Long lived states induced by extended illumination of carbonmonoxy-myoglobin

"Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures (> 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be measured by monitoring the time dependence of the absorption spectrum of the sample after photodissociation. After a period of intense illumination with light, the recombination kinetics slow down. The proteins are ""pumped"" to longer lived states. After waiting, the system resets, such that a photodissociation initiates regular, non-pumped, kinetics. I have measured the kinetics of the ""pumped"" states and the time course of the resetting, at various temperatures. Physical models, including connections to glass theories, are considered, and thermodynamic parameters for the various processes involved havebeen determined."

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Physics

Year dc:date

2011

Author dc:creator

• Sauke, Todd Bennet

Contributors dc:contributor

• Frauenfelder, Hans

• carbonmonoxymyoglobin
• myoglobin
• protein kinetics
• ligand binding kinetics
• recombination kinetics
• illumination

Statement dc:rights

• 1989 Todd Bennet Sauke

Language dc:language

en

Identifier

3478197

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/23939