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        <identifier>oai:www.ideals.illinois.edu:2142/85481</identifier>
        <datestamp>2023-07-11</datestamp>
        <setSpec>col_2142_5131</setSpec>
        <setSpec>col_2142_14828</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>Crofts, Antony R.</dc:contributor>
          <dc:creator>Kanazawa, Atsuko</dc:creator>
          <dc:date>2015-09-25T22:46:14Z</dc:date>
          <dc:date>2015-09-25T22:46:14Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1997</dc:date>
          <dc:date>1997</dc:date>
          <dc:description>H252Q and six donor-side mutants became the important tools to investigate a new model of neutral tyrosine radical, $\rm Y\sb{Z}\sp\cdot,$ introduced by Gilchrist et al. (1995) and Hoganson et al. (1995). In this new model, $\rm Y\sb{Z}$ is not simply a redox active residue in the electron transfer reactions, but is also directly involved in the water-oxidation. The models are critically-dependent on the presence of a neutral radical form of $\rm Y\sb{Z}\ (Y\sb{Z}\sp{\cdot}).$ The donor-side mutants, $\rm E189 &gt; L,Q,$ and $\rm N191 &gt; A,D,L,$ had only small effects on the pH-dependence of the rate of Q$\rm\sb{A}\sp-$ and oxidized $\rm Y\sb{Z}$ recombination. On the other hand, E189D mutant showed a pH-independent in rate of $\rm Q\sb{A}\sp-$ and oxidized $\rm Y\sb{Z}$ recombination. Based on these data, a simple thermodynamic model was introduced to explain the results and the model of $\rm Y\sb{Z}\sp{\cdot}$ as an oxidized form.</dc:description>
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  Previous issue date: 1997</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 86762
Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:description>174 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/85481</dc:identifier>
          <dc:identifier>(MiAaPQ)AAI9812648</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:subject>Biology, Plant Physiology</dc:subject>
          <dc:title>Electron Transfer on the Donor and Acceptor Sides of Photosystem II Explored by Site-Directed Mutagenesis and Kinetic Spectroscopy</dc:title>
          <dc:type>text</dc:type>
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            <department>Biophysics and Computational Biology</department>
            <discipline>Biophysics and Computational Biology</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
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