pH effects and rebinding pathways in CO adducts of heme proteins

CO-adducts of heme proteins have IR absorption bands over the range 2200-1900 cm$\sp{-1}$. Flash photolysis can break the Fe-C bond, freeing the ligand. Below the glass-transition temperature of the protein-solvent system, $T\sb{g} \approx$ 185K, heme proteins are frozen into static conformations, and the photolyzed ligand, trapped within the protein, is restricted to the local environment of the binding site. The IR spectra of the bound and photolyzed ligands display several bands that are sensitive to changes in the local structure of the binding site and the pH of the solvent surrounding the protein. Each band represents a distinct conformation substate (CS) of the protein. The kinetics of the geminate rebinding of CO in heme proteins following flash photolysis, below $T\sb{g}$, is well described by a time- and temperature-independent distribution of enthalpic barriers, $g(H)$.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Physics

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Braunstein, David Phillip

Contributors dc:contributor

• Frauenfelder, Hans

• Chemistry, Biochemistry
• Physics, Molecular

Statement dc:rights

• Copyright 1991 Braunstein, David Phillip

Language dc:language

eng

Identifier

AAI9124386
(UMI)AAI9124386

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/22777