Anion Size Modulates the Structure of the A State of Cytochrome c
Several studies have shown that anions induce collapse of acid-denatured cytochrome c into the compact A state having the properties of the molten globule and that the anion charge is the main determinant for the A state stabilization. The results here reported show that the anion size plays a role...
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| Veröffentlicht in: | Biochemistry (Easton) 2000-10, Vol.39 (41), p.12632-12638 |
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| creator | Santucci, Roberto Bongiovanni, Cristiana Mei, Giampiero Ferri, Tommaso Polizio, Francesca Desideri, Alessandro |
| description | Several studies have shown that anions induce collapse of acid-denatured cytochrome c into the compact A state having the properties of the molten globule and that the anion charge is the main determinant for the A state stabilization. The results here reported show that the anion size plays a role in determining the overall structure of the A state. In particular, small anions induce formation of an A state in which the native Met80−Fe(III) axial bond is recovered and the nativelike redox properties restored. On the other hand, the A state stabilized by large anions shows a histidine (His26 or His33) as the sixth ligand of the heme-iron, a very weak interaction between Trp59 and the heme propionate, and lacks nativelike redox properties. The two anion-stabilized states show similar stability, indicating that (i) the hydrophobic core (which is equally stabilized by all the anions investigated, independently of their size) is the region that mainly contributes to the macromolecule stabilization, and (ii) the flexible loops are responsible for the spectroscopic (and, thus, structural) and redox differences observed. |
| doi_str_mv | 10.1021/bi000516v |
| format | Article |
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The results here reported show that the anion size plays a role in determining the overall structure of the A state. In particular, small anions induce formation of an A state in which the native Met80−Fe(III) axial bond is recovered and the nativelike redox properties restored. On the other hand, the A state stabilized by large anions shows a histidine (His26 or His33) as the sixth ligand of the heme-iron, a very weak interaction between Trp59 and the heme propionate, and lacks nativelike redox properties. The two anion-stabilized states show similar stability, indicating that (i) the hydrophobic core (which is equally stabilized by all the anions investigated, independently of their size) is the region that mainly contributes to the macromolecule stabilization, and (ii) the flexible loops are responsible for the spectroscopic (and, thus, structural) and redox differences observed.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi000516v</identifier><identifier>PMID: 11027143</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Anions ; Circular Dichroism ; Cytochrome c Group - chemistry ; Electrochemistry ; Electron Spin Resonance Spectroscopy ; Horses ; Hydrogen-Ion Concentration ; Models, Chemical ; Oxidation-Reduction ; Perchlorates - chemistry ; Protein Denaturation ; Protein Folding ; Salts - chemistry ; Sodium Chloride - chemistry ; Sodium Compounds - chemistry ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Structure-Activity Relationship ; Temperature ; Thermodynamics ; Titrimetry</subject><ispartof>Biochemistry (Easton), 2000-10, Vol.39 (41), p.12632-12638</ispartof><rights>Copyright © 2000 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a415t-c61e849a5886d433994a9d8b66d0bfb27cd0555f658025e052b1972e08b337bd3</citedby><cites>FETCH-LOGICAL-a415t-c61e849a5886d433994a9d8b66d0bfb27cd0555f658025e052b1972e08b337bd3</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/bi000516v$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi000516v$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11027143$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Santucci, Roberto</creatorcontrib><creatorcontrib>Bongiovanni, Cristiana</creatorcontrib><creatorcontrib>Mei, Giampiero</creatorcontrib><creatorcontrib>Ferri, Tommaso</creatorcontrib><creatorcontrib>Polizio, Francesca</creatorcontrib><creatorcontrib>Desideri, Alessandro</creatorcontrib><title>Anion Size Modulates the Structure of the A State of Cytochrome c</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Several studies have shown that anions induce collapse of acid-denatured cytochrome c into the compact A state having the properties of the molten globule and that the anion charge is the main determinant for the A state stabilization. The results here reported show that the anion size plays a role in determining the overall structure of the A state. In particular, small anions induce formation of an A state in which the native Met80−Fe(III) axial bond is recovered and the nativelike redox properties restored. On the other hand, the A state stabilized by large anions shows a histidine (His26 or His33) as the sixth ligand of the heme-iron, a very weak interaction between Trp59 and the heme propionate, and lacks nativelike redox properties. The two anion-stabilized states show similar stability, indicating that (i) the hydrophobic core (which is equally stabilized by all the anions investigated, independently of their size) is the region that mainly contributes to the macromolecule stabilization, and (ii) the flexible loops are responsible for the spectroscopic (and, thus, structural) and redox differences observed.</description><subject>Animals</subject><subject>Anions</subject><subject>Circular Dichroism</subject><subject>Cytochrome c Group - chemistry</subject><subject>Electrochemistry</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Horses</subject><subject>Hydrogen-Ion Concentration</subject><subject>Models, Chemical</subject><subject>Oxidation-Reduction</subject><subject>Perchlorates - chemistry</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Salts - chemistry</subject><subject>Sodium Chloride - chemistry</subject><subject>Sodium Compounds - chemistry</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Structure-Activity Relationship</subject><subject>Temperature</subject><subject>Thermodynamics</subject><subject>Titrimetry</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>eNptkM1Kw0AUhQdRbK0ufAHJRsFFdP4nsyxFW6Gi0CruhkkyoalJp84kYn16p6bUjavLOee798IB4BzBGwQxuk1LCCFD_PMA9BHDMKZSskPQDy6PseSwB068XwZJoaDHoIfCmkCU9MFwuCrtKpqV3yZ6tHlb6cb4qFmYaNa4NmtaZyJb_BrDYIV0K0ebxmYLZ2sTZafgqNCVN2e7OQAv93fz0SSePo0fRsNprCliTZxxZBIqNUsSnlNCpKRa5knKeQ7TIsUiyyFjrOAsgZgZyHCKpMAGJikhIs3JAFx1d9fOfrTGN6oufWaqSq-Mbb0SmGAChQzgdQdmznrvTKHWrqy12ygE1bYvte8rsBe7o21am_yP3BUUgLgDSt-Yr32u3bviggim5s8zhV75GL1N5ooG_rLjdebV0rZuFTr55_EPWm19-w</recordid><startdate>20001017</startdate><enddate>20001017</enddate><creator>Santucci, Roberto</creator><creator>Bongiovanni, Cristiana</creator><creator>Mei, Giampiero</creator><creator>Ferri, Tommaso</creator><creator>Polizio, Francesca</creator><creator>Desideri, Alessandro</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>20001017</creationdate><title>Anion Size Modulates the Structure of the A State of Cytochrome c</title><author>Santucci, Roberto ; Bongiovanni, Cristiana ; Mei, Giampiero ; Ferri, Tommaso ; Polizio, Francesca ; Desideri, Alessandro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a415t-c61e849a5886d433994a9d8b66d0bfb27cd0555f658025e052b1972e08b337bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Anions</topic><topic>Circular Dichroism</topic><topic>Cytochrome c Group - chemistry</topic><topic>Electrochemistry</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Horses</topic><topic>Hydrogen-Ion Concentration</topic><topic>Models, Chemical</topic><topic>Oxidation-Reduction</topic><topic>Perchlorates - chemistry</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Salts - chemistry</topic><topic>Sodium Chloride - chemistry</topic><topic>Sodium Compounds - chemistry</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Structure-Activity Relationship</topic><topic>Temperature</topic><topic>Thermodynamics</topic><topic>Titrimetry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Santucci, Roberto</creatorcontrib><creatorcontrib>Bongiovanni, Cristiana</creatorcontrib><creatorcontrib>Mei, Giampiero</creatorcontrib><creatorcontrib>Ferri, Tommaso</creatorcontrib><creatorcontrib>Polizio, Francesca</creatorcontrib><creatorcontrib>Desideri, Alessandro</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>Santucci, Roberto</au><au>Bongiovanni, Cristiana</au><au>Mei, Giampiero</au><au>Ferri, Tommaso</au><au>Polizio, Francesca</au><au>Desideri, Alessandro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Anion Size Modulates the Structure of the A State of Cytochrome c</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2000-10-17</date><risdate>2000</risdate><volume>39</volume><issue>41</issue><spage>12632</spage><epage>12638</epage><pages>12632-12638</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Several studies have shown that anions induce collapse of acid-denatured cytochrome c into the compact A state having the properties of the molten globule and that the anion charge is the main determinant for the A state stabilization. The results here reported show that the anion size plays a role in determining the overall structure of the A state. In particular, small anions induce formation of an A state in which the native Met80−Fe(III) axial bond is recovered and the nativelike redox properties restored. On the other hand, the A state stabilized by large anions shows a histidine (His26 or His33) as the sixth ligand of the heme-iron, a very weak interaction between Trp59 and the heme propionate, and lacks nativelike redox properties. The two anion-stabilized states show similar stability, indicating that (i) the hydrophobic core (which is equally stabilized by all the anions investigated, independently of their size) is the region that mainly contributes to the macromolecule stabilization, and (ii) the flexible loops are responsible for the spectroscopic (and, thus, structural) and redox differences observed.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>11027143</pmid><doi>10.1021/bi000516v</doi><tpages>7</tpages></addata></record> |
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| subjects | Animals Anions Circular Dichroism Cytochrome c Group - chemistry Electrochemistry Electron Spin Resonance Spectroscopy Horses Hydrogen-Ion Concentration Models, Chemical Oxidation-Reduction Perchlorates - chemistry Protein Denaturation Protein Folding Salts - chemistry Sodium Chloride - chemistry Sodium Compounds - chemistry Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Structure-Activity Relationship Temperature Thermodynamics Titrimetry |
| title | Anion Size Modulates the Structure of the A State of Cytochrome c |
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