Chiral Recognition in Mediated Electron Transfer in Redox Proteins

Marx–Tibbon, Sharon; Katz, Eugenii; Willner, Itamar

doi:10.1021/ja00144a025

Cited by 29 publications

(23 citation statements)

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“…[185] The chiral electron relays (S)-or (R)-N,Ndimethyl-1-ferrocenyl-ethylamine [(S)-or (R)-(Fc)] were reported to stimulate chiroselective bioelectrocatalyzed oxidation of glucose in the presence of glucose oxidase, [185a] whereby the oxidation in the presence of (S)-(Fc) was double that in the presence of (R)-(Fc). Kinetic analysis of the bioelectrocatalyzed oxidation of glucose by the two enantiomeric electron relays suggests that the protein induces chiral discrimination through diastereoisomeric interaction with the penetration ± dissociation routes of the electron mediator, to and from the biocatalyst.…”

Section: Electron Transfer In Layered Enzyme Electrode Assembliesmentioning

confidence: 99%

Integration of Layered Redox Proteins and Conductive Supports for Bioelectronic Applications

Willner

Katz

2000

Angew. Chem. Int. Ed.

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977

598

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Integration of redox enzymes with an electrode support and formation of an electrical contact between the biocatalysts and the electrode is the fundamental subject of bioelectronics and optobioelectronics. This review addresses the recent advances and the scientific progress in electrically contacted, layered enzyme electrodes, and discusses the future applications of the systems in various bioelectronic devices, for example, amperometric biosensors, sensoric arrays, logic gates, and optical memories. This review presents the methods for the immobilization of redox enzymes on electrodes and discusses the covalent linkage of proteins, the use of supramolecular affinity complexes, and the reconstitution of apo-redox enzymes for the nanoengineering of electrodes with protein monolayers of electrodes with protein monolayers and multilayers. Electrical contact in the layered enzyme electrode is achieved by the application of diffusional electron mediators, such as ferrocene derivatives, ferricyanide, quinones, and bipyridinium salts. Covalent tethering of electron relay units to layered enzyme electrodes, the cross-linking of affinity complexes formed between redox proteins and electrodes functionalized with relay-cofactor units, or surface reconstitution of apo-enzymes on relay-cofactor-functionalized electrodes yield bioelectrocatalytic electrodes. The application of the functionalized electrodes as biosensor devices is addressed and further application of electrically "wired" enzymes as catalytic interfaces in biofuel cells is discussed. The organization of sensor arrays, self-calibrated biosensors, or gated bioelectronic devices requires the microstructuring of biomaterials on solid supports in the form of ordered micro-patterns. For example, light-sensitive layers composed of azides, benzophenone, or diazine derivatives associated with solid supports can be irradiated through masks to enable the patterned covalent linkage of biomaterials to surfaces. Alternatively, patterning of biomaterials can be accomplished by noncovalent interactions (such as in affinity complexes between avidin and a photolabeled biotin, or between an antibody and a photoisomerizable antigen layer) to provide a means of organizing protein microstructures on surfaces. The organization of patterned hydrophilic/hydrophobic domains on surfaces, by using photolithography, stamping, or micromachining methods, allows the selective patterning of surfaces by hydrophobic, noncovalent interactions. Photoactivated layered enzyme electrodes act as light-switchable optobioelectronic systems for the amperometric transduction of recorded photonic information. These systems can act as optical memories, biomolecular amplifiers, or logic gates. The photoswitchable enzyme electrodes are generated by the tethering of photoisomerizable groups to the protein, the reconstitution of apo-enzymes with semisynthetic photoisomerizable cofactor units, or the coupling of photoisomerizable electron relay units.

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Section: Electron Transfer In Layered Enzyme Electrode Assembliesmentioning

confidence: 99%

Integration of Layered Redox Proteins and Conductive Supports for Bioelectronic Applications

Willner

Katz

2000

Angew. Chem. Int. Ed.

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977

598

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“…[168] Als leitendes Material wurden Ruû, [156] Pyrolysegraphit, [169] platinierte Kohlenstoffpartikel [170] und kolloidales Gold [171] verwendet, und Kohlenstoffpaste [172] Chiroselektiver MET wurde in einer Reihe von Untersuchungen mit diffundierenden, chiralen Elektronenvermittlern behandelt. [185] So stimulieren die chiralen Verbindungen (S)-Fc etwa doppelt so wirksam ist wie (R)-Fc. Die kinetische Analyse der beiden Glucose-Oxidationen lässt darauf schlieûen, dass das Protein über diastereomere Wechselwirkungen eine chirale Diskriminierung der Ein-und Austrittswege des Elektronenvermittlers induziert.…”

Section: Elektronentransfer In Enzymelektrodenunclassified

Redoxproteinschichten auf leitenden Trägern – Systeme für bioelektronische Anwendungen

Willner

Katz

2000

Angewandte Chemie

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“…In addition to the related previous recent [17,18] and relevant older work [37] we have presented here several new examples of the enantioselective electron transfer to or from ferrocenes with the elements of planar chirality. HRP and GO proved to be the enzymes with different reactivity toward both enantiomers of 2-methylferrocene carboxylic acid and the corresponding ferricenium cations.…”

Section: Discussionmentioning

confidence: 84%

Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

et al. 1998

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/k(R)-1 are 1.7 and 1.6, respectively. Based on the known X-ray structural data for the active site of GO, it has been tentatively suggested that the enantioselectivity originates from the hydrophobic contact between the enzyme tyr-68 residue and the h 5 -C 5 H 5 ring of 1 , and a hydrogen bond network formed by his-516 and/or his-559 residues and the carboxylic group of the ferrocene derivative. The findings reported confirm the existence of enantioselective electron transfer between oxidoreductases and organometallic compounds with a planar chirality. The lack of kinetic enantioselectivity may be a result of i) the incorrect ratelimiting step, ii) unfavorable pH region, and iii) the deficit of charged groups attached to ferrocenes.

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Chiral Recognition in Mediated Electron Transfer in Redox Proteins

Cited by 29 publications

References 0 publications

Integration of Layered Redox Proteins and Conductive Supports for Bioelectronic Applications

Integration of Layered Redox Proteins and Conductive Supports for Bioelectronic Applications

Redoxproteinschichten auf leitenden Trägern – Systeme für bioelektronische Anwendungen

Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

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