Infrared spectroscopy of photodissociated carboxymyoglobin
Good, David Eckert
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https://hdl.handle.net/2142/25428
Description
Title
Infrared spectroscopy of photodissociated carboxymyoglobin
Author(s)
Good, David Eckert
Issue Date
1981
Doctoral Committee Chair(s)
Frauenfelder, Hans
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
infrared spectroscopy
photodissociated carboxymyoglobin
myoglobin
Language
en
Abstract
Infrared 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.
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