Enzymatic activation of cytochrome P-450(cam)

Cytochrome P-450$\sb{\rm cam}$, a camphor monoxygenase from Pseudomonas putida, has served as a model system for the entire family of the P-450s in exploring structure-function relationships, molecular recognition, substrate specificity, and oxygen activation. There are several universal features of the P-450s that have been addressed in this thesis work. The active site is centered around the heme prosthetic group, which is primarily responsible for the redox activity of the enzyme. Iron chlorin groups, which are partially saturated analogues of protoporphyrin IX, were substituted for the native heme in cytochrome P-450$\sb{\rm cam}$ and also rat liver cytochrome $b\sb5$, which served as a useful model for the more difficult reconstitution and subsequent characterization of the P-450 enzyme. Optical and electron paramagnetic resonance spectroscopies were used to study the physical properties of the reconstituted proteins. In addition reduction potentials were measured and the ability of the chlorin-substituted proteins to carry out native and redox activity was investigated.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Martinis, Susan Anne

Contributors dc:contributor

• Sligar, Stephen G.

• Chemistry, Biochemistry
• Chemistry, Pharmaceutical
• Biophysics, General

Statement dc:rights

• Copyright 1990 Martinis, Susan Anne

Language dc:language

eng

Identifier

AAI9114336
(UMI)AAI9114336

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/23130