Presenter

Emma Altman

Abstract

PcpA is an enzyme involved in the degradation of the pollutant pentachlorophenol. It is a hydroquinone ring- cleaving dioxygenase (HQDO), and it oxidatively cleaves 2,6-dichlorohydroquinone. In order to better characterize and understand the specificity of PcpA, homologs of PcpA were studied. The homologs, selected based on sequence similarity, were procured and cloned into appropriate vectors, if necessary. Of the homologs grown and expressed, MnpC and MhqO currently have the most promise in demonstrating activity with hydroquinones. Recent experiments show 2-hydroxylhydroquinone as a possible substrate for MnpC, and 2-methylhydroquinone as a possible substrate for MhqO. Kinetic studies of these enzymes will help to elucidate more information about their binding affinities for their respective substrates. This information, coupled with ongoing and completed research, may help to further clarify the specificity of HQDOs; in the future, this information may be relevant to environmental remediation of chlorinated aromatic>hydrocarbons.

Faculty Sponsor

Tim Machonkin

Sponsor Department/Programs

Chemistry

Tracks

Poster Session

Terms of Use

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Location

Cordiner Hall

Presentation Type

Poster- restricted to Whitman students/faculty/staff

Research Funding Source or OCS Program

Funding proveded by Perry Summer Research Grant

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Apr 19th, 1:00 PM Apr 19th, 12:00 AM

Growth, Expression, and Characterization of Two Putative Hydroquinone Dioxygenases, MhqO and MnpC

Cordiner Hall

PcpA is an enzyme involved in the degradation of the pollutant pentachlorophenol. It is a hydroquinone ring- cleaving dioxygenase (HQDO), and it oxidatively cleaves 2,6-dichlorohydroquinone. In order to better characterize and understand the specificity of PcpA, homologs of PcpA were studied. The homologs, selected based on sequence similarity, were procured and cloned into appropriate vectors, if necessary. Of the homologs grown and expressed, MnpC and MhqO currently have the most promise in demonstrating activity with hydroquinones. Recent experiments show 2-hydroxylhydroquinone as a possible substrate for MnpC, and 2-methylhydroquinone as a possible substrate for MhqO. Kinetic studies of these enzymes will help to elucidate more information about their binding affinities for their respective substrates. This information, coupled with ongoing and completed research, may help to further clarify the specificity of HQDOs; in the future, this information may be relevant to environmental remediation of chlorinated aromatic>hydrocarbons.

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