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        <identifier>oai:www.ideals.illinois.edu:2142/25725</identifier>
        <datestamp>2023-07-10</datestamp>
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        <setSpec>col_2142_5131</setSpec>
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        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:contributor>Frauenfelder, Hans</dc:contributor>
          <dc:creator>Cooke, Arthur Roger</dc:creator>
          <dc:date>2011-07-08T17:27:42Z</dc:date>
          <dc:date>2011-07-08T17:27:42Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1968</dc:date>
          <dc:description>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.</dc:description>
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  Previous issue date: 1968</dc:description>
          <dc:description>Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-07-08T17:27:42Z
Item is restricted indefinitely.</dc:description>
          <dc:description>Restriction data tranferred 2014-07-01T11:32:51-05:00
Original Data
Group with Access UIUC Users [automated]
Release Date: none
Reason: Thesis</dc:description>
          <dc:description>Thesis</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:identifier>6081935</dc:identifier>
          <dc:identifier>http://hdl.handle.net/2142/25725</dc:identifier>
          <dc:language>en</dc:language>
          <dc:rights>1968 Arthur Roger Cooke</dc:rights>
          <dc:subject>Mossbauer</dc:subject>
          <dc:subject>putidaredoxin</dc:subject>
          <dc:subject>iron sulfide protein</dc:subject>
          <dc:title>Mössbauer studies of putidaredoxin</dc:title>
          <dc:type>Dissertation / Thesis</dc:type>
          <dc:type>text</dc:type>
          <degree>
            <department>Physics</department>
            <discipline>Physics</discipline>
            <disciplineCode>University of Illinois at Urbana-Champaign</disciplineCode>
            <level>Dissertation</level>
            <name>Ph.D.</name>
          </degree>
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