Characterization of an Alkaline Transition Intermediate Stabilized in the Phe82Trp Variant of Yeast iso-1-Cytochrome c
In general, mutation of the phylogenetically conserved residue Phe82 in yeast iso-1-cytochrome c destabilizes the native conformation of the protein by facilitating the ligand exchange reactions that are associated with the alkaline conformational transitions of the ferricytochrome. Of the Phe82 var...
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| Veröffentlicht in: | Biochemistry (Easton) 2000-08, Vol.39 (30), p.9047-9054 |
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| creator | Rosell, Federico I Harris, Thomas R Hildebrand, Dean P Döpner, Susanne Hildebrandt, Peter Mauk, A. Grant |
| description | In general, mutation of the phylogenetically conserved residue Phe82 in yeast iso-1-cytochrome c destabilizes the native conformation of the protein by facilitating the ligand exchange reactions that are associated with the alkaline conformational transitions of the ferricytochrome. Of the Phe82 variants surveyed thus far, Phe82Trp is unique in that it adopts a thermodynamically stable, high-spin conformation at mildly alkaline pH. This species exhibits spectroscopic features that can only be detected transiently in other ferricytochromes c within the first 100 ms immediately after a pH-jump from neutrality to pH >10. Spectroscopic characterization of this high-spin reaction intermediate suggests that in addition to an obligatory pentacoordinate heme iron, a group within the heme pocket coordinates the heme iron but is then replaced either by Met80, to revert to the native conformation, or by Lys73 or Lys79, to yield one of the conventional alkaline conformers. Evidence is presented to suggest that this group is either a hydroxide ion or Tyr67 rather than a loosely bound Met80. |
| doi_str_mv | 10.1021/bi001095k |
| format | Article |
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Grant</creator><creatorcontrib>Rosell, Federico I ; Harris, Thomas R ; Hildebrand, Dean P ; Döpner, Susanne ; Hildebrandt, Peter ; Mauk, A. Grant</creatorcontrib><description>In general, mutation of the phylogenetically conserved residue Phe82 in yeast iso-1-cytochrome c destabilizes the native conformation of the protein by facilitating the ligand exchange reactions that are associated with the alkaline conformational transitions of the ferricytochrome. Of the Phe82 variants surveyed thus far, Phe82Trp is unique in that it adopts a thermodynamically stable, high-spin conformation at mildly alkaline pH. This species exhibits spectroscopic features that can only be detected transiently in other ferricytochromes c within the first 100 ms immediately after a pH-jump from neutrality to pH >10. Spectroscopic characterization of this high-spin reaction intermediate suggests that in addition to an obligatory pentacoordinate heme iron, a group within the heme pocket coordinates the heme iron but is then replaced either by Met80, to revert to the native conformation, or by Lys73 or Lys79, to yield one of the conventional alkaline conformers. Evidence is presented to suggest that this group is either a hydroxide ion or Tyr67 rather than a loosely bound Met80.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi001095k</identifier><identifier>PMID: 10913318</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Substitution ; Cytochrome c Group - chemistry ; Cytochrome c Group - genetics ; Cytochrome c Group - metabolism ; Cytochromes c ; Electrochemistry ; Electron Spin Resonance Spectroscopy ; Enzyme Stability ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Heme - chemistry ; Heme - metabolism ; Hydrogen-Ion Concentration ; Iron - chemistry ; Iron - metabolism ; Kinetics ; Nuclear Magnetic Resonance, Biomolecular ; Oxidation-Reduction ; Phenylalanine - chemistry ; Phenylalanine - genetics ; Phenylalanine - metabolism ; Protein Conformation ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins ; Spectrum Analysis, Raman ; Structure-Activity Relationship ; Tryptophan - chemistry ; Tryptophan - genetics ; Tryptophan - metabolism</subject><ispartof>Biochemistry (Easton), 2000-08, Vol.39 (30), p.9047-9054</ispartof><rights>Copyright © 2000 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a349t-83704eea044605c390439d252d1e0a499e29957c83f6872a8f2efb0937ba72af3</citedby><cites>FETCH-LOGICAL-a349t-83704eea044605c390439d252d1e0a499e29957c83f6872a8f2efb0937ba72af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi001095k$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi001095k$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2751,27055,27903,27904,56716,56766</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10913318$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rosell, Federico I</creatorcontrib><creatorcontrib>Harris, Thomas R</creatorcontrib><creatorcontrib>Hildebrand, Dean P</creatorcontrib><creatorcontrib>Döpner, Susanne</creatorcontrib><creatorcontrib>Hildebrandt, Peter</creatorcontrib><creatorcontrib>Mauk, A. Grant</creatorcontrib><title>Characterization of an Alkaline Transition Intermediate Stabilized in the Phe82Trp Variant of Yeast iso-1-Cytochrome c</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>In general, mutation of the phylogenetically conserved residue Phe82 in yeast iso-1-cytochrome c destabilizes the native conformation of the protein by facilitating the ligand exchange reactions that are associated with the alkaline conformational transitions of the ferricytochrome. Of the Phe82 variants surveyed thus far, Phe82Trp is unique in that it adopts a thermodynamically stable, high-spin conformation at mildly alkaline pH. This species exhibits spectroscopic features that can only be detected transiently in other ferricytochromes c within the first 100 ms immediately after a pH-jump from neutrality to pH >10. Spectroscopic characterization of this high-spin reaction intermediate suggests that in addition to an obligatory pentacoordinate heme iron, a group within the heme pocket coordinates the heme iron but is then replaced either by Met80, to revert to the native conformation, or by Lys73 or Lys79, to yield one of the conventional alkaline conformers. Evidence is presented to suggest that this group is either a hydroxide ion or Tyr67 rather than a loosely bound Met80.</description><subject>Amino Acid Substitution</subject><subject>Cytochrome c Group - chemistry</subject><subject>Cytochrome c Group - genetics</subject><subject>Cytochrome c Group - metabolism</subject><subject>Cytochromes c</subject><subject>Electrochemistry</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Enzyme Stability</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Heme - chemistry</subject><subject>Heme - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Iron - chemistry</subject><subject>Iron - metabolism</subject><subject>Kinetics</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Oxidation-Reduction</subject><subject>Phenylalanine - chemistry</subject><subject>Phenylalanine - genetics</subject><subject>Phenylalanine - metabolism</subject><subject>Protein Conformation</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Spectrum Analysis, Raman</subject><subject>Structure-Activity Relationship</subject><subject>Tryptophan - chemistry</subject><subject>Tryptophan - genetics</subject><subject>Tryptophan - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkMFu1DAQhi0EokvhwAsgX6jEIXRsJ3FyrBboFlXqSl2QOFmT7ETrbtZebG9F-_S4TVVx4DT6NZ_-0XyMvRfwWYAUp50FENBW2xdsJioJRdm21Us2A4C6kG0NR-xNjDc5lqDL1-wow0Ip0czY7XyDAftEwd5jst5xP3B0_Gzc4mgd8VVAF-3j5sJlbEdri4n4dcLOjvae1tw6njbElxtq5Crs-U8MFl16aPpFGBO30ReimN8l32-C3xHv37JXA46R3j3NY_bj29fVfFFcXp1fzM8uC1Rlm4pGaSiJEMqyhqpXLZSqXctKrgUB5i9J5k9136ihbrTEZpA0dNAq3WGOgzpmJ1PvPvjfB4rJ7GzsaRzRkT9Eo4XUMpvI4KcJ7IOPMdBg9sHuMNwZAeZBsnmWnNkPT6WHLuv4h5ysZqCYABsT_XneY9iaWitdmdXy2tSL74svy3Zh6sx_nHjso7nxh-Cyk_8c_gsObpG_</recordid><startdate>20000801</startdate><enddate>20000801</enddate><creator>Rosell, Federico I</creator><creator>Harris, Thomas R</creator><creator>Hildebrand, Dean P</creator><creator>Döpner, Susanne</creator><creator>Hildebrandt, Peter</creator><creator>Mauk, A. Grant</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7X8</scope></search><sort><creationdate>20000801</creationdate><title>Characterization of an Alkaline Transition Intermediate Stabilized in the Phe82Trp Variant of Yeast iso-1-Cytochrome c</title><author>Rosell, Federico I ; Harris, Thomas R ; Hildebrand, Dean P ; Döpner, Susanne ; Hildebrandt, Peter ; Mauk, A. Grant</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a349t-83704eea044605c390439d252d1e0a499e29957c83f6872a8f2efb0937ba72af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Substitution</topic><topic>Cytochrome c Group - chemistry</topic><topic>Cytochrome c Group - genetics</topic><topic>Cytochrome c Group - metabolism</topic><topic>Cytochromes c</topic><topic>Electrochemistry</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Enzyme Stability</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Heme - chemistry</topic><topic>Heme - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Iron - chemistry</topic><topic>Iron - metabolism</topic><topic>Kinetics</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Oxidation-Reduction</topic><topic>Phenylalanine - chemistry</topic><topic>Phenylalanine - genetics</topic><topic>Phenylalanine - metabolism</topic><topic>Protein Conformation</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Spectrum Analysis, Raman</topic><topic>Structure-Activity Relationship</topic><topic>Tryptophan - chemistry</topic><topic>Tryptophan - genetics</topic><topic>Tryptophan - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rosell, Federico I</creatorcontrib><creatorcontrib>Harris, Thomas R</creatorcontrib><creatorcontrib>Hildebrand, Dean P</creatorcontrib><creatorcontrib>Döpner, Susanne</creatorcontrib><creatorcontrib>Hildebrandt, Peter</creatorcontrib><creatorcontrib>Mauk, A. Grant</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rosell, Federico I</au><au>Harris, Thomas R</au><au>Hildebrand, Dean P</au><au>Döpner, Susanne</au><au>Hildebrandt, Peter</au><au>Mauk, A. Grant</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of an Alkaline Transition Intermediate Stabilized in the Phe82Trp Variant of Yeast iso-1-Cytochrome c</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2000-08-01</date><risdate>2000</risdate><volume>39</volume><issue>30</issue><spage>9047</spage><epage>9054</epage><pages>9047-9054</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>In general, mutation of the phylogenetically conserved residue Phe82 in yeast iso-1-cytochrome c destabilizes the native conformation of the protein by facilitating the ligand exchange reactions that are associated with the alkaline conformational transitions of the ferricytochrome. Of the Phe82 variants surveyed thus far, Phe82Trp is unique in that it adopts a thermodynamically stable, high-spin conformation at mildly alkaline pH. This species exhibits spectroscopic features that can only be detected transiently in other ferricytochromes c within the first 100 ms immediately after a pH-jump from neutrality to pH >10. Spectroscopic characterization of this high-spin reaction intermediate suggests that in addition to an obligatory pentacoordinate heme iron, a group within the heme pocket coordinates the heme iron but is then replaced either by Met80, to revert to the native conformation, or by Lys73 or Lys79, to yield one of the conventional alkaline conformers. Evidence is presented to suggest that this group is either a hydroxide ion or Tyr67 rather than a loosely bound Met80.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>10913318</pmid><doi>10.1021/bi001095k</doi><tpages>8</tpages></addata></record> |
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| subjects | Amino Acid Substitution Cytochrome c Group - chemistry Cytochrome c Group - genetics Cytochrome c Group - metabolism Cytochromes c Electrochemistry Electron Spin Resonance Spectroscopy Enzyme Stability Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Heme - chemistry Heme - metabolism Hydrogen-Ion Concentration Iron - chemistry Iron - metabolism Kinetics Nuclear Magnetic Resonance, Biomolecular Oxidation-Reduction Phenylalanine - chemistry Phenylalanine - genetics Phenylalanine - metabolism Protein Conformation Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins Spectrum Analysis, Raman Structure-Activity Relationship Tryptophan - chemistry Tryptophan - genetics Tryptophan - metabolism |
| title | Characterization of an Alkaline Transition Intermediate Stabilized in the Phe82Trp Variant of Yeast iso-1-Cytochrome c |
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