Thiol redox biochemistry: insights from computer simulations
Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly due to the presence of low-molecular-weight thiols and cysteine residues in proteins involved in catalysis and regulation. Specifically, the subtle sensitivity of thiol reactivity to the environment makes...
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| Veröffentlicht in: | Biophysical reviews 2014-03, Vol.6 (1), p.27-46 |
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| container_title | Biophysical reviews |
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| creator | Zeida, Ari Guardia, Carlos M. Lichtig, Pablo Perissinotti, Laura L. Defelipe, Lucas A. Turjanski, Adrián Radi, Rafael Trujillo, Madia Estrin, Darío A. |
| description | Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly due to the presence of low-molecular-weight thiols and cysteine residues in proteins involved in catalysis and regulation. Specifically, the subtle sensitivity of thiol reactivity to the environment makes the use of simulation techniques extremely valuable for obtaining microscopic insights. In this work we review the application of classical and quantum–mechanical atomistic simulation tools to the investigation of selected relevant issues in thiol redox biochemistry, such as investigations on (1) the protonation state of cysteine in protein, (2) two-electron oxidation of thiols by hydroperoxides, chloramines, and hypochlorous acid, (3) mechanistic and kinetics aspects of the de novo formation of disulfide bonds and thiol−disulfide exchange, (4) formation of sulfenamides, (5) formation of nitrosothiols and transnitrosation reactions, and (6) one-electron oxidation pathways. |
| doi_str_mv | 10.1007/s12551-013-0127-x |
| format | Article |
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In this work we review the application of classical and quantum–mechanical atomistic simulation tools to the investigation of selected relevant issues in thiol redox biochemistry, such as investigations on (1) the protonation state of cysteine in protein, (2) two-electron oxidation of thiols by hydroperoxides, chloramines, and hypochlorous acid, (3) mechanistic and kinetics aspects of the de novo formation of disulfide bonds and thiol−disulfide exchange, (4) formation of sulfenamides, (5) formation of nitrosothiols and transnitrosation reactions, and (6) one-electron oxidation pathways.</description><identifier>ISSN: 1867-2450</identifier><identifier>EISSN: 1867-2469</identifier><identifier>DOI: 10.1007/s12551-013-0127-x</identifier><identifier>PMID: 28509962</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Biochemistry ; Biological and Medical Physics ; Biological Techniques ; Biomedical and Life Sciences ; Biophysics ; Cell Biology ; Life Sciences ; Membrane Biology ; Nanotechnology ; Review</subject><ispartof>Biophysical reviews, 2014-03, Vol.6 (1), p.27-46</ispartof><rights>International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg 2014</rights><rights>International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357x-5c4dfb3b11897fc9f5f15b3d526bb9a56944472620018a3c58d58c734e8a92b33</citedby><cites>FETCH-LOGICAL-c357x-5c4dfb3b11897fc9f5f15b3d526bb9a56944472620018a3c58d58c734e8a92b33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5427810/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5427810/$$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/28509962$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zeida, Ari</creatorcontrib><creatorcontrib>Guardia, Carlos M.</creatorcontrib><creatorcontrib>Lichtig, Pablo</creatorcontrib><creatorcontrib>Perissinotti, Laura L.</creatorcontrib><creatorcontrib>Defelipe, Lucas A.</creatorcontrib><creatorcontrib>Turjanski, Adrián</creatorcontrib><creatorcontrib>Radi, Rafael</creatorcontrib><creatorcontrib>Trujillo, Madia</creatorcontrib><creatorcontrib>Estrin, Darío A.</creatorcontrib><title>Thiol redox biochemistry: insights from computer simulations</title><title>Biophysical reviews</title><addtitle>Biophys Rev</addtitle><addtitle>Biophys Rev</addtitle><description>Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly due to the presence of low-molecular-weight thiols and cysteine residues in proteins involved in catalysis and regulation. Specifically, the subtle sensitivity of thiol reactivity to the environment makes the use of simulation techniques extremely valuable for obtaining microscopic insights. In this work we review the application of classical and quantum–mechanical atomistic simulation tools to the investigation of selected relevant issues in thiol redox biochemistry, such as investigations on (1) the protonation state of cysteine in protein, (2) two-electron oxidation of thiols by hydroperoxides, chloramines, and hypochlorous acid, (3) mechanistic and kinetics aspects of the de novo formation of disulfide bonds and thiol−disulfide exchange, (4) formation of sulfenamides, (5) formation of nitrosothiols and transnitrosation reactions, and (6) one-electron oxidation pathways.</description><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biological Techniques</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Cell Biology</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Nanotechnology</subject><subject>Review</subject><issn>1867-2450</issn><issn>1867-2469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNp9kF9PwyAUxYnRuDn9AL6YPvpSBQoFjDExi_-SJb7MZ0Ip3VjaMqE13beXZXPRFx-Am5xzz738ALhE8AZByG4DwpSiFKIsHszS4QiMEc9Zikkujg81hSNwFsIKwpxgTk_BKN5QiByPwf18aV2deFO6ISms00vT2ND5zV1i22AXyy4klXdNol2z7jvjk2CbvladdW04ByeVqoO52L8T8PH8NJ--prP3l7fp4yzVGWVDSjUpqyIrEOKCVVpUtEK0yEqK86IQiuaCEMJwjiFEXGWa8pJyzTJiuBK4yLIJeNjlrvuiMaU2bedVLdfeNspvpFNW_lVau5QL9yUpwYwjGAOu9wHeffYmdDJ-Upu6Vq1xfZBxMUEgw5hHK9pZtXcheFMdxiAot9TljrqM1OWWuhxiz9Xv_Q4dP5ijAe8MIUrtwni5cr1vI7N_Ur8BaxuO5w</recordid><startdate>201403</startdate><enddate>201403</enddate><creator>Zeida, Ari</creator><creator>Guardia, Carlos M.</creator><creator>Lichtig, Pablo</creator><creator>Perissinotti, Laura L.</creator><creator>Defelipe, Lucas A.</creator><creator>Turjanski, Adrián</creator><creator>Radi, Rafael</creator><creator>Trujillo, Madia</creator><creator>Estrin, Darío A.</creator><general>Springer Berlin Heidelberg</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201403</creationdate><title>Thiol redox biochemistry: insights from computer simulations</title><author>Zeida, Ari ; Guardia, Carlos M. ; Lichtig, Pablo ; Perissinotti, Laura L. ; Defelipe, Lucas A. ; Turjanski, Adrián ; Radi, Rafael ; Trujillo, Madia ; Estrin, Darío A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357x-5c4dfb3b11897fc9f5f15b3d526bb9a56944472620018a3c58d58c734e8a92b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biological Techniques</topic><topic>Biomedical and Life Sciences</topic><topic>Biophysics</topic><topic>Cell Biology</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Nanotechnology</topic><topic>Review</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zeida, Ari</creatorcontrib><creatorcontrib>Guardia, Carlos M.</creatorcontrib><creatorcontrib>Lichtig, Pablo</creatorcontrib><creatorcontrib>Perissinotti, Laura L.</creatorcontrib><creatorcontrib>Defelipe, Lucas A.</creatorcontrib><creatorcontrib>Turjanski, Adrián</creatorcontrib><creatorcontrib>Radi, Rafael</creatorcontrib><creatorcontrib>Trujillo, Madia</creatorcontrib><creatorcontrib>Estrin, Darío A.</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>Zeida, Ari</au><au>Guardia, Carlos M.</au><au>Lichtig, Pablo</au><au>Perissinotti, Laura L.</au><au>Defelipe, Lucas A.</au><au>Turjanski, Adrián</au><au>Radi, Rafael</au><au>Trujillo, Madia</au><au>Estrin, Darío A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thiol redox biochemistry: insights from computer simulations</atitle><jtitle>Biophysical reviews</jtitle><stitle>Biophys Rev</stitle><addtitle>Biophys Rev</addtitle><date>2014-03</date><risdate>2014</risdate><volume>6</volume><issue>1</issue><spage>27</spage><epage>46</epage><pages>27-46</pages><issn>1867-2450</issn><eissn>1867-2469</eissn><abstract>Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly due to the presence of low-molecular-weight thiols and cysteine residues in proteins involved in catalysis and regulation. 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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; SpringerLink Journals - AutoHoldings |
| subjects | Biochemistry Biological and Medical Physics Biological Techniques Biomedical and Life Sciences Biophysics Cell Biology Life Sciences Membrane Biology Nanotechnology Review |
| title | Thiol redox biochemistry: insights from computer simulations |
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