Relating the multi-functionality of cytochrome c to membrane binding and structural conversion
Cytochrome c is known as an electron-carrying protein in the respiratory chain of mitochondria. Over the last 20 years, however, alternative functions of this very versatile protein have become the focus of research interests. Upon binding to anionic lipids such as cardiolipin, the protein acquires...
Gespeichert in:
Veröffentlicht in: | Biophysical reviews 2018-08, Vol.10 (4), p.1151-1185 |
---|---|
1. Verfasser: | |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1185 |
---|---|
container_issue | 4 |
container_start_page | 1151 |
container_title | Biophysical reviews |
container_volume | 10 |
creator | Schweitzer-Stenner, Reinhard |
description | Cytochrome c is known as an electron-carrying protein in the respiratory chain of mitochondria. Over the last 20 years, however, alternative functions of this very versatile protein have become the focus of research interests. Upon binding to anionic lipids such as cardiolipin, the protein acquires peroxidase activity. Multiple lines of evidence suggest that this requires a conformational change of the protein which involves partial unfolding of its tertiary structure. This review summarizes the current state of knowledge of how cytochrome c interacts with cardiolipin-containing surfaces and how this affects its structure and function. In this context, we delineate partially conflicting results regarding the affinity of cytochrome c binding to cardiolipin-containing liposomes of different size and its influence on the structure of the protein and the morphology of the membrane. |
doi_str_mv | 10.1007/s12551-018-0409-4 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6082307</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2084396602</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4884-d013e299c5e11eeb802af46dd7be18c4db5b83c25009fa7cc9685d770e94d3383</originalsourceid><addsrcrecordid>eNp1kUtr3TAQhU1padK0P6CbIuimGzcjWS9vCiWkDwgESrutkKXxvQ62lEpy4P776HLT2wdkpYH5ztHMnKZ5TeE9BVDnmTIhaAtUt8Chb_mT5pRqqVrGZf_0WAs4aV7kfAMgOdPieXPCeqG4ZPS0-fkNZ1umsCFli2RZ5zK14xpcmWKw81R2JI7E7Up02xQXJI6USBZchmQDkmEKfq-1wZNc0urKmuxMXAx3mHK1eNk8G-2c8dXDe9b8-HT5_eJLe3X9-evFx6vWca1564F2yPreCaQUcdDA7Mil92pAqh33gxh055gA6EernOulFl4pwJ77rtPdWfPh4Hu7Dgt6h6HUQcxtmhabdibayfzbCdPWbOKdkaBZB6oavHswSPHXirmYZcoO57muGddsWD2ylEppqOjb_9CbuKZ6rT2leddLCaxS9EC5FHNOOB6HoWD26ZlDeqYam316hlfNm7-3OCp-x1UBdgBybYUNpj9fP-56D68QpwM</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2084396602</pqid></control><display><type>article</type><title>Relating the multi-functionality of cytochrome c to membrane binding and structural conversion</title><source>Springer Online Journals Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Schweitzer-Stenner, Reinhard</creator><creatorcontrib>Schweitzer-Stenner, Reinhard</creatorcontrib><description>Cytochrome c is known as an electron-carrying protein in the respiratory chain of mitochondria. Over the last 20 years, however, alternative functions of this very versatile protein have become the focus of research interests. Upon binding to anionic lipids such as cardiolipin, the protein acquires peroxidase activity. Multiple lines of evidence suggest that this requires a conformational change of the protein which involves partial unfolding of its tertiary structure. This review summarizes the current state of knowledge of how cytochrome c interacts with cardiolipin-containing surfaces and how this affects its structure and function. In this context, we delineate partially conflicting results regarding the affinity of cytochrome c binding to cardiolipin-containing liposomes of different size and its influence on the structure of the protein and the morphology of the membrane.</description><identifier>ISSN: 1867-2450</identifier><identifier>EISSN: 1867-2469</identifier><identifier>DOI: 10.1007/s12551-018-0409-4</identifier><identifier>PMID: 29574621</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Binding ; Biochemistry ; Biological and Medical Physics ; Biological Techniques ; Biomedical and Life Sciences ; Biophysics ; Cardiolipin ; Cell Biology ; Cytochrome ; Cytochrome c ; Cytochromes ; Electron transport ; Life Sciences ; Lipid peroxidation ; Lipids ; Liposomes ; Membrane Biology ; Mitochondria ; Mitochondrial DNA ; Morphology ; Nanotechnology ; Peroxidase ; Protein folding ; Protein structure ; Proteins ; Review ; Structure-function relationships ; Tertiary structure</subject><ispartof>Biophysical reviews, 2018-08, Vol.10 (4), p.1151-1185</ispartof><rights>International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2018</rights><rights>Copyright Springer Science & Business Media 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4884-d013e299c5e11eeb802af46dd7be18c4db5b83c25009fa7cc9685d770e94d3383</citedby><cites>FETCH-LOGICAL-c4884-d013e299c5e11eeb802af46dd7be18c4db5b83c25009fa7cc9685d770e94d3383</cites><orcidid>0000-0001-5616-0722</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6082307/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6082307/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41488,42557,51319,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29574621$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schweitzer-Stenner, Reinhard</creatorcontrib><title>Relating the multi-functionality of cytochrome c to membrane binding and structural conversion</title><title>Biophysical reviews</title><addtitle>Biophys Rev</addtitle><addtitle>Biophys Rev</addtitle><description>Cytochrome c is known as an electron-carrying protein in the respiratory chain of mitochondria. Over the last 20 years, however, alternative functions of this very versatile protein have become the focus of research interests. Upon binding to anionic lipids such as cardiolipin, the protein acquires peroxidase activity. Multiple lines of evidence suggest that this requires a conformational change of the protein which involves partial unfolding of its tertiary structure. This review summarizes the current state of knowledge of how cytochrome c interacts with cardiolipin-containing surfaces and how this affects its structure and function. In this context, we delineate partially conflicting results regarding the affinity of cytochrome c binding to cardiolipin-containing liposomes of different size and its influence on the structure of the protein and the morphology of the membrane.</description><subject>Binding</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biological Techniques</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Cardiolipin</subject><subject>Cell Biology</subject><subject>Cytochrome</subject><subject>Cytochrome c</subject><subject>Cytochromes</subject><subject>Electron transport</subject><subject>Life Sciences</subject><subject>Lipid peroxidation</subject><subject>Lipids</subject><subject>Liposomes</subject><subject>Membrane Biology</subject><subject>Mitochondria</subject><subject>Mitochondrial DNA</subject><subject>Morphology</subject><subject>Nanotechnology</subject><subject>Peroxidase</subject><subject>Protein folding</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Review</subject><subject>Structure-function relationships</subject><subject>Tertiary structure</subject><issn>1867-2450</issn><issn>1867-2469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp1kUtr3TAQhU1padK0P6CbIuimGzcjWS9vCiWkDwgESrutkKXxvQ62lEpy4P776HLT2wdkpYH5ztHMnKZ5TeE9BVDnmTIhaAtUt8Chb_mT5pRqqVrGZf_0WAs4aV7kfAMgOdPieXPCeqG4ZPS0-fkNZ1umsCFli2RZ5zK14xpcmWKw81R2JI7E7Up02xQXJI6USBZchmQDkmEKfq-1wZNc0urKmuxMXAx3mHK1eNk8G-2c8dXDe9b8-HT5_eJLe3X9-evFx6vWca1564F2yPreCaQUcdDA7Mil92pAqh33gxh055gA6EernOulFl4pwJ77rtPdWfPh4Hu7Dgt6h6HUQcxtmhabdibayfzbCdPWbOKdkaBZB6oavHswSPHXirmYZcoO57muGddsWD2ylEppqOjb_9CbuKZ6rT2leddLCaxS9EC5FHNOOB6HoWD26ZlDeqYam316hlfNm7-3OCp-x1UBdgBybYUNpj9fP-56D68QpwM</recordid><startdate>20180801</startdate><enddate>20180801</enddate><creator>Schweitzer-Stenner, Reinhard</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-5616-0722</orcidid></search><sort><creationdate>20180801</creationdate><title>Relating the multi-functionality of cytochrome c to membrane binding and structural conversion</title><author>Schweitzer-Stenner, Reinhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4884-d013e299c5e11eeb802af46dd7be18c4db5b83c25009fa7cc9685d770e94d3383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Binding</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biological Techniques</topic><topic>Biomedical and Life Sciences</topic><topic>Biophysics</topic><topic>Cardiolipin</topic><topic>Cell Biology</topic><topic>Cytochrome</topic><topic>Cytochrome c</topic><topic>Cytochromes</topic><topic>Electron transport</topic><topic>Life Sciences</topic><topic>Lipid peroxidation</topic><topic>Lipids</topic><topic>Liposomes</topic><topic>Membrane Biology</topic><topic>Mitochondria</topic><topic>Mitochondrial DNA</topic><topic>Morphology</topic><topic>Nanotechnology</topic><topic>Peroxidase</topic><topic>Protein folding</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Review</topic><topic>Structure-function relationships</topic><topic>Tertiary structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schweitzer-Stenner, Reinhard</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical reviews</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schweitzer-Stenner, Reinhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Relating the multi-functionality of cytochrome c to membrane binding and structural conversion</atitle><jtitle>Biophysical reviews</jtitle><stitle>Biophys Rev</stitle><addtitle>Biophys Rev</addtitle><date>2018-08-01</date><risdate>2018</risdate><volume>10</volume><issue>4</issue><spage>1151</spage><epage>1185</epage><pages>1151-1185</pages><issn>1867-2450</issn><eissn>1867-2469</eissn><abstract>Cytochrome c is known as an electron-carrying protein in the respiratory chain of mitochondria. Over the last 20 years, however, alternative functions of this very versatile protein have become the focus of research interests. Upon binding to anionic lipids such as cardiolipin, the protein acquires peroxidase activity. Multiple lines of evidence suggest that this requires a conformational change of the protein which involves partial unfolding of its tertiary structure. This review summarizes the current state of knowledge of how cytochrome c interacts with cardiolipin-containing surfaces and how this affects its structure and function. In this context, we delineate partially conflicting results regarding the affinity of cytochrome c binding to cardiolipin-containing liposomes of different size and its influence on the structure of the protein and the morphology of the membrane.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29574621</pmid><doi>10.1007/s12551-018-0409-4</doi><tpages>35</tpages><orcidid>https://orcid.org/0000-0001-5616-0722</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1867-2450 |
ispartof | Biophysical reviews, 2018-08, Vol.10 (4), p.1151-1185 |
issn | 1867-2450 1867-2469 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6082307 |
source | Springer Online Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
subjects | Binding Biochemistry Biological and Medical Physics Biological Techniques Biomedical and Life Sciences Biophysics Cardiolipin Cell Biology Cytochrome Cytochrome c Cytochromes Electron transport Life Sciences Lipid peroxidation Lipids Liposomes Membrane Biology Mitochondria Mitochondrial DNA Morphology Nanotechnology Peroxidase Protein folding Protein structure Proteins Review Structure-function relationships Tertiary structure |
title | Relating the multi-functionality of cytochrome c to membrane binding and structural conversion |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-21T01%3A22%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Relating%20the%20multi-functionality%20of%20cytochrome%20c%20to%20membrane%20binding%20and%20structural%20conversion&rft.jtitle=Biophysical%20reviews&rft.au=Schweitzer-Stenner,%20Reinhard&rft.date=2018-08-01&rft.volume=10&rft.issue=4&rft.spage=1151&rft.epage=1185&rft.pages=1151-1185&rft.issn=1867-2450&rft.eissn=1867-2469&rft_id=info:doi/10.1007/s12551-018-0409-4&rft_dat=%3Cproquest_pubme%3E2084396602%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2084396602&rft_id=info:pmid/29574621&rfr_iscdi=true |