Long-lived states induced by extended illumination of carbonmonoxy-myoglobin

Myoglobin is a heme-protein that binds small ligands, such as O$\sb2$ 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 carbonmonoxy-myoglobin 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.

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

• Sauke, Todd Bennet

Contributors dc:contributor

• Frauenfelder, Hans

• Physics, Molecular

Statement dc:rights

• Copyright 1989 Sauke, Todd Bennet

Language dc:language

eng

Identifier

AAI8924937
(UMI)AAI8924937

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/23055