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dc.creatorHeasley, Carl J
dc.date.accessioned2012-06-07T22:40:47Z
dc.date.available2012-06-07T22:40:47Z
dc.date.created1995
dc.date.issued1995
dc.identifier.urihttps://hdl.handle.net/1969.1/ETD-TAMU-1995-THESIS-H425
dc.descriptionDue to the character of the original source materials and the nature of batch digitization, quality control issues may be present in this document. Please report any quality issues you encounter to digital@library.tamu.edu, referencing the URI of the item.en
dc.descriptionIncludes bibliographical references.en
dc.descriptionIssued also on microfiche from Lange Micrographics.en
dc.description.abstractThis 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.en
dc.format.mediumelectronicen
dc.format.mimetypeapplication/pdf
dc.language.isoen_US
dc.publisherTexas A&M University
dc.rightsThis thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries in 2008. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use.en
dc.subjectbiochemistry.en
dc.subjectMajor biochemistry.en
dc.titleMechanistic and structural studies of nitroalkane oxidase from Fusarium oxysporumen
dc.typeThesisen
thesis.degree.disciplinebiochemistryen
thesis.degree.nameM.S.en
thesis.degree.levelMastersen
dc.type.genrethesisen
dc.type.materialtexten
dc.format.digitalOriginreformatted digitalen


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