Title

Characterization of MnpC: A Novel Hydroquinone Ring-Cleaving Dioxygenase

Abstract

PcpA, isolated from the pentachlorophenol metabolizing bacterium Sphingobium chlorophenolicum, is a member of the mononuclear non-heme Fe(II)-dependent hydroquinone ring-cleaving dioxygenases. It is structurally and mechanistically related to the much better characterized catechol extradiol dioxygenases. While there are hundreds of genes homologous to PcpA widely distributed among bacteria, virtually nothing is known about any of them. MnpC, isolated from Cupriavidus necator JMP134, is one such homolog of PcpA. It is believed that its native substrate is aminohydroquinone. After optimization of the expression and purification of this protein, MnpC has been found to show ring-cleaving activity with hydroquinone substrates. The further characterization of this novel hydroquinone ring-cleaving dioxygenase will further illuminate the substrate specificity of this little-studied class of enzymes.

Faculty Sponsor

Tim Machonkin

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poster

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Cordiner Hall

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Poster

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Characterization of MnpC: A Novel Hydroquinone Ring-Cleaving Dioxygenase

Cordiner Hall

PcpA, isolated from the pentachlorophenol metabolizing bacterium Sphingobium chlorophenolicum, is a member of the mononuclear non-heme Fe(II)-dependent hydroquinone ring-cleaving dioxygenases. It is structurally and mechanistically related to the much better characterized catechol extradiol dioxygenases. While there are hundreds of genes homologous to PcpA widely distributed among bacteria, virtually nothing is known about any of them. MnpC, isolated from Cupriavidus necator JMP134, is one such homolog of PcpA. It is believed that its native substrate is aminohydroquinone. After optimization of the expression and purification of this protein, MnpC has been found to show ring-cleaving activity with hydroquinone substrates. The further characterization of this novel hydroquinone ring-cleaving dioxygenase will further illuminate the substrate specificity of this little-studied class of enzymes.

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