Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin
15N NMR hyperfine-shift data were collected for wild-type and site-specific mutant (V44I, V44A, and V44G) Clostridium pasteurianum rubredoxins in the oxidized state. Whereas most of the (15)N NMR signals did not exhibit large systematic changes upon mutation of residue 44, the signal from the backbo...
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| Veröffentlicht in: | Journal of the American Chemical Society 2003-02, Vol.125 (6), p.1464-1465 |
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| container_title | Journal of the American Chemical Society |
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| creator | LIN, I-Jin GEBEL, Erika B. MACHONKIN, Timothy E. WESTLER, William M. MARKLEY, John L. |
| description | 15N NMR hyperfine-shift data were collected for wild-type and site-specific mutant (V44I, V44A, and V44G) Clostridium pasteurianum rubredoxins in the oxidized state. Whereas most of the (15)N NMR signals did not exhibit large systematic changes upon mutation of residue 44, the signal from the backbone nitrogen of residue 44 itself (arrows) shifted by approximately 400 ppm. These shifts were used to determine the lengths of the hydrogen bond between the backbone amide of residue 44 and the side-chain sulfur of cysteine-44, which is covalently ligated to the iron of the metal center. The results, which demonstrated that this hydrogen bond is shorter in mutants with higher reduction potential, point to the importance of hydrogen bonds in modulating the reduction potential of iron-sulfur proteins. |
| doi_str_mv | 10.1021/ja028710n |
| format | Article |
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Whereas most of the (15)N NMR signals did not exhibit large systematic changes upon mutation of residue 44, the signal from the backbone nitrogen of residue 44 itself (arrows) shifted by approximately 400 ppm. These shifts were used to determine the lengths of the hydrogen bond between the backbone amide of residue 44 and the side-chain sulfur of cysteine-44, which is covalently ligated to the iron of the metal center. The results, which demonstrated that this hydrogen bond is shorter in mutants with higher reduction potential, point to the importance of hydrogen bonds in modulating the reduction potential of iron-sulfur proteins.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja028710n</identifier><identifier>PMID: 12568591</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Clostridium - chemistry ; Clostridium - metabolism ; Electrochemistry ; Fundamental and applied biological sciences. Psychology ; Hydrogen Bonding ; Metalloproteins ; Nuclear Magnetic Resonance, Biomolecular ; Other metalloproteins ; Oxidation-Reduction ; Proteins ; Rubredoxins - chemistry ; Rubredoxins - metabolism ; Structure-Activity Relationship</subject><ispartof>Journal of the American Chemical Society, 2003-02, Vol.125 (6), p.1464-1465</ispartof><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14526583$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12568591$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LIN, I-Jin</creatorcontrib><creatorcontrib>GEBEL, Erika B.</creatorcontrib><creatorcontrib>MACHONKIN, Timothy E.</creatorcontrib><creatorcontrib>WESTLER, William M.</creatorcontrib><creatorcontrib>MARKLEY, John L.</creatorcontrib><title>Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>15N NMR hyperfine-shift data were collected for wild-type and site-specific mutant (V44I, V44A, and V44G) Clostridium pasteurianum rubredoxins in the oxidized state. Whereas most of the (15)N NMR signals did not exhibit large systematic changes upon mutation of residue 44, the signal from the backbone nitrogen of residue 44 itself (arrows) shifted by approximately 400 ppm. These shifts were used to determine the lengths of the hydrogen bond between the backbone amide of residue 44 and the side-chain sulfur of cysteine-44, which is covalently ligated to the iron of the metal center. The results, which demonstrated that this hydrogen bond is shorter in mutants with higher reduction potential, point to the importance of hydrogen bonds in modulating the reduction potential of iron-sulfur proteins.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Clostridium - chemistry</subject><subject>Clostridium - metabolism</subject><subject>Electrochemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen Bonding</subject><subject>Metalloproteins</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Other metalloproteins</subject><subject>Oxidation-Reduction</subject><subject>Proteins</subject><subject>Rubredoxins - chemistry</subject><subject>Rubredoxins - metabolism</subject><subject>Structure-Activity Relationship</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpF0E1PGzEQBmCrApUUeugfqPZCb1v8sV57jxABqRQJCPS8Gq8n1HRjB9urhn-PVUJ7mnk1j0aaIeQLo98Z5ezsCSjXilH_gcyY5LSWjLcHZEYp5bXSrTgin1J6KrHhmn0kR4zLVsuOzYibhxhxhOyCrwzmP4i-WrzYGB5LcxG8rZboH_OvVEHpV2in4a-9DRl9djCmyvlqPoaUo7Nu2lRbSBmn6MCXsJpMRBt2zp-Qw3XR-Hlfj8nPq8uH-aJe3lz_mJ8va8eVzHVjhBqUMlQz1UiQCNAa6KxFSrXg1nCFLTNGD0Z0FtiaKiGEbNSwZoZJFMfk29vebQzPE6bcb1wacBzBY5hSr3jXtUqpAr_u4WQ2aPttdBuIL_37cwo43QNIA4zrCH5w6b9rJG-lFsXVb86Vw3f_5hB_960SSvYPt_f9QrPF6uqO9kvxCl09g5k</recordid><startdate>20030212</startdate><enddate>20030212</enddate><creator>LIN, I-Jin</creator><creator>GEBEL, Erika B.</creator><creator>MACHONKIN, Timothy E.</creator><creator>WESTLER, William M.</creator><creator>MARKLEY, John L.</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20030212</creationdate><title>Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin</title><author>LIN, I-Jin ; GEBEL, Erika B. ; MACHONKIN, Timothy E. ; WESTLER, William M. ; MARKLEY, John L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i275t-4b37c77b081745a5eaa6ba9dde00832db27e61bb8cb39da1f07333547cf1b15e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Clostridium - chemistry</topic><topic>Clostridium - metabolism</topic><topic>Electrochemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen Bonding</topic><topic>Metalloproteins</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Other metalloproteins</topic><topic>Oxidation-Reduction</topic><topic>Proteins</topic><topic>Rubredoxins - chemistry</topic><topic>Rubredoxins - metabolism</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LIN, I-Jin</creatorcontrib><creatorcontrib>GEBEL, Erika B.</creatorcontrib><creatorcontrib>MACHONKIN, Timothy E.</creatorcontrib><creatorcontrib>WESTLER, William M.</creatorcontrib><creatorcontrib>MARKLEY, John L.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LIN, I-Jin</au><au>GEBEL, Erika B.</au><au>MACHONKIN, Timothy E.</au><au>WESTLER, William M.</au><au>MARKLEY, John L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2003-02-12</date><risdate>2003</risdate><volume>125</volume><issue>6</issue><spage>1464</spage><epage>1465</epage><pages>1464-1465</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>15N NMR hyperfine-shift data were collected for wild-type and site-specific mutant (V44I, V44A, and V44G) Clostridium pasteurianum rubredoxins in the oxidized state. Whereas most of the (15)N NMR signals did not exhibit large systematic changes upon mutation of residue 44, the signal from the backbone nitrogen of residue 44 itself (arrows) shifted by approximately 400 ppm. These shifts were used to determine the lengths of the hydrogen bond between the backbone amide of residue 44 and the side-chain sulfur of cysteine-44, which is covalently ligated to the iron of the metal center. The results, which demonstrated that this hydrogen bond is shorter in mutants with higher reduction potential, point to the importance of hydrogen bonds in modulating the reduction potential of iron-sulfur proteins.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12568591</pmid><doi>10.1021/ja028710n</doi><tpages>2</tpages></addata></record> |
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| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Clostridium - chemistry Clostridium - metabolism Electrochemistry Fundamental and applied biological sciences. Psychology Hydrogen Bonding Metalloproteins Nuclear Magnetic Resonance, Biomolecular Other metalloproteins Oxidation-Reduction Proteins Rubredoxins - chemistry Rubredoxins - metabolism Structure-Activity Relationship |
| title | Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin |
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