The Protein Redesign Approach to Modeling Manganese Peroxidase

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Gengenbach, Alan James

Contributors dc:contributor

• Lu, Yi

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI9990003

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84482