Electrochemical aspects of cytochrome P-450 system from liver microsomes

Scheller, Frieder W.; Renneberg, Reinhard; Strnad, Gabriela; Pommerening, K.; Mohr, Peter J.

doi:10.1016/0302-4598(77)80048-2

Cited by 36 publications

(10 citation statements)

References 14 publications

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“…30-32 An early attempt at voltammetry of cyt P450s used microsomal preparations in solution, but electron transfer to cyt P450 was not achieved. 33 Several proteins and small molecules that deliver electrons to the enzyme have been used to mediate electron transfer and catalytic reactions of cyt P450s. 34-36 …”

Section: Overview Of Thin Film Voltammetry and Biocatalysis With mentioning

confidence: 99%

Bioelectronic Delivery of Electrons to Cytochrome P450 Enzymes

2011

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Cytochrome P450s (cyt P450s) are the major oxidative enzymes in human oxidative metabolism of drugs and xenobiotic chemicals. In nature, the iron heme cyt P450s utilize oxygen and electrons delivered from NADPH by a reductase enzyme to oxidize substrates stereo- and regioselectively. Significant research has been directed toward achieving these events electrochemically. This feature article discusses the direct electrochemistry of cyt P450s in thin films, and the utilization of such films for electrochemically-driven biocatalysis. Maintaining and confirming structural integrity and catalytic activity of cyt P450s in films is an essential feature of these efforts. We highlight here our efforts to elucidate the influence of iron heme spin state and secondary structure of human cyt P450s on voltammetric and biocatalytic properties, using methodologies to quantitatively describe the dynamics of these processes in thin films. We also describe the first cyt P450/reductase films that accurately mimic the natural biocatalytic pathway, and show how they can be used with voltammetry to elucidate key mechanistic features. Such bioelectronic cyt P450 systems have high value for future drug development, toxicity screening, fundamental investigations, and chemical synthesis systems.

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Section: Overview Of Thin Film Voltammetry and Biocatalysis With mentioning

confidence: 99%

Bioelectronic Delivery of Electrons to Cytochrome P450 Enzymes

2011

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“…P450s and enzyme electrodes based on P450s are promising for the application as test-systems, biosensors and bioreactors. The main principles of bioelectrocatalysis were discussed earlier [6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22]. Electrochemical approach to redox enzymes and, especially, to metalloproteins is a rapidly developing area of research [23][24][25][26].…”

Section: Introductionmentioning

confidence: 99%

Electrochemical reduction of cytochrome P450 as an approach to the construction of biosensors and bioreactors

Shumyantseva

Булко²,

Archakov³

2005

Journal of Inorganic Biochemistry

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“…This concept was established by us [17] in parallel with the development of the 'promoted' direct electron exchange of modified electrode for c-type cytochromes [28,29]. Regarding protein electrochemistry, the number of papers on P450 ranks third after cytochrome c and glucose oxidase.…”

Section: Electrochemical Behaviour Of Cytochrome P450smentioning

confidence: 97%

“…The cycle of P450-catalysed reactions offers different alternatives for coupling the substrate conversion with an indicator electrode, which are presented in our 'classical' scheme of P450-based biosensors [17].…”

Section: Principles Of Coupling Cytochrome P450 With Signal Transducersmentioning

confidence: 99%

Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors

Yarman

Peng

et al. 2011

Bioanal Rev

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Aromatic peroxygenase (APO) from the basidiomycetous mushroom Agrocybe aegerita (AaeAPO) and microperoxidases (MPs) obtained from cytochrome c exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of cytochrome P450 (P450), making MPs and APOs to alternate recognition elements in biosensors for the detection of typical P450 substrates. Here, we discuss recently developed approaches using microperoxidases and peroxygenases in view of their potential to supplement P450 enzymes as recognition elements in biosensors for aromatic compounds. Starting as early as the 1970s, the direct electron transfer between electrodes and the heme group of heme peptides called microperoxidases has been used as a model of oxidoreductases. These MP-modified electrodes are used as hydrogen peroxide detectors based on the catalytic current generated by electrically contacted microperoxidase molecules. A similar catalytic reaction has been obtained for the electrode-immobilised heme protein AaeAPO. However, up to now, no MP-based sensors for substrates have been described. In this review, we present biosensors which indicate 4-nitrophenol, aniline, naphthalene and p-aminophenol based on the peroxide-dependent substrate conversion by electrode-immobilised MP and AaeAPO. In these enzyme electrodes, the signal is generated by the conversion of all substrates, thus representing in complex media an overall parameter. The performance of these sensors and their further development are discussed in comparison with P450-based electrodes

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Electrochemical aspects of cytochrome P-450 system from liver microsomes

Cited by 36 publications

References 14 publications

Bioelectronic Delivery of Electrons to Cytochrome P450 Enzymes

Bioelectronic Delivery of Electrons to Cytochrome P450 Enzymes

Electrochemical reduction of cytochrome P450 as an approach to the construction of biosensors and bioreactors

Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors

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