Neutral versus Charged Species in Enzyme Catalysis. Classical and Free Energy Barriers for Oxygen Atom Transfer from C4a-Hydroperoxyflavin to Dimethyl Sulfide

2002 ◽  
Vol 67 (24) ◽  
pp. 8653-8661 ◽  
Author(s):  
Carlo Canepa ◽  
Robert D. Bach ◽  
Olga Dmitrenko
Keyword(s):  
Free Energy ◽  
Oxygen Atom ◽  
Enzyme Catalysis ◽  
Dimethyl Sulfide ◽  
Atom Transfer ◽  
Oxygen Atom Transfer ◽  
Energy Barriers ◽  
Charged Species

Oxygen atom transfer in the oxidations of dimethyl sulfide and dimethyl sulfoxide by bis(bipyridine)oxo(pyridine)ruthenium(2+)

1987 ◽  
Vol 26 (5) ◽  
pp. 779-781 ◽  
Author(s):  
Lee Roecker ◽  
John C. Dobson ◽  
William J. Vining ◽  
Thomas J. Meyer
Keyword(s):  
Oxygen Atom ◽  
Dimethyl Sulfoxide ◽  
Dimethyl Sulfide ◽  
Atom Transfer ◽  
Oxygen Atom Transfer

A kinetic study of dimethyl sulfoxide reductase based on density functional theory

2010 ◽  
Vol 88 (8) ◽  
pp. 683-693 ◽  
Author(s):  
Elizabeth Hernandez-Marin ◽  
Tom Ziegler
Keyword(s):  
Density Functional Theory ◽  
Free Energy ◽  
Oxygen Atom ◽  
Dimethyl Sulfoxide ◽  
Density Functional ◽  
Synthetic Analogue ◽  
Atom Transfer ◽  
Oxygen Atom Transfer ◽  
Functional Theory ◽  
Model Complexes

We present a density functional theory study on the oxygen atom transfer (OAT) reaction of dimethyl sulfoxide (DMSO) with model complexes resembling a functional synthetic analogue of the molybdoenzyme DMSO reductase. The good agreement between our calculated Gibbs free energy profile and data derived from experimental kinetic parameters supports the reaction mechanisms of the oxygen atom transfer proposed in this study. When the mechanism involves the formation of a DMSO-bound intermediate, the calculations on the free energy surface provide valuable information that explains the origin of the apparent contradiction between the experimental findings and previous theoretical calculations with respect to the rate-limiting step of the reaction mechanism. The enzymatic mechanism of the OAT reaction is more complex than the mechanism of any synthetic analogue, mainly due to the formation of an enzyme-substrate adduct prior to the appearance of the substrate-bound intermediate. This study also presents a possible mechanism for the formation of such an adduct and the subsequent oxygen atom transfer. The mechanism involves a proton transfer to and from the substrate.

scholarly journals Oxygen Atom Transfer Catalysis by Dioxidomolybdenum(VI) Complexes of Pyridyl Aminophenolate Ligands

Polyhedron ◽  
2021 ◽  
pp. 115234
Author(s):  
Md. Kamal Hossain ◽  
Jörg A. Schachner ◽  
Matti Haukka ◽  
Michael G. Richmond ◽  
Nadia C. Mösch-Zanetti ◽  
...  
Keyword(s):  
Oxygen Atom ◽  
Atom Transfer ◽  
Oxygen Atom Transfer

Nonclassical oxygen atom transfer reactions of an eight-coordinate dioxomolybdenum(vi) complex

2021 ◽  
Author(s):  
Leila G. Ranis ◽  
Jacqueline Gianino ◽  
Justin M. Hoffman ◽  
Seth N. Brown
Keyword(s):  
Oxygen Atom ◽  
Transfer Reaction ◽  
Transfer Reactions ◽  
Atom Transfer ◽  
Oxygen Atom Transfer ◽  
Oxygen Atom Transfer Reactions ◽  
Atom Transfer Reactions ◽  
Oxygen Atoms

Eight-coordinate MoO2(DOPOQ)2 can donate two oxygen atoms to substrates such as phosphines in a four-electron nonclassical oxygen atom transfer reaction.

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