guest ::
| Home > Publications database > Long distance electron transfer in cytochrome c oxidase immobilised on electrodes. A surface enhanced resonance Raman spectroscopic study > print |
| Home > Publications database > Long distance electron transfer in cytochrome c oxidase immobilised on electrodes. A surface enhanced resonance Raman spectroscopic study > print |
| 001 | 51336 | ||
| 005 | 20200423204330.0 | ||
| 024 | 7 | _ | |a pmid:16482317 |2 pmid |
| 024 | 7 | _ | |a 10.1039/b513379n |2 DOI |
| 024 | 7 | _ | |a WOS:000235608500011 |2 WOS |
| 024 | 7 | _ | |a 1463-9076 |2 ISSN |
| 024 | 7 | _ | |a 2128/713 |2 Handle |
| 037 | _ | _ | |a PreJuSER-51336 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Chemistry, Physical |
| 084 | _ | _ | |2 WoS |a Physics, Atomic, Molecular & Chemical |
| 100 | 1 | _ | |a Hrabakova, J. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a Long distance electron transfer in cytochrome c oxidase immobilised on electrodes. A surface enhanced resonance Raman spectroscopic study |
| 260 | _ | _ | |c 2006 |a Cambridge |b RSC Publ. |
| 300 | _ | _ | |a 759 - 766 |
| 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 Physical Chemistry Chemical Physics |x 1463-9076 |0 4916 |v 8 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Cytochrome c oxidase was tethered to a functionalised Ag electrode via a histidine-tag on the C-terminus of subunit I or II and embedded in a phospholipid bilayer. The uniformly oriented membrane-bound proteins were studied by surface enhanced resonance Raman spectroscopy (SERRS) that reveals preservation of the native structures of the heme a and heme a(3) sites. On the basis of time-dependent SERRS measurements, the rate constant for the heterogeneous electron transfer to heme a was determined to be 0.002 s(-1) independent of the enzyme orientation and the overpotential. Taking into account that the electrode-to-heme a distance is larger than 50 A, these findings suggest an electron hopping mechanism in which the Cu(A) center is not involved. Electrochemical reduction is restricted to heme a whereas electron transfer from heme a to heme a(3), which in solution occurs on the nanosecond time scale, is drastically slowed down. It may be that the network of cooperativities that links intramolecular electron transfer and proton translocation is perturbed in the immobilised enzyme, possibly due to the effect of the interfacial electric field. |
| 536 | _ | _ | |a Funktion und Dysfunktion des Nervensystems |c P33 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK409 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Chemistry, Physical |
| 650 | _ | 2 | |2 MeSH |a Electrodes |
| 650 | _ | 2 | |2 MeSH |a Electron Transport Complex IV: chemistry |
| 650 | _ | 2 | |2 MeSH |a Enzymes, Immobilized: chemistry |
| 650 | _ | 2 | |2 MeSH |a Models, Chemical |
| 650 | _ | 2 | |2 MeSH |a Oxidation-Reduction |
| 650 | _ | 2 | |2 MeSH |a Physicochemical Phenomena |
| 650 | _ | 2 | |2 MeSH |a Silver: chemistry |
| 650 | _ | 2 | |2 MeSH |a Spectrum Analysis, Raman: methods |
| 650 | _ | 2 | |2 MeSH |a Surface Properties |
| 650 | _ | 2 | |2 MeSH |a Time Factors |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Enzymes, Immobilized |
| 650 | _ | 7 | |0 7440-22-4 |2 NLM Chemicals |a Silver |
| 650 | _ | 7 | |0 EC 1.9.3.1 |2 NLM Chemicals |a Electron Transport Complex IV |
| 650 | _ | 7 | |a J |2 WoSType |
| 700 | 1 | _ | |a Ataka, K. |b 1 |u FZJ |0 P:(DE-Juel1)VDB5396 |
| 700 | 1 | _ | |a Heberle, J. |b 2 |u FZJ |0 P:(DE-Juel1)VDB572 |
| 700 | 1 | _ | |a Hildebrandt, P. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Murgida, D. |b 4 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |0 PERI:(DE-600)1476244-4 |a 10.1039/b513379n |g Vol. 8, p. 759 - 766 |p 759 - 766 |q 8<759 - 766 |t Physical Chemistry Chemical Physics |v 8 |x 1463-9076 |y 2006 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1039/b513379n |u http://hdl.handle.net/2128/713 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/51336/files/80532.pdf |y OpenAccess |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/51336/files/80532.jpg?subformat=icon-1440 |x icon-1440 |y OpenAccess |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/51336/files/80532.jpg?subformat=icon-180 |x icon-180 |y OpenAccess |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/51336/files/80532.jpg?subformat=icon-640 |x icon-640 |y OpenAccess |
| 909 | C | O | |o oai:juser.fz-juelich.de:51336 |p openaire |p open_access |p driver |p VDB |p dnbdelivery |
| 913 | 1 | _ | |k P33 |v Funktion und Dysfunktion des Nervensystems |l Funktion und Dysfunktion des Nervensystems |b Gesundheit |0 G:(DE-Juel1)FUEK409 |x 0 |
| 914 | 1 | _ | |y 2006 |
| 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)80532 |
| 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 |
| 980 | _ | _ | |a FullTexts |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|