Peroxidase-promoted aerobic oxidation of 2-nitropropane: mechanism of excited state formation. Biochim Biophys Acta 1987 Mar 19;923(3):347-54
Date
03/19/1987Pubmed ID
3828378DOI
10.1016/0304-4165(87)90042-0Scopus ID
2-s2.0-0023118106 (requires institutional sign-in at Scopus site) 7 CitationsAbstract
Using sensitized emission, the horseradish peroxidase-catalyzed aerobic oxidation of the toxic pollutant 2-nitropropane to nitrite and acetone is shown to produce the latter in the electronically excited triplet state. In turn, this chemiexcitation implies a hydroperoxide precursor. Taking into account the stoichiometry of the reaction and available isotopic data it is inferred that the hydroperoxide reacts with a second molecule of the substrate (aci form). While triplet acetone formed from isobutanal (enol form) is generated within the enzyme, in the present case triplet acetone is formed in the bulk solution.
Author List
Indig GL, Cilento GAuthor
Guilherme L. Indig BS,PhD Associate Professor in the Chemistry and Biochemistry department at University of Wisconsin - MilwaukeeMESH terms used to index this publication - Major topics in bold
AcetoneAerobiosis
Alkanes
Animals
Biomechanical Phenomena
Cattle
Chlorophyll
Electrochemistry
Energy Metabolism
Horseradish Peroxidase
Hydrogen Peroxide
Hydrogen-Ion Concentration
Kinetics
Nitrites
Nitroparaffins
Osmolar Concentration
Oxidation-Reduction
Peroxidases
Propane
Superoxide Dismutase
Tryptophan
