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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Chloride Inhibition of Spinach Nitrate Reductase <xref ref-type="fn" rid="fn1"><sup>1</sup></xref></title><author><name sortKey="Barber, Michael J" sort="Barber, Michael J" uniqKey="Barber M" first="Michael J." last="Barber">Michael J. Barber</name></author><author><name sortKey="Notton, Brian A" sort="Notton, Brian A" uniqKey="Notton B" first="Brian A." last="Notton">Brian A. Notton</name></author><author><name sortKey="Kay, Christopher J" sort="Kay, Christopher J" uniqKey="Kay C" first="Christopher J." last="Kay">Christopher J. Kay</name></author><author><name sortKey="Solomonson, Larry P" sort="Solomonson, Larry P" uniqKey="Solomonson L" first="Larry P." last="Solomonson">Larry P. Solomonson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16666771</idno><idno type="pmc">1061679</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1061679</idno><idno type="RBID">PMC:1061679</idno><date when="1989">1989</date><idno type="wicri:Area/Pmc/Corpus">000088</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000088</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Chloride Inhibition of Spinach Nitrate Reductase <xref ref-type="fn" rid="fn1"><sup>1</sup></xref></title><author><name sortKey="Barber, Michael J" sort="Barber, Michael J" uniqKey="Barber M" first="Michael J." last="Barber">Michael J. Barber</name></author><author><name sortKey="Notton, Brian A" sort="Notton, Brian A" uniqKey="Notton B" first="Brian A." last="Notton">Brian A. Notton</name></author><author><name sortKey="Kay, Christopher J" sort="Kay, Christopher J" uniqKey="Kay C" first="Christopher J." last="Kay">Christopher J. Kay</name></author><author><name sortKey="Solomonson, Larry P" sort="Solomonson, Larry P" uniqKey="Solomonson L" first="Larry P." last="Solomonson">Larry P. Solomonson</name></author></analytic><series><title level="j">Plant Physiology</title><idno type="ISSN">0032-0889</idno><idno type="eISSN">1532-2548</idno><imprint><date when="1989">1989</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Initial rate studies of spinach (<italic>Spinacia oleracea</italic> L.) nitrate reductase showed that NADH:nitrate reductase activity was ionic strength dependent with elevated ionic concentration resulting in inhibition. In contrast, NADH:ferricyanide reductase was markedly less ionic strength dependent. At pH 7.0, NADH:nitrate reductase activity exhibited changes in the <italic>V</italic><sub>max</sub> and <italic>K</italic><sub>m</sub> for NO<sub>3</sub><sup>−</sup> yielding <italic>V</italic><sub>max</sub> values of 6.1 and 4.1 micromoles NADH per minute per nanomoles heme and <italic>K</italic><sub>m</sub> values of 13 and 18 micromolar at ionic strengths of 50 and 200 millimolar, respectively. Control experiments in phosphate buffer (5 millimolar) yielded a single <italic>K</italic><sub>m</sub> of 93 micromolar. Chloride ions decreased both NADH:nitrate reductase and reduced methyl viologen:nitrate reductase activities, suggesting involvement of the Mo center. Chloride was determined to act as a linear, mixed-type inhibitor with a <italic>K</italic><sub>i</sub> of 15 millimolar for binding to the native enzyme and 176 millimolar for binding to the enzyme-NO<sub>3</sub><sup>−</sup> complex. Binding of Cl<sup>−</sup> to the enzyme-NO<sub>3</sub><sup>−</sup> complex resulted in an inactive E-S-I complex. Electron paramagnetic resonance spectra showed that chloride altered the observed Mo(V) lineshape, confirming Mo as the site of interaction of chloride with nitrate reductase.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Physiol</journal-id><journal-title>Plant Physiology</journal-title><issn pub-type="ppub">0032-0889</issn><issn pub-type="epub">1532-2548</issn></journal-meta><article-meta><article-id pub-id-type="pmid">16666771</article-id><article-id pub-id-type="pmc">1061679</article-id><article-categories><subj-group subj-group-type="heading"><subject>Metabolism and Enzymology</subject></subj-group></article-categories><title-group><article-title>Chloride Inhibition of Spinach Nitrate Reductase <xref ref-type="fn" rid="fn1"><sup>1</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Barber</surname><given-names>Michael J.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Notton</surname><given-names>Brian A.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Kay</surname><given-names>Christopher J.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Solomonson</surname><given-names>Larry P.</given-names></name></contrib></contrib-group><aff id="af1">Department of Biochemistry and Molecular Biology, University of South Florida, College of Medicine, Tampa, Florida 33612</aff><aff id="af2">Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS18 9AF, United Kingdom</aff><aff id="af3">Institute of Arable Crops Research, Long Ashton Research Station, Long Ashton, Bristol BS18 9AF, United Kingdom</aff><author-notes><fn id="fn1"><label>1</label><p> This work was supported by Grants GM 32696 from the National Institutes of Health, 88-37120-3871 from the U.S. Department of Agriculture and NATO Collaborative Research Grant 04-0015-86. Long Ashton Research Station is funded through the Agricultural and Food Research Council, UK.</p></fn></author-notes><pub-date pub-type="ppub"><month>05</month><year>1989</year></pub-date><volume>90</volume><issue>1</issue><fpage>70</fpage><lpage>74</lpage><abstract><p>Initial rate studies of spinach (<italic>Spinacia oleracea</italic> L.) nitrate reductase showed that NADH:nitrate reductase activity was ionic strength dependent with elevated ionic concentration resulting in inhibition. In contrast, NADH:ferricyanide reductase was markedly less ionic strength dependent. At pH 7.0, NADH:nitrate reductase activity exhibited changes in the <italic>V</italic><sub>max</sub> and <italic>K</italic><sub>m</sub> for NO<sub>3</sub><sup>−</sup> yielding <italic>V</italic><sub>max</sub> values of 6.1 and 4.1 micromoles NADH per minute per nanomoles heme and <italic>K</italic><sub>m</sub> values of 13 and 18 micromolar at ionic strengths of 50 and 200 millimolar, respectively. Control experiments in phosphate buffer (5 millimolar) yielded a single <italic>K</italic><sub>m</sub> of 93 micromolar. Chloride ions decreased both NADH:nitrate reductase and reduced methyl viologen:nitrate reductase activities, suggesting involvement of the Mo center. Chloride was determined to act as a linear, mixed-type inhibitor with a <italic>K</italic><sub>i</sub> of 15 millimolar for binding to the native enzyme and 176 millimolar for binding to the enzyme-NO<sub>3</sub><sup>−</sup> complex. Binding of Cl<sup>−</sup> to the enzyme-NO<sub>3</sub><sup>−</sup> complex resulted in an inactive E-S-I complex. Electron paramagnetic resonance spectra showed that chloride altered the observed Mo(V) lineshape, confirming Mo as the site of interaction of chloride with nitrate reductase.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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