Hauptseite > Publikationsdatenbank > Orientational control on the physiological reaction of cytochrome c oxidase tethered to a gold electrode > print

001     51339
005     20200423204330.0
024 7 _ |a pmid:16671753
|2 pmid
024 7 _ |a 10.1021/jp0534131
|2 DOI
024 7 _ |a WOS:000237451300063
|2 WOS
024 7 _ |a 2128/715
|2 Handle
037 _ _ |a PreJuSER-51339
041 _ _ |a eng
082 _ _ |a 530
084 _ _ |2 WoS
|a Chemistry, Physical
100 1 _ |a Ataka, K.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Orientational control on the physiological reaction of cytochrome c oxidase tethered to a gold electrode
260 _ _ |a Washington, DC
|b Soc.
|c 2006
300 _ _ |a 9339 - 9347
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 Physical Chemistry B
|x 1520-6106
|0 3694
|v 110
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The physiological reaction of a membrane protein is reconstituted on a solid-supported electrode by orientational control via the position of an affinity tag. Recombinant cytochrome c oxidase (CcO) from Rhodobacter sphaeroides is immobilized on a chemically modified gold surface via the affinity of a histidine tag (His-tag) to a nickel chelating nitrilotriacetic acid surface. Control of the orientation is achieved by the adsorption of CcO through the His-tag engineered into the two opposite sites of the membrane protein surface. After reconstitution into a lipid layer, the functionality of this enzyme film electrode is probed by surface-enhanced infrared absorption spectroscopy and cyclic voltammetry. We demonstrate that cytochrome c (Cc) binds and initiates the catalytic reaction of CcO only when the latter is orientated with subunit II facing the bulk aqueous phase while Cc does not interact with the oppositely orientated CcO. We infer from the observed catalytic dioxygen reduction at potentials below 240 mV (vs a normal hydrogen electrode) that reduced Cc mediates electron input into CcO in a way similar to the physiological pathway. The quantitative analysis of the IR spectra indicates the presence of an inactive population of Cc bound to CcO at equal amounts as the redox-active population. This methodological approach demonstrates that the orientation of the membrane protein can be controlled depending on the position of the affinity tag. The approach is considered to be of general applicability as the introduction of affinity tags is routine in current biochemistry.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
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|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Adsorption
650 _ 2 |2 MeSH
|a Electrochemistry
650 _ 2 |2 MeSH
|a Electrodes
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: chemistry
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: isolation & purification
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: physiology
650 _ 2 |2 MeSH
|a Enzymes, Immobilized: chemistry
650 _ 2 |2 MeSH
|a Gold: chemistry
650 _ 2 |2 MeSH
|a Kinetics
650 _ 2 |2 MeSH
|a Membranes, Artificial
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Rhodobacter sphaeroides: chemistry
650 _ 2 |2 MeSH
|a Spectroscopy, Fourier Transform Infrared
650 _ 2 |2 MeSH
|a Surface Properties
650 _ 7 |0 0
|2 NLM Chemicals
|a Enzymes, Immobilized
650 _ 7 |0 0
|2 NLM Chemicals
|a Membranes, Artificial
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |0 7440-57-5
|2 NLM Chemicals
|a Gold
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 Richter, B.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Heberle, J.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB572
773 _ _ |a 10.1021/jp0534131
|g Vol. 110, p. 9339 - 9347
|p 9339 - 9347
|q 110<9339 - 9347
|0 PERI:(DE-600)2006039-7
|t The @journal of physical chemistry / B
|v 110
|y 2006
|x 1520-6106
856 7 _ |u http://dx.doi.org/10.1021/jp0534131
|u http://hdl.handle.net/2128/715
856 4 _ |u https://juser.fz-juelich.de/record/51339/files/80535.pdf
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913 1 _ |k P33
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914 1 _ |y 2006
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920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
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