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        <identifier>oai:www.ideals.illinois.edu:2142/22961</identifier>
        <datestamp>2023-07-10</datestamp>
        <setSpec>col_2142_5131</setSpec>
        <setSpec>col_2142_16338</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>Wolfe, R.S.</dc:contributor>
          <dc:creator>Olson, Karl Daniel</dc:creator>
          <dc:date>2011-05-07T13:57:19Z</dc:date>
          <dc:date>2011-05-07T13:57:19Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1991</dc:date>
          <dc:description>The final step of methane formation in Methanobacterium thermoautotrophicum is a reductive demethylation of 2-(methylthio)ethanesulfonic acid (CH$\sb3$-S-CoM) with reducing equivalents from 7-(mercaptoheptanoyl)-L-threonine O$\sp3$-phosphate (HS-HTP). The enzyme that catalyzes this step is the CH$\sb3$-S-CoM reductase. Bound to the enzyme (non-covalently) is the prosthetic group, native coenzyme F430, a unique nickel-containing tetrapyrrole.</dc:description>
          <dc:description>Coenzyme F430 and a structural analogue were purified to homogeneity and studied by several types of two-dimensional (2D) nuclear magnetic resonance (NMR) techniques. Modelling studies using 2D nuclear Overhauser effect spectroscopy (NOESY) data, and distance geometry (DG) and back-calculations were used to determine 3-D structural aspects of these molecules.</dc:description>
          <dc:description>It was also found that inactive CH$\sb3$-S-CoM reductase can be partially activated in the presence of light. This is a major simplification of the terminal step. Interestingly, methanogens were found to be sensitive to visible light (in blue end of the spectrum).</dc:description>
          <dc:description>Experiments were completed to determine the experimental mid-point potentials electrochemically. These experiments are described.</dc:description>
          <dc:description>Made available in DSpace on 2011-05-07T13:57:19Z (GMT). No. of bitstreams: 2
license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5)
9210943.pdf: 5460559 bytes, checksum: c8413096c9e3ea34872ccc2c567078b4 (MD5)
  Previous issue date: 1991</dc:description>
          <dc:description>Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T15:01:13Z
Item is restricted indefinitely.</dc:description>
          <dc:description>Restriction data tranferred 2014-07-01T11:29:02-05:00
Original Data
Group with Access UIUC Users [automated]
Release Date: none
Reason: ETDs are only available to UIUC Users without author permission</dc:description>
          <dc:description>ETDs are only available to UIUC Users without author permission</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:identifier>AAI9210943</dc:identifier>
          <dc:identifier>(UMI)AAI9210943</dc:identifier>
          <dc:identifier>http://hdl.handle.net/2142/22961</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:rights>Copyright 1991 Olson, Karl Daniel</dc:rights>
          <dc:subject>Biology, Microbiology</dc:subject>
          <dc:subject>Chemistry, Biochemistry</dc:subject>
          <dc:title>Biochemical and chemical studies of the components involved in the final step of methane formation in Methanobacterium</dc:title>
          <dc:type>text</dc:type>
          <degree>
            <department>Microbiology</department>
            <discipline>Microbiology</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
          </degree>
        </thesis>
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