Abstract
This thesis describes the purification and the initial mechanistic studies of nitroalkane oxidase from Fusarium oxysponim. Nitroalkane oxidase catalyzes the oxidative denitrification of a nitroalkane to the corresponding aidehyde or ketone. The enzyme was purified by using a three step purification scheme in large enough quantities to perform many analyses. The substrates used to date, nitroethane, 1-nitropropane, and 1-nitropentane, all fit to a ping pong mechanism. The pH dependence of the V/K data are consistent with the enzyme having an ionizable group which must be deprotonated for activity with a pKa of 6.8 and a requirement for the substrate to be protonated in the a carbon position. The enzyme activity is dependent on added oxidized flavin. In addition, the amino acid sequence of the N-terminus has been determined.
Heasley, Carl J (1995). Mechanistic and structural studies of nitroalkane oxidase from Fusarium oxysporum. Master's thesis, Texas A&M University. Available electronically from
https : / /hdl .handle .net /1969 .1 /ETD -TAMU -1995 -THESIS -H425.