Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins

The tunneling pathway model for electron transfer, which accounts for the unique covalent, hydrogen-bonded, and van der Waals contact linking donor and acceptor in a protein, gives a consistent description of electron-transfer rates in ruthenated proteins (cytochrome c, myogloblin, and cytochrome b{...

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Veröffentlicht in:	Journal of Physical Chemistry 1992-04, Vol.96 (7), p.2852-2855
Hauptverfasser:	Beratan, David N, Betts, Jonathan N, Onuchic, Jose Nelson
Format:	Artikel
Sprache:	eng
Schlagworte:	40 CHEMISTRY BIOLOGY AND MEDICINE, BASIC STUDIES ELECTRON TRANSFER MATHEMATICAL MODELS PROTEINS TUNNELING VALENCE
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container_title	Journal of Physical Chemistry
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creator	Beratan, David N Betts, Jonathan N Onuchic, Jose Nelson
description	The tunneling pathway model for electron transfer, which accounts for the unique covalent, hydrogen-bonded, and van der Waals contact linking donor and acceptor in a protein, gives a consistent description of electron-transfer rates in ruthenated proteins (cytochrome c, myogloblin, and cytochrome b{sub 5}), while simpler exponential decay models are not fully adequate. The authors report several new testable predictions of the pathway model relating electron-transfer rates to protein structure. The analysis predicts qualitative differences in the distance dependence of protein electron transfer at short (
doi_str_mv	10.1021/j100186a014
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The authors report several new testable predictions of the pathway model relating electron-transfer rates to protein structure. The analysis predicts qualitative differences in the distance dependence of protein electron transfer at short (<5{angstrom}) vs long distance, differences in the nature of the coupling through {alpha}-helix vs {beta}-sheet, and the possibility of switching electronic coupling upon oxidation/reduction or ligation/deligation in metalloproteins. 16 refs., 3 figs.</description><identifier>ISSN: 0022-3654</identifier><identifier>EISSN: 1541-5740</identifier><identifier>DOI: 10.1021/j100186a014</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>40 CHEMISTRY ; BIOLOGY AND MEDICINE, BASIC STUDIES ; ELECTRON TRANSFER ; MATHEMATICAL MODELS ; PROTEINS ; TUNNELING ; VALENCE</subject><ispartof>Journal of Physical Chemistry, 1992-04, Vol.96 (7), p.2852-2855</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a393t-8c1743cbc8646a2437b7b952f7227cf6486bf6757e54b932fc7474c4ce9dd45d3</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/j100186a014$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/j100186a014$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,881,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/263813$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Beratan, David N</creatorcontrib><creatorcontrib>Betts, Jonathan N</creatorcontrib><creatorcontrib>Onuchic, Jose Nelson</creatorcontrib><title>Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins</title><title>Journal of Physical Chemistry</title><addtitle>J. Phys. Chem</addtitle><description>The tunneling pathway model for electron transfer, which accounts for the unique covalent, hydrogen-bonded, and van der Waals contact linking donor and acceptor in a protein, gives a consistent description of electron-transfer rates in ruthenated proteins (cytochrome c, myogloblin, and cytochrome b{sub 5}), while simpler exponential decay models are not fully adequate. The authors report several new testable predictions of the pathway model relating electron-transfer rates to protein structure. The analysis predicts qualitative differences in the distance dependence of protein electron transfer at short (<5{angstrom}) vs long distance, differences in the nature of the coupling through {alpha}-helix vs {beta}-sheet, and the possibility of switching electronic coupling upon oxidation/reduction or ligation/deligation in metalloproteins. 16 refs., 3 figs.</description><subject>40 CHEMISTRY</subject><subject>BIOLOGY AND MEDICINE, BASIC STUDIES</subject><subject>ELECTRON TRANSFER</subject><subject>MATHEMATICAL MODELS</subject><subject>PROTEINS</subject><subject>TUNNELING</subject><subject>VALENCE</subject><issn>0022-3654</issn><issn>1541-5740</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNpt0EtPGzEUBWALgUQIrPgD7opFNa1fY0-WKOJREakIwtryXN8Bh9Qzsh2R_HsGBaEuWN3Nd650DiHnnP3iTPDfK84Yb7RjXB2QCa8Vr2qj2CGZMCZEJXWtjslJzis2Oin5hLwtNzHiOsRnOrjy8uZ21EVPE_p-W-XiClYeB4weY6G4RiipjwEo9JvhI5WpKzSiS-sd7cIWPfVhjEVAGuJXgJbkYu4w0SH1BUPMp-Soc-uMZ593Sp6ur5bz22rx9-bP_HJROTmTpWqAGyWhhUYr7YSSpjXtrBadEcJAp1Wj206b2mCt2pkUHRhlFCjAmfeq9nJKfuz_9rkEmyEUhBfox85QrNCyGWeYkp97A6nPOWFnhxT-ubSznNmPXe1_u4662uuxJ26_qEuvVhtparu8f7TyccEEu5vbh9Ff7L2DbFf9JsWx77ef3wH7tYfs</recordid><startdate>199204</startdate><enddate>199204</enddate><creator>Beratan, David N</creator><creator>Betts, Jonathan N</creator><creator>Onuchic, Jose Nelson</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>OTOTI</scope></search><sort><creationdate>199204</creationdate><title>Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins</title><author>Beratan, David N ; Betts, Jonathan N ; Onuchic, Jose Nelson</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a393t-8c1743cbc8646a2437b7b952f7227cf6486bf6757e54b932fc7474c4ce9dd45d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>40 CHEMISTRY</topic><topic>BIOLOGY AND MEDICINE, BASIC STUDIES</topic><topic>ELECTRON TRANSFER</topic><topic>MATHEMATICAL MODELS</topic><topic>PROTEINS</topic><topic>TUNNELING</topic><topic>VALENCE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Beratan, David N</creatorcontrib><creatorcontrib>Betts, Jonathan N</creatorcontrib><creatorcontrib>Onuchic, Jose Nelson</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>OSTI.GOV</collection><jtitle>Journal of Physical Chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Beratan, David N</au><au>Betts, Jonathan N</au><au>Onuchic, Jose Nelson</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins</atitle><jtitle>Journal of Physical Chemistry</jtitle><addtitle>J. Phys. Chem</addtitle><date>1992-04</date><risdate>1992</risdate><volume>96</volume><issue>7</issue><spage>2852</spage><epage>2855</epage><pages>2852-2855</pages><issn>0022-3654</issn><eissn>1541-5740</eissn><abstract>The tunneling pathway model for electron transfer, which accounts for the unique covalent, hydrogen-bonded, and van der Waals contact linking donor and acceptor in a protein, gives a consistent description of electron-transfer rates in ruthenated proteins (cytochrome c, myogloblin, and cytochrome b{sub 5}), while simpler exponential decay models are not fully adequate. The authors report several new testable predictions of the pathway model relating electron-transfer rates to protein structure. The analysis predicts qualitative differences in the distance dependence of protein electron transfer at short (<5{angstrom}) vs long distance, differences in the nature of the coupling through {alpha}-helix vs {beta}-sheet, and the possibility of switching electronic coupling upon oxidation/reduction or ligation/deligation in metalloproteins. 16 refs., 3 figs.</abstract><cop>United States</cop><pub>American Chemical Society</pub><doi>10.1021/j100186a014</doi><tpages>4</tpages></addata></record>
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subjects	40 CHEMISTRY BIOLOGY AND MEDICINE, BASIC STUDIES ELECTRON TRANSFER MATHEMATICAL MODELS PROTEINS TUNNELING VALENCE
title	Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins
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