University of Illinois Urbana-Champaign

Mössbauer studies of putidaredoxin

Cooke, Arthur Roger

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Description

Title
Mössbauer studies of putidaredoxin
Author(s)
Cooke, Arthur Roger
Issue Date
1968
Doctoral Committee Chair(s)
Frauenfelder, Hans
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
  • Mossbauer
  • putidaredoxin
  • iron sulfide protein
Language
en
Abstract
Putidaredoxin is the iron sulfide protein component of an enzyme system which hydroxylates a methylene group with O2 to form a secondary alcohol. It contains, in a molecular weight of 12,000, two atoms each of iron and acid labile sulfur. We have used the Mossbauer effect to study the symmetry of the ligands and the electronic configuration of the iron. These studies were facilitated by the removal of the iron and subsequent replacement with iron-57. Our main conclusions are as follows. The sites of the two iron atoms are identical in the oxidized as well as in the reduced state. In the oxidized state, the spectrum consists of a pure quadrupole doublet, and the absence of magnetic interaction indicates that the electrons on the two iron atoms are coupled to a total spin of zero. The reduced state contains one additional electron which is shared between the two iron atoms and produces an internal field in excess of 200 KG at each iron nucleus. To share an electron, the two iron atoms must be close together. The spectrum of the reduced enzyme also provides evidence for a temperature-dependent relaxation mechanism.
Type of Resource
text
Permalink
http://hdl.handle.net/2142/25725
Copyright and License Information
1968 Arthur Roger Cooke

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