Date of Award
4-22-2008
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
First Advisor
Dr. Giovanni Gadda - Chair
Second Advisor
Dr. Jenny Yang
Third Advisor
Dr. Alfons Baumstark
Abstract
2-Nitropropane dioxygenase from Hansenula mrakii is a flavin-dependent enzyme that catalyzes the oxidation of anionic nitroalkanes into the corresponding carbonyl compounds and nitrite, with oxygen as the electron acceptor. Although nitroalkanes are anticipated to be toxic and carcinogenic, they are used widely in chemical industry for a quick and effective way of synthesizing common reagents. Consequently, the biochemical and biophysical analysis of 2-nitropropane dioxyganase has a potential for bioremediation purposes. In this study, recombinant enzyme is purified to high levels, allowing for detailed characterization. The biochemical analysis of 2-nitropropane dioxygenase presented in this study has established that enzyme utilizes alkyl nitronates as substrates by forming an anionic flavosemiquinone in catalysis. The enzyme is inhibited by halide ions, does not contain iron and has a positive charge located close to the N(1)-C(2)=O locus of the isoalloxazine moiety of the FMN cofactor.
DOI
https://doi.org/10.57709/1059229
Recommended Citation
Mijatovic, Slavica, "Biochemical Characterization of 2-Nitropropane Dioxygenase from Hansenula MRAKII." Thesis, Georgia State University, 2008.
doi: https://doi.org/10.57709/1059229