Membrane binding induces destabilization of cytochrome c structure
The effect of membranes binding on the structure and stability of ferricytochrome c was studied by Fourier-transform infrared spectroscopy and differential scanning calorimetry. Association of cytochrome c with phospholipid membranes containing phosphatidylglycerol as a model acidic phospholipid res...
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Veröffentlicht in: | Biochemistry (Easton) 1991-07, Vol.30 (29), p.7219-7224 |
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description | The effect of membranes binding on the structure and stability of ferricytochrome c was studied by Fourier-transform infrared spectroscopy and differential scanning calorimetry. Association of cytochrome c with phospholipid membranes containing phosphatidylglycerol as a model acidic phospholipid results in only slight, if any, perturbation of the protein secondary structure. However, upon membrane binding, there is a considerable increase in the accessibility of protein backbone amide groups to hydrogen-deuterium exchange, which suggests a lipid-mediated loosening and/or destabilization of the protein tertiary structure. A lipid-induced conformational perturbation of ferricytochrome c is also indicated by a marked decrease in the thermodynamic stability of the membrane-bound protein. Upon binding to membranes containing dimyristoylphosphatidylglycerol (DMPG) or dioleoylphosphatidylglycerol (DOPG) as a single lipid component, the denaturation temperature of ferricytochrome c decreases by approximately 30 degrees C. This is accompanied by a decrease in the calorimetric enthalpy of denaturation, particularly for the DMPG-associated protein. With ferricytochrome c bound to membranes containing a mixture of DMPG (or DOPG) and zwitterionic phosphatidylcholine, the extent of structural perturbation depends on the surface density of the negatively charged lipid head groups, becoming smaller with decreasing proportions of acidic phospholipid in the membrane. The observed destabilization of protein structure mediated by acidic phospholipids (and possibly formation of folding intermediates at the membrane surface) may represent a general property of a larger class of water-soluble proteins for which membrane binding is governed by electrostatic forces. |
doi_str_mv | 10.1021/bi00243a025 |
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Association of cytochrome c with phospholipid membranes containing phosphatidylglycerol as a model acidic phospholipid results in only slight, if any, perturbation of the protein secondary structure. However, upon membrane binding, there is a considerable increase in the accessibility of protein backbone amide groups to hydrogen-deuterium exchange, which suggests a lipid-mediated loosening and/or destabilization of the protein tertiary structure. A lipid-induced conformational perturbation of ferricytochrome c is also indicated by a marked decrease in the thermodynamic stability of the membrane-bound protein. Upon binding to membranes containing dimyristoylphosphatidylglycerol (DMPG) or dioleoylphosphatidylglycerol (DOPG) as a single lipid component, the denaturation temperature of ferricytochrome c decreases by approximately 30 degrees C. This is accompanied by a decrease in the calorimetric enthalpy of denaturation, particularly for the DMPG-associated protein. With ferricytochrome c bound to membranes containing a mixture of DMPG (or DOPG) and zwitterionic phosphatidylcholine, the extent of structural perturbation depends on the surface density of the negatively charged lipid head groups, becoming smaller with decreasing proportions of acidic phospholipid in the membrane. The observed destabilization of protein structure mediated by acidic phospholipids (and possibly formation of folding intermediates at the membrane surface) may represent a general property of a larger class of water-soluble proteins for which membrane binding is governed by electrostatic forces.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00243a025</identifier><identifier>PMID: 1649625</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Calorimetry, Differential Scanning ; Cell Membrane - metabolism ; Circular Dichroism ; Cytochrome c Group - metabolism ; differential scanning calorimetry ; Fourier Analysis ; Fundamental and applied biological sciences. Psychology ; Hemoproteins ; Horses ; I.R. spectroscopy ; Membrane Lipids - metabolism ; Metalloproteins ; Phosphatidylglycerols - metabolism ; Phospholipids - metabolism ; plasma membranes ; Proteins ; Spectrophotometry, Infrared ; Temperature ; Thermodynamics</subject><ispartof>Biochemistry (Easton), 1991-07, Vol.30 (29), p.7219-7224</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a443t-93b3ecbb49e605309554fcd17d4b753e65133a3bbdeafc138a1191c5f6f951ee3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00243a025$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00243a025$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5599292$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1649625$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Muga, Arturo</creatorcontrib><creatorcontrib>Mantsch, Henry H</creatorcontrib><creatorcontrib>Surewicz, Witold K</creatorcontrib><title>Membrane binding induces destabilization of cytochrome c structure</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The effect of membranes binding on the structure and stability of ferricytochrome c was studied by Fourier-transform infrared spectroscopy and differential scanning calorimetry. Association of cytochrome c with phospholipid membranes containing phosphatidylglycerol as a model acidic phospholipid results in only slight, if any, perturbation of the protein secondary structure. However, upon membrane binding, there is a considerable increase in the accessibility of protein backbone amide groups to hydrogen-deuterium exchange, which suggests a lipid-mediated loosening and/or destabilization of the protein tertiary structure. A lipid-induced conformational perturbation of ferricytochrome c is also indicated by a marked decrease in the thermodynamic stability of the membrane-bound protein. Upon binding to membranes containing dimyristoylphosphatidylglycerol (DMPG) or dioleoylphosphatidylglycerol (DOPG) as a single lipid component, the denaturation temperature of ferricytochrome c decreases by approximately 30 degrees C. This is accompanied by a decrease in the calorimetric enthalpy of denaturation, particularly for the DMPG-associated protein. With ferricytochrome c bound to membranes containing a mixture of DMPG (or DOPG) and zwitterionic phosphatidylcholine, the extent of structural perturbation depends on the surface density of the negatively charged lipid head groups, becoming smaller with decreasing proportions of acidic phospholipid in the membrane. The observed destabilization of protein structure mediated by acidic phospholipids (and possibly formation of folding intermediates at the membrane surface) may represent a general property of a larger class of water-soluble proteins for which membrane binding is governed by electrostatic forces.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calorimetry, Differential Scanning</subject><subject>Cell Membrane - metabolism</subject><subject>Circular Dichroism</subject><subject>Cytochrome c Group - metabolism</subject><subject>differential scanning calorimetry</subject><subject>Fourier Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemoproteins</subject><subject>Horses</subject><subject>I.R. spectroscopy</subject><subject>Membrane Lipids - metabolism</subject><subject>Metalloproteins</subject><subject>Phosphatidylglycerols - metabolism</subject><subject>Phospholipids - metabolism</subject><subject>plasma membranes</subject><subject>Proteins</subject><subject>Spectrophotometry, Infrared</subject><subject>Temperature</subject><subject>Thermodynamics</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LHTEUhkOp6K3tyrUwi2IXMvZk8jE3y1ZaFbxWUNvSTUgyZzR2PjSZAW9_vdG5XLsodHU4vA8vLw8hOxQOKBT0o_UABWcGCvGKzKgoIOdKiddkBgAyL5SELfImxtv0cij5JtmkkitZiBn5vMDWBtNhZn1X-e46S2d0GLMK42Csb_wfM_i-y_o6c8uhdzehbzFzWRzC6IYx4FuyUZsm4rvV3SZXX79cHh7np9-OTg4_neaGczbkilmGzlquUIJgoITgtatoWXFbCoZSUMYMs7ZCUzvK5oZSRZ2oZa0ERWTbZG_qvQv9_ZjW6dZHh02T1vdj1HOQqpwL-C9IZdKlnsH9CXShjzFgre-Cb01Yagr6Sa3-S22id1e1o22xemEnlyl_v8pNdKapk1Xn4xoTQqlCFQnLJ8zHAR_WsQm_tSxZKfTl-YVenMHP778WP7RK_IeJNy7q234MXZL8z4GPnMOcBA</recordid><startdate>19910723</startdate><enddate>19910723</enddate><creator>Muga, Arturo</creator><creator>Mantsch, Henry H</creator><creator>Surewicz, Witold K</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>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19910723</creationdate><title>Membrane binding induces destabilization of cytochrome c structure</title><author>Muga, Arturo ; Mantsch, Henry H ; Surewicz, Witold K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a443t-93b3ecbb49e605309554fcd17d4b753e65133a3bbdeafc138a1191c5f6f951ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calorimetry, Differential Scanning</topic><topic>Cell Membrane - metabolism</topic><topic>Circular Dichroism</topic><topic>Cytochrome c Group - metabolism</topic><topic>differential scanning calorimetry</topic><topic>Fourier Analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemoproteins</topic><topic>Horses</topic><topic>I.R. spectroscopy</topic><topic>Membrane Lipids - metabolism</topic><topic>Metalloproteins</topic><topic>Phosphatidylglycerols - metabolism</topic><topic>Phospholipids - metabolism</topic><topic>plasma membranes</topic><topic>Proteins</topic><topic>Spectrophotometry, Infrared</topic><topic>Temperature</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Muga, Arturo</creatorcontrib><creatorcontrib>Mantsch, Henry H</creatorcontrib><creatorcontrib>Surewicz, Witold K</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>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Muga, Arturo</au><au>Mantsch, Henry H</au><au>Surewicz, Witold K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane binding induces destabilization of cytochrome c structure</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1991-07-23</date><risdate>1991</risdate><volume>30</volume><issue>29</issue><spage>7219</spage><epage>7224</epage><pages>7219-7224</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The effect of membranes binding on the structure and stability of ferricytochrome c was studied by Fourier-transform infrared spectroscopy and differential scanning calorimetry. Association of cytochrome c with phospholipid membranes containing phosphatidylglycerol as a model acidic phospholipid results in only slight, if any, perturbation of the protein secondary structure. However, upon membrane binding, there is a considerable increase in the accessibility of protein backbone amide groups to hydrogen-deuterium exchange, which suggests a lipid-mediated loosening and/or destabilization of the protein tertiary structure. A lipid-induced conformational perturbation of ferricytochrome c is also indicated by a marked decrease in the thermodynamic stability of the membrane-bound protein. Upon binding to membranes containing dimyristoylphosphatidylglycerol (DMPG) or dioleoylphosphatidylglycerol (DOPG) as a single lipid component, the denaturation temperature of ferricytochrome c decreases by approximately 30 degrees C. This is accompanied by a decrease in the calorimetric enthalpy of denaturation, particularly for the DMPG-associated protein. With ferricytochrome c bound to membranes containing a mixture of DMPG (or DOPG) and zwitterionic phosphatidylcholine, the extent of structural perturbation depends on the surface density of the negatively charged lipid head groups, becoming smaller with decreasing proportions of acidic phospholipid in the membrane. The observed destabilization of protein structure mediated by acidic phospholipids (and possibly formation of folding intermediates at the membrane surface) may represent a general property of a larger class of water-soluble proteins for which membrane binding is governed by electrostatic forces.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>1649625</pmid><doi>10.1021/bi00243a025</doi><tpages>6</tpages></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calorimetry, Differential Scanning Cell Membrane - metabolism Circular Dichroism Cytochrome c Group - metabolism differential scanning calorimetry Fourier Analysis Fundamental and applied biological sciences. Psychology Hemoproteins Horses I.R. spectroscopy Membrane Lipids - metabolism Metalloproteins Phosphatidylglycerols - metabolism Phospholipids - metabolism plasma membranes Proteins Spectrophotometry, Infrared Temperature Thermodynamics |
title | Membrane binding induces destabilization of cytochrome c structure |
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