Structural and Dynamic Aspects of the Cytochrome P450(cam) Protein Conformation

The ferric spin equilibrium of cytochrome P-450$\sb{\rm cam}$ varys from a predominantly low-spin (S = 1/2) form to a predominantly high-spin (S = 5/2) form upon binding the natural substrate camphor. Cytochrome P-450$\sb{\rm cam}$ exhibits a distribution of spin states when various camphor analogs are bound to the cytochrome. These camphor analogs provide a means of independently varying the ferric spin equilibrium of the cytochrome in order to examine the relationship between this internal protein equilibrium and important functional aspects of the cytochrome.

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

2014

Author dc:creator

• Fisher, Mark Thomas

• Chemistry, Biochemistry

Identifier

(UMI)AAI8721634

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70567