Pulse EPR, ENDOR, and ELDOR Study of Anionic Flavin Radicals in Na+-Translocating NADH:Quinone Oxidoreductase
The Na + -translocating nicotinamide adenine dinucleotide (NADH):quinine oxidoreductase (Na + –NQR) is a component of respiratory chain of various bacteria and it generates a redox-driven transmembrane electrochemical Na + potential. It contains four different flavin prosthetic groups, including two...
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| Veröffentlicht in: | Applied magnetic resonance 2010, Vol.37 (1-4), p.353-361 |
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| creator | Kulik, Leonid V. Pivtsov, Andrey V. Bogachev, Alexander V. |
| description | The Na
+
-translocating nicotinamide adenine dinucleotide (NADH):quinine oxidoreductase (Na
+
–NQR) is a component of respiratory chain of various bacteria and it generates a redox-driven transmembrane electrochemical Na
+
potential. It contains four different flavin prosthetic groups, including two flavin mononucleotide (FMN) residues covalently bound to the subunits NqrB and NqrC. Na
+
–NQR from
Vibrio harveyi
was poised at different redox potentials to prepare two samples, containing either both FMN
NqrB
and FMN
NqrC
or only FMN
NqrB
in a paramagnetic state. These two samples were comparatively studied using pulse electron paramagnetic resonance (EPR), electron-nuclear double resonance (ENDOR), and electron-electron double resonance (ELDOR) spectroscopy. The echo-detected EPR spectra and electron spin relaxation properties were very similar for flavin radicals in both samples. The splitting of the outer peaks in the proton ENDOR spectra, assigned to the C(8α) methyl protons, allows to identify both radicals as anionic flavosemiquinones. The mean interspin distance of 20.7 Å between these radicals was determined by pulse ELDOR experiment, which allows to estimate the edge-to-edge distance (
r
e
) between these flavin centers as: 11.7 Å |
| doi_str_mv | 10.1007/s00723-009-0075-6 |
| format | Article |
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+
-translocating nicotinamide adenine dinucleotide (NADH):quinine oxidoreductase (Na
+
–NQR) is a component of respiratory chain of various bacteria and it generates a redox-driven transmembrane electrochemical Na
+
potential. It contains four different flavin prosthetic groups, including two flavin mononucleotide (FMN) residues covalently bound to the subunits NqrB and NqrC. Na
+
–NQR from
Vibrio harveyi
was poised at different redox potentials to prepare two samples, containing either both FMN
NqrB
and FMN
NqrC
or only FMN
NqrB
in a paramagnetic state. These two samples were comparatively studied using pulse electron paramagnetic resonance (EPR), electron-nuclear double resonance (ENDOR), and electron-electron double resonance (ELDOR) spectroscopy. The echo-detected EPR spectra and electron spin relaxation properties were very similar for flavin radicals in both samples. The splitting of the outer peaks in the proton ENDOR spectra, assigned to the C(8α) methyl protons, allows to identify both radicals as anionic flavosemiquinones. The mean interspin distance of 20.7 Å between these radicals was determined by pulse ELDOR experiment, which allows to estimate the edge-to-edge distance (
r
e
) between these flavin centers as: 11.7 Å <
r
e
< 20.7 Å. The direct electron transfer between FMN
NqrB
and FMN
NqrC
during the physiological turnover of the Na
+
–NQR complex is suggested.</description><identifier>ISSN: 0937-9347</identifier><identifier>EISSN: 1613-7507</identifier><identifier>DOI: 10.1007/s00723-009-0075-6</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Acids ; Adenine ; Atoms and Molecules in Strong Fields ; Electron paramagnetic resonance ; Electron spin ; Electron transfer ; Electrons ; Enzymes ; Experiments ; Fourier transforms ; Laser Matter Interaction ; Nicotinamide ; Nicotinamide adenine dinucleotide ; Organic Chemistry ; Physical Chemistry ; Physics ; Physics and Astronomy ; Prostheses ; Proteins ; Protons ; Quinones ; Solid State Physics ; Spectra ; Spectroscopy/Spectrometry ; Spectrum analysis ; Vitamin B</subject><ispartof>Applied magnetic resonance, 2010, Vol.37 (1-4), p.353-361</ispartof><rights>Springer 2009</rights><rights>Springer 2009.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c316t-f4a7d14632ee951f14f37ec9ce8531cae08c657d2e36589883a77fda95cc7c6d3</citedby><cites>FETCH-LOGICAL-c316t-f4a7d14632ee951f14f37ec9ce8531cae08c657d2e36589883a77fda95cc7c6d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00723-009-0075-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2918001434?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,21387,21388,21389,21390,23255,27923,27924,33529,33702,33743,34004,34313,41487,42556,43658,43786,43804,43952,44066,51318,64384,64388,72240</link.rule.ids></links><search><creatorcontrib>Kulik, Leonid V.</creatorcontrib><creatorcontrib>Pivtsov, Andrey V.</creatorcontrib><creatorcontrib>Bogachev, Alexander V.</creatorcontrib><title>Pulse EPR, ENDOR, and ELDOR Study of Anionic Flavin Radicals in Na+-Translocating NADH:Quinone Oxidoreductase</title><title>Applied magnetic resonance</title><addtitle>Appl Magn Reson</addtitle><description>The Na
+
-translocating nicotinamide adenine dinucleotide (NADH):quinine oxidoreductase (Na
+
–NQR) is a component of respiratory chain of various bacteria and it generates a redox-driven transmembrane electrochemical Na
+
potential. It contains four different flavin prosthetic groups, including two flavin mononucleotide (FMN) residues covalently bound to the subunits NqrB and NqrC. Na
+
–NQR from
Vibrio harveyi
was poised at different redox potentials to prepare two samples, containing either both FMN
NqrB
and FMN
NqrC
or only FMN
NqrB
in a paramagnetic state. These two samples were comparatively studied using pulse electron paramagnetic resonance (EPR), electron-nuclear double resonance (ENDOR), and electron-electron double resonance (ELDOR) spectroscopy. The echo-detected EPR spectra and electron spin relaxation properties were very similar for flavin radicals in both samples. The splitting of the outer peaks in the proton ENDOR spectra, assigned to the C(8α) methyl protons, allows to identify both radicals as anionic flavosemiquinones. The mean interspin distance of 20.7 Å between these radicals was determined by pulse ELDOR experiment, which allows to estimate the edge-to-edge distance (
r
e
) between these flavin centers as: 11.7 Å <
r
e
< 20.7 Å. The direct electron transfer between FMN
NqrB
and FMN
NqrC
during the physiological turnover of the Na
+
–NQR complex is suggested.</description><subject>Acids</subject><subject>Adenine</subject><subject>Atoms and Molecules in Strong Fields</subject><subject>Electron paramagnetic resonance</subject><subject>Electron spin</subject><subject>Electron transfer</subject><subject>Electrons</subject><subject>Enzymes</subject><subject>Experiments</subject><subject>Fourier transforms</subject><subject>Laser Matter Interaction</subject><subject>Nicotinamide</subject><subject>Nicotinamide adenine dinucleotide</subject><subject>Organic Chemistry</subject><subject>Physical Chemistry</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Prostheses</subject><subject>Proteins</subject><subject>Protons</subject><subject>Quinones</subject><subject>Solid State Physics</subject><subject>Spectra</subject><subject>Spectroscopy/Spectrometry</subject><subject>Spectrum analysis</subject><subject>Vitamin B</subject><issn>0937-9347</issn><issn>1613-7507</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1ULFOwzAUtBBIlMIHsFliBIMdx3HMVrUpRaraUspsWbZTpUqdYieI_j2ugsTE8N7dcHdP7wC4JfiRYMyfQlwJRRiLOJyh7AwMSEYo4gzzczDAgnIkaMovwVUIO4wJywkfgP2qq4OFxWr9AIvFZBlBOQOLeaTwve3METYlHLmqcZWG01p9VQ6ulam0qgOMfKHu0cYrF-pGq7ZyW7gYTWbPb13lGmfh8rsyjbem060K9hpclNFnb35xCD6mxWY8Q_Ply-t4NEeakqxFZaq4IWlGE2sFIyVJS8qtFtrmjBKtLM51xrhJLM1YLvKcKs5LowTTmuvM0CG463MPvvnsbGjlrum8iydlIkgev09pGlWkV2nfhOBtKQ--2it_lATLU6uyb1XGVuWpVZlFT9J7QtS6rfV_yf-bfgCyw3gj</recordid><startdate>2010</startdate><enddate>2010</enddate><creator>Kulik, Leonid V.</creator><creator>Pivtsov, Andrey V.</creator><creator>Bogachev, Alexander V.</creator><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7XB</scope><scope>88I</scope><scope>8FE</scope><scope>8FG</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>KB.</scope><scope>M2P</scope><scope>P5Z</scope><scope>P62</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>2010</creationdate><title>Pulse EPR, ENDOR, and ELDOR Study of Anionic Flavin Radicals in Na+-Translocating NADH:Quinone Oxidoreductase</title><author>Kulik, Leonid V. ; Pivtsov, Andrey V. ; Bogachev, Alexander V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c316t-f4a7d14632ee951f14f37ec9ce8531cae08c657d2e36589883a77fda95cc7c6d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Acids</topic><topic>Adenine</topic><topic>Atoms and Molecules in Strong Fields</topic><topic>Electron paramagnetic resonance</topic><topic>Electron spin</topic><topic>Electron transfer</topic><topic>Electrons</topic><topic>Enzymes</topic><topic>Experiments</topic><topic>Fourier transforms</topic><topic>Laser Matter Interaction</topic><topic>Nicotinamide</topic><topic>Nicotinamide adenine dinucleotide</topic><topic>Organic Chemistry</topic><topic>Physical Chemistry</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Prostheses</topic><topic>Proteins</topic><topic>Protons</topic><topic>Quinones</topic><topic>Solid State Physics</topic><topic>Spectra</topic><topic>Spectroscopy/Spectrometry</topic><topic>Spectrum analysis</topic><topic>Vitamin B</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kulik, Leonid V.</creatorcontrib><creatorcontrib>Pivtsov, Andrey V.</creatorcontrib><creatorcontrib>Bogachev, Alexander V.</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>Materials Science Database</collection><collection>Science Database</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Applied magnetic resonance</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kulik, Leonid V.</au><au>Pivtsov, Andrey V.</au><au>Bogachev, Alexander V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pulse EPR, ENDOR, and ELDOR Study of Anionic Flavin Radicals in Na+-Translocating NADH:Quinone Oxidoreductase</atitle><jtitle>Applied magnetic resonance</jtitle><stitle>Appl Magn Reson</stitle><date>2010</date><risdate>2010</risdate><volume>37</volume><issue>1-4</issue><spage>353</spage><epage>361</epage><pages>353-361</pages><issn>0937-9347</issn><eissn>1613-7507</eissn><abstract>The Na
+
-translocating nicotinamide adenine dinucleotide (NADH):quinine oxidoreductase (Na
+
–NQR) is a component of respiratory chain of various bacteria and it generates a redox-driven transmembrane electrochemical Na
+
potential. It contains four different flavin prosthetic groups, including two flavin mononucleotide (FMN) residues covalently bound to the subunits NqrB and NqrC. Na
+
–NQR from
Vibrio harveyi
was poised at different redox potentials to prepare two samples, containing either both FMN
NqrB
and FMN
NqrC
or only FMN
NqrB
in a paramagnetic state. These two samples were comparatively studied using pulse electron paramagnetic resonance (EPR), electron-nuclear double resonance (ENDOR), and electron-electron double resonance (ELDOR) spectroscopy. The echo-detected EPR spectra and electron spin relaxation properties were very similar for flavin radicals in both samples. The splitting of the outer peaks in the proton ENDOR spectra, assigned to the C(8α) methyl protons, allows to identify both radicals as anionic flavosemiquinones. The mean interspin distance of 20.7 Å between these radicals was determined by pulse ELDOR experiment, which allows to estimate the edge-to-edge distance (
r
e
) between these flavin centers as: 11.7 Å <
r
e
< 20.7 Å. The direct electron transfer between FMN
NqrB
and FMN
NqrC
during the physiological turnover of the Na
+
–NQR complex is suggested.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><doi>10.1007/s00723-009-0075-6</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Applied magnetic resonance, 2010, Vol.37 (1-4), p.353-361 |
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| language | eng |
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| source | ProQuest Central Essentials; ProQuest Central (Alumni Edition); ProQuest Central Student; ProQuest Central Korea; ProQuest Central UK/Ireland; SpringerLink Journals - AutoHoldings; ProQuest Central |
| subjects | Acids Adenine Atoms and Molecules in Strong Fields Electron paramagnetic resonance Electron spin Electron transfer Electrons Enzymes Experiments Fourier transforms Laser Matter Interaction Nicotinamide Nicotinamide adenine dinucleotide Organic Chemistry Physical Chemistry Physics Physics and Astronomy Prostheses Proteins Protons Quinones Solid State Physics Spectra Spectroscopy/Spectrometry Spectrum analysis Vitamin B |
| title | Pulse EPR, ENDOR, and ELDOR Study of Anionic Flavin Radicals in Na+-Translocating NADH:Quinone Oxidoreductase |
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