Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides dimethyl sulfoxide reductase

1995 ◽  
Vol 117 (2) ◽  
pp. 827-828 ◽  
Author(s):  
Brian E. Schultz ◽  
Russ Hille ◽  
R. H. Holm
Keyword(s):  
Oxygen Atom ◽  
Dimethyl Sulfoxide ◽  
Mechanism Of Action ◽  
Rhodobacter Sphaeroides ◽  
Atom Transfer ◽  
Oxygen Atom Transfer ◽  
Dimethyl Sulfoxide Reductase

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.

Oxygen Atom Transfer in the Oxidation of Dimethyl Sulfoxide by Oxoammonium Cations

2021 ◽  
Vol 86 (4) ◽  
pp. 3176-3185
Author(s):  
Vasily D. Sen’ ◽  
Valery A. Golubev ◽  
Gennadii V. Shilov ◽  
Alexander V. Chernyak ◽  
Vladimir A. Kurmaz ◽  
...  
Keyword(s):  
Oxygen Atom ◽  
Dimethyl Sulfoxide ◽  
Atom Transfer ◽  
Oxygen Atom Transfer

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
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