Metalloprotein Design

CcP has been used as a template for the purpose of producing a protein model of cytochrome P450 (cyt P450), and both CcP and swMb have been used as templates for engineering metal-binding sites characteristic of the active site in cytochrome c oxidase (CcO). Spectroscopic characterization of the mutants will be presented and will demonstrate that new metal centers, with spectral properties similar to the native enzymes, have been successfully engineered in the protein models. This study represents an advance in the field of protein redesign by using protein models with scaffolds bearing no sequence or structural homology to the modeled systems. Furthermore, this work demonstrates the usefulness of these models in understanding secondary coordination effects at the metal-binding sites within proteins and in introducing new activity into the redesigned protein.

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

• Sigman, Jeffrey Allen

Contributors dc:contributor

• Lu, Yi

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI9990139

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84499