University of Illinois - Urbana-Champaign
Infrared spectroscopy of photodissociated carboxymyoglobin
Abstract
dc:descriptionInfrared spectra of carbon monoxide bound myoglobin reveal several lines due only to the carbon monoxide. Studies with isotopically enriched CO confirm the assignment of these lines. After photodissociation, the lines shift and change in extinction coefficient, giving an indication of the nature of the neighborhood of the photodissociated CO. At temperatures between 10K and lOOK three different CO environments are seen after photodissociation, with relative populations depending on temperature. Two forms are found to be weakly bound to the protein, but not at the iron center. The third form moves freely within a cavity formed by the protein structure. The binding entha1pies relative to the third form have been determined.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Physics
- Year dc:date
- 2011
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Good, David Eckert
- Contributors dc:contributor
-
- Frauenfelder, Hans
Subjects
dc:subject × 3Rights
dc:rights- Statement dc:rights
-
- 1981 David Eckert Good
- Language dc:language
- en
Identifiers
dc:identifier.*- Identifier
- 487673
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/25428