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        <identifier>oai:www.ideals.illinois.edu:2142/23829</identifier>
        <datestamp>2023-07-10</datestamp>
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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>Gennis, Robert B.</dc:contributor>
          <dc:creator>Newton, Gail Ann</dc:creator>
          <dc:date>2011-05-07T14:28:40Z</dc:date>
          <dc:date>2011-05-07T14:28:40Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1990</dc:date>
          <dc:description>The cytochrome d terminal oxidase is one of two terminal oxidases in the aerobic respiratory chain of E. coli. The topology of the two subunits of the complex were examined by the use of alkaline phosphatase gene fusions, and models proposed. The expression and assembly of the subunits was also examined. It was found that subunit II of the complex can be expressed independently of subunit I and associates with the cytoplasmic membrane. It does not appear to have any of the cytochrome components associated with it under these conditions. The plasmid expressing subunit II complements another plasmid expressing subunit I, restoring oxidase activity. The incorporation of the $b\sb{595}$ and $d$ cytochrome components requires the association of the two subunits. It has also been confirmed that the expression of the cytochrome $d$ complex is not regulated by the presence or absence of heme. A model for the assembly of the complex has been proposed.</dc:description>
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  Previous issue date: 1990</dc:description>
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Item is restricted indefinitely.</dc:description>
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Original Data
Group with Access UIUC Users [automated]
Release Date: none
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          <dc:description>U of I Only</dc:description>
          <dc:identifier>AAI9026280</dc:identifier>
          <dc:identifier>(UMI)AAI9026280</dc:identifier>
          <dc:identifier>http://hdl.handle.net/2142/23829</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:rights>Copyright 1990 Newton, Gail Ann</dc:rights>
          <dc:subject>Chemistry, Biochemistry</dc:subject>
          <dc:title>Analysis of the topology of the cytochrome d terminal oxidase complex of Escherichia coli by genetic methods</dc:title>
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            <level>Dissertation</level>
            <name>Ph.D.</name>
            <department>Chemistry, Biochemistry</department>
            <discipline>Chemistry, Biochemistry</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
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