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| Hauptseite > Publikationsdatenbank > Functional vibrational spectroscopy of a cytochrome c monolayer: SEIDAS probes the interaction with different surface modified electrodes > print |
| Hauptseite > Publikationsdatenbank > Functional vibrational spectroscopy of a cytochrome c monolayer: SEIDAS probes the interaction with different surface modified electrodes > print |
| 001 | 41691 | ||
| 005 | 20200423203925.0 | ||
| 024 | 7 | _ | |a pmid:15281838 |2 pmid |
| 024 | 7 | _ | |a 10.1021/ja048346n |2 DOI |
| 024 | 7 | _ | |a WOS:000222950900057 |2 WOS |
| 024 | 7 | _ | |a 2128/698 |2 Handle |
| 037 | _ | _ | |a PreJuSER-41691 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Chemistry, Multidisciplinary |
| 100 | 1 | _ | |a Ataka, K. |b 0 |u FZJ |0 P:(DE-Juel1)VDB5396 |
| 245 | _ | _ | |a Functional vibrational spectroscopy of a cytochrome c monolayer: SEIDAS probes the interaction with different surface modified electrodes |
| 260 | _ | _ | |a Washington, DC |b American Chemical Society |c 2004 |
| 300 | _ | _ | |a 9445 - 9457 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |a Journal of the American Chemical Society |x 0002-7863 |0 8502 |v 126 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Electrochemically induced infrared difference spectra of cytochrome c on various chemically modified electrodes (CMEs) are recorded by exploiting the surface-enhancement exerted by a granular gold film. We have recently developed surface-enhanced infrared difference absorption spectroscopy (SEIDAS), which provides acute sensitivity to observe the minute enzymatic change of a protein on the level of a monolayer. By these means, we demonstrate that the relative band intensities in the potential-induced difference spectra of adsorbed cytochrome c are significantly dependent on the type of CME used (mercaptopropionic acid, mercaptoethanol, 4,4'-dithiodipyridine, or L-cysteine). These differences are attributed to the altered interaction of cytochrome c with the headgroup of the various CMEs leading to variations in surface orientation and relative distance from the surface. Nevertheless, the peak positions of the observed bands are identical among the CMEs employed. This implies that the internal conformational changes induced by the redox reaction of the adsorbed cytochrome c are not disturbed by the interaction with the CME and that full functionality of the protein is retained. Finally, we critically discuss our results within the framework of the different models for cytochrome c adsorption on CMEs. |
| 536 | _ | _ | |a Neurowissenschaften |c L01 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK255 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Cytochromes c: chemistry |
| 650 | _ | 2 | |2 MeSH |a Electrochemistry: instrumentation |
| 650 | _ | 2 | |2 MeSH |a Electrochemistry: methods |
| 650 | _ | 2 | |2 MeSH |a Electrodes |
| 650 | _ | 2 | |2 MeSH |a Gold: chemistry |
| 650 | _ | 2 | |2 MeSH |a Nuclear Magnetic Resonance, Biomolecular |
| 650 | _ | 2 | |2 MeSH |a Oxidation-Reduction |
| 650 | _ | 2 | |2 MeSH |a Spectroscopy, Fourier Transform Infrared: instrumentation |
| 650 | _ | 2 | |2 MeSH |a Spectroscopy, Fourier Transform Infrared: methods |
| 650 | _ | 7 | |0 7440-57-5 |2 NLM Chemicals |a Gold |
| 650 | _ | 7 | |0 9007-43-6 |2 NLM Chemicals |a Cytochromes c |
| 650 | _ | 7 | |a J |2 WoSType |
| 700 | 1 | _ | |a Heberle, J. |b 1 |u FZJ |0 P:(DE-Juel1)VDB572 |
| 773 | _ | _ | |a 10.1021/ja048346n |g Vol. 126, p. 9445 - 9457 |p 9445 - 9457 |q 126<9445 - 9457 |0 PERI:(DE-600)1472210-0 |t Journal of the American Chemical Society |v 126 |y 2004 |x 0002-7863 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1021/ja048346n |u http://hdl.handle.net/2128/698 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/41691/files/57707.pdf |y OpenAccess |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/41691/files/57707.jpg?subformat=icon-1440 |x icon-1440 |y OpenAccess |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/41691/files/57707.jpg?subformat=icon-180 |x icon-180 |y OpenAccess |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/41691/files/57707.jpg?subformat=icon-640 |x icon-640 |y OpenAccess |
| 909 | C | O | |o oai:juser.fz-juelich.de:41691 |p openaire |p open_access |p driver |p VDB |p dnbdelivery |
| 913 | 1 | _ | |k L01 |v Neurowissenschaften |l Funktion und Dysfunktion des Nervensystems |b Leben |0 G:(DE-Juel1)FUEK255 |x 0 |
| 914 | 1 | _ | |y 2004 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 915 | _ | _ | |2 StatID |0 StatID:(DE-HGF)0510 |a OpenAccess |
| 920 | 1 | _ | |k IBI-2 |l Biologische Strukturforschung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB58 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)57707 |
| 980 | 1 | _ | |a FullTexts |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a JUWEL |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
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