University of Illinois Urbana-Champaign

Long lived states induced by extended illumination of carbonmonoxy-myoglobin

Sauke, Todd Bennet

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https://hdl.handle.net/2142/23939

Description

Title
Long lived states induced by extended illumination of carbonmonoxy-myoglobin
Author(s)
Sauke, Todd Bennet
Issue Date
1989
Doctoral Committee Chair(s)
Frauenfelder, Hans
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
  • carbonmonoxymyoglobin
  • myoglobin
  • protein kinetics
  • ligand binding kinetics
  • recombination kinetics
  • illumination
Language
en
Abstract
"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."
Type of Resource
text
Permalink
http://hdl.handle.net/2142/23939
Copyright and License Information
1989 Todd Bennet Sauke

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