Preparation and Characterization of a Pentaammineruthenium(III) Derivative of Horse Heart Ferricytochrome c
A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium bindi...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1982-11, Vol.79 (22), p.7052-7055 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Yocom, Kathryn M. Shelton, Joan B. Shelton, J. Roger Schroeder, Walter A. Worosila, Greg Isied, Stephan S. Bordignon, Emilio Gray, Harry B. |
| description | A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)$^{3+/2+}$, 0.15 V (vs. normal hydrogen electrode). |
| doi_str_mv | 10.1073/pnas.79.22.7052 |
| format | Article |
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Roger ; Schroeder, Walter A. ; Worosila, Greg ; Isied, Stephan S. ; Bordignon, Emilio ; Gray, Harry B.</creator><creatorcontrib>Yocom, Kathryn M. ; Shelton, Joan B. ; Shelton, J. Roger ; Schroeder, Walter A. ; Worosila, Greg ; Isied, Stephan S. ; Bordignon, Emilio ; Gray, Harry B.</creatorcontrib><description>A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)$^{3+/2+}$, 0.15 V (vs. normal hydrogen electrode).</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.79.22.7052</identifier><identifier>PMID: 6294670</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Absorption spectra ; Amino Acid Sequence ; Amino acids ; Animals ; aquopentaammineruthenium (II) ; chemical modification ; Chromatography ; Chromatography, High Pressure Liquid ; Chromium ; cytochrome c ; Cytochrome c Group - metabolism ; Cytochromes ; Electrodes ; heart ; Histidine ; Horses ; Myocardium ; Organometallic Compounds ; Peptide Fragments - analysis ; Phosphates ; Protein Binding ; Ruthenium ; Sodium ; Spectrophotometry ; Trypsin</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1982-11, Vol.79 (22), p.7052-7055</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c558t-f80e92e071fa358180cdb8dbadcddede9dfb2bffbafa9b081d1ddfb13e34d7783</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/79/22.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/13150$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/13150$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,725,778,782,801,883,27907,27908,53774,53776,58000,58233</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6294670$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yocom, Kathryn M.</creatorcontrib><creatorcontrib>Shelton, Joan B.</creatorcontrib><creatorcontrib>Shelton, J. Roger</creatorcontrib><creatorcontrib>Schroeder, Walter A.</creatorcontrib><creatorcontrib>Worosila, Greg</creatorcontrib><creatorcontrib>Isied, Stephan S.</creatorcontrib><creatorcontrib>Bordignon, Emilio</creatorcontrib><creatorcontrib>Gray, Harry B.</creatorcontrib><title>Preparation and Characterization of a Pentaammineruthenium(III) Derivative of Horse Heart Ferricytochrome c</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)$^{3+/2+}$, 0.15 V (vs. normal hydrogen electrode).</description><subject>Absorption spectra</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>aquopentaammineruthenium (II)</subject><subject>chemical modification</subject><subject>Chromatography</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromium</subject><subject>cytochrome c</subject><subject>Cytochrome c Group - metabolism</subject><subject>Cytochromes</subject><subject>Electrodes</subject><subject>heart</subject><subject>Histidine</subject><subject>Horses</subject><subject>Myocardium</subject><subject>Organometallic Compounds</subject><subject>Peptide Fragments - analysis</subject><subject>Phosphates</subject><subject>Protein Binding</subject><subject>Ruthenium</subject><subject>Sodium</subject><subject>Spectrophotometry</subject><subject>Trypsin</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EKtvCGQkJlFMLh2z9kaztAwe0pexKlegBzpZjj9mUJF5sZ0X719fRLoVe4GR53u-N3ugh9IrgOcGcnW8HHedczimdc1zTJ2hGsCTlopL4KZphTHkpKlo9R8cx3mCMZS3wETpaUFktOJ6hH9cBtjro1Pqh0IMtlpv8MwlCe7cfelfo4hqGpHXftwOEMW1gaMf-3Xq9fl9cZHKXyR1M5MqHCMUKdEjFJYTQmtvkzSb4HgrzAj1zuovw8vCeoG-Xn74uV-XVl8_r5cer0tS1SKUTGCQFzInTrBZEYGMbYRttjbVgQVrX0Ma5RjstGyyIJTaPCANWWc4FO0Ef9nu3Y9ODNTl70J3ahrbX4VZ53arHytBu1He_U6zilLPsPz34g_85Qkyqb6OBrtMD-DEqgSlbcFH_FyR1TXN-mcHzPWiCjzGAewhDsJp6VFOPiktFqZp6zI43f9_wwB-Ky_rbgz4Zf6uPFpz9E1Bu7LoEv1ImX-_Jm5h8-JOMkRqzeyW9vuE</recordid><startdate>19821101</startdate><enddate>19821101</enddate><creator>Yocom, Kathryn M.</creator><creator>Shelton, Joan B.</creator><creator>Shelton, J. Roger</creator><creator>Schroeder, Walter A.</creator><creator>Worosila, Greg</creator><creator>Isied, Stephan S.</creator><creator>Bordignon, Emilio</creator><creator>Gray, Harry B.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19821101</creationdate><title>Preparation and Characterization of a Pentaammineruthenium(III) Derivative of Horse Heart Ferricytochrome c</title><author>Yocom, Kathryn M. ; Shelton, Joan B. ; Shelton, J. Roger ; Schroeder, Walter A. ; Worosila, Greg ; Isied, Stephan S. ; Bordignon, Emilio ; Gray, Harry B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c558t-f80e92e071fa358180cdb8dbadcddede9dfb2bffbafa9b081d1ddfb13e34d7783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Absorption spectra</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>aquopentaammineruthenium (II)</topic><topic>chemical modification</topic><topic>Chromatography</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromium</topic><topic>cytochrome c</topic><topic>Cytochrome c Group - metabolism</topic><topic>Cytochromes</topic><topic>Electrodes</topic><topic>heart</topic><topic>Histidine</topic><topic>Horses</topic><topic>Myocardium</topic><topic>Organometallic Compounds</topic><topic>Peptide Fragments - analysis</topic><topic>Phosphates</topic><topic>Protein Binding</topic><topic>Ruthenium</topic><topic>Sodium</topic><topic>Spectrophotometry</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yocom, Kathryn M.</creatorcontrib><creatorcontrib>Shelton, Joan B.</creatorcontrib><creatorcontrib>Shelton, J. Roger</creatorcontrib><creatorcontrib>Schroeder, Walter A.</creatorcontrib><creatorcontrib>Worosila, Greg</creatorcontrib><creatorcontrib>Isied, Stephan S.</creatorcontrib><creatorcontrib>Bordignon, Emilio</creatorcontrib><creatorcontrib>Gray, Harry B.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yocom, Kathryn M.</au><au>Shelton, Joan B.</au><au>Shelton, J. Roger</au><au>Schroeder, Walter A.</au><au>Worosila, Greg</au><au>Isied, Stephan S.</au><au>Bordignon, Emilio</au><au>Gray, Harry B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and Characterization of a Pentaammineruthenium(III) Derivative of Horse Heart Ferricytochrome c</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1982-11-01</date><risdate>1982</risdate><volume>79</volume><issue>22</issue><spage>7052</spage><epage>7055</epage><pages>7052-7055</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)$^{3+/2+}$, 0.15 V (vs. normal hydrogen electrode).</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6294670</pmid><doi>10.1073/pnas.79.22.7052</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1982-11, Vol.79 (22), p.7052-7055 |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Absorption spectra Amino Acid Sequence Amino acids Animals aquopentaammineruthenium (II) chemical modification Chromatography Chromatography, High Pressure Liquid Chromium cytochrome c Cytochrome c Group - metabolism Cytochromes Electrodes heart Histidine Horses Myocardium Organometallic Compounds Peptide Fragments - analysis Phosphates Protein Binding Ruthenium Sodium Spectrophotometry Trypsin |
| title | Preparation and Characterization of a Pentaammineruthenium(III) Derivative of Horse Heart Ferricytochrome c |
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