University of Illinois Urbana-Champaign

The Protein Redesign Approach to Modeling Manganese Peroxidase

Gengenbach, Alan James

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Description

Title
The Protein Redesign Approach to Modeling Manganese Peroxidase
Author(s)
Gengenbach, Alan James
Issue Date
2000
Doctoral Committee Chair(s)
Lu, Yi
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
The active site tryptophans were removed from MnCcP in order to investigate the roles of Trp51 and Trp191 in MnP activity. These residues are phenyalanines in MnP. In CcP mutants without the Mn(II)-binding site, Trp191 and Trp51 greatly influence the lifetime of the porphyrin pi-cation radical. The W51F, W191F, and W51F/W191F double mutations were incorporated along with the binding-site mutations (G41E,V45E,H181D) to create MnCcP(W51F), MnCcP(W191F) and MnCcP(W51F, W191F). The MnP activity observed varied between mutants and increased activity was observed for MnCcP(W51F,W191F) and MnCcP(W51F). The trend in activity reflects the extent of compound II stabilization present for the various mutants. MnC cP(W51F,W191F) is the most active protein model of MnP constructed to date.
Graduation Semester
2000
Type of Resource
text
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http://hdl.handle.net/2142/84482

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