygenase Variant PaDa-I

2020 ◽  
Vol 21 (16) ◽  
pp. 5734
Author(s):  
Joaquin Ramirez-Ramirez ◽  
Javier Martin-Diaz ◽  
Nina Pastor ◽  
Miguel Alcalde ◽  
Marcela Ayala
Keyword(s):  
Hydrogen Peroxide ◽  
Cytochrome P450 ◽  
Active Site ◽  
Bulk Solution ◽  
Computational Studies ◽  
Organic Substrates ◽  
Oxidation Reactions ◽  
Heme Group ◽  
Wide Range

Unspecific peroxygenases (UPOs) are fungal heme-thiolate enzymes able to catalyze a wide range of oxidation reactions, such as peroxidase-like, catalase-like, haloperoxidase-like, and, most interestingly, cytochrome P450-like. One of the most outstanding properties of these enzymes is the ability to catalyze the oxidation a wide range of organic substrates (both aromatic and aliphatic) through cytochrome P450-like reactions (the so-called peroxygenase activity), which involves the insertion of an oxygen atom from hydrogen peroxide. To catalyze this reaction, the substrate must access a channel connecting the bulk solution to the heme group. The composition, shape, and flexibility of this channel surely modulate the catalytic ability of the enzymes in this family. In order to gain an understanding of the role of the residues comprising the channel, mutants derived from PaDa-I, a laboratory-evolved UPO variant from Agrocybe aegerita, were obtained. The two phenylalanine residues at the surface of the channel, which regulate the traffic towards the heme active site, were mutated by less bulky residues (alanine and leucine). The mutants were experimentally characterized, and computational studies (i.e., molecular dynamics (MD)) were performed. The results suggest that these residues are necessary to reduce the flexibility of the region and maintain the topography of the channel.

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