From electrochemistry to enzyme kinetics of cytochrome P450

Shumyantseva, Victoria V.; Kuzikov, Alexey V.; Masamrekh, Rami A.; Булко, Т. В.; Archakov, Alexander I.

doi:10.1016/j.bios.2018.08.040

Cited by 70 publications

(37 citation statements)

References 92 publications

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“…The interpretation of electrochemical signals in DET biosensors is complex because the reduction of the ferric P450 requires a potential at which the co-substrate O 2 is also reduced. It is generally accepted that the current for the O 2 catalytic reduction is further increased in the presence of P450 substrates [179]. However, this increase may simply be due to a variation of O 2 concentration upon addition of the organic substrate.…”

Section: Rh + O 2 + Nad(p)h + H + → Roh + H 2 O + Nad(p) + (11)mentioning

confidence: 99%

Electrocatalysis by Heme Enzymes—Applications in Biosensing

et al. 2021

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Heme proteins take part in a number of fundamental biological processes, including oxygen transport and storage, electron transfer, catalysis and signal transduction. The redox chemistry of the heme iron and the biochemical diversity of heme proteins have led to the development of a plethora of biotechnological applications. This work focuses on biosensing devices based on heme proteins, in which they are electronically coupled to an electrode and their activity is determined through the measurement of catalytic currents in the presence of substrate, i.e., the target analyte of the biosensor. After an overview of the main concepts of amperometric biosensors, we address transduction schemes, protein immobilization strategies, and the performance of devices that explore reactions of heme biocatalysts, including peroxidase, cytochrome P450, catalase, nitrite reductase, cytochrome c oxidase, cytochrome c and derived microperoxidases, hemoglobin, and myoglobin. We further discuss how structural information about immobilized heme proteins can lead to rational design of biosensing devices, ensuring insights into their efficiency and long-term stability.

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Section: Rh + O 2 + Nad(p)h + H + → Roh + H 2 O + Nad(p) + (11)mentioning

confidence: 99%

Electrocatalysis by Heme Enzymes—Applications in Biosensing

et al. 2021

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“…Although involved in the redox metabolism of a wide range of drugs and xenobiotics [4], cytochromes like P450 have given rise to only few electrochemical characterization [18,19], probably due to the difficulty in isolating and solubilizing appropriate amounts of this enzyme, which therefore directed electrochemical investigations towards immobilized systems [20][21][22]. A recent example of P450 related metabolism was explored for omeprazole [23], a proton pump inhibitor used to regulate stomach acidity.…”

Section: Electrochemical Behavior Of Redox Enzymes Towards Drugsmentioning

confidence: 99%

Disclosing the redox metabolism of drugs: The essential role of electrochemistry

Buriez

Labbé

2020

Current Opinion in Electrochemistry

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Electrochemical methods provide a wide range of strategies to explore the metabolism of drugs. These approaches traditionally encompass preparative aspects viz. the electrochemical generation of potent metabolites or the electrochemical exploration of the reactivity of redox enzymes (or their mimics) towards drugs. More recently the electroanalytical characterization of the successive redox and redoxcoupled reactions was found effective to unravel more complex mechanisms, especially those related to the reactivity of bioorganometallic drugs. This minireview highlights the contribution of these different electrochemical strategies to the determination of drug metabolism through representative recent examples.

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“…These oxygen reduction peaks shift to a more negative potential of À 290 mV and À 620 mV respectively upon attachment of the CYP3A4 enzyme. This indicates an interaction of oxygen with the enzyme which is what is expected of CYP3A4 since it undergoes a monooxygenation reaction [8,23,24]. This response is caused by the CYP3A4 enzyme which catalyses the mass transport limited reduction of the dioxygen molecule [25].…”

Section: Characterisation Of Cyp3a4 Biosensormentioning

confidence: 99%

“…A biosensor will be able to distinguish between fast, slow or intermediate metabolisers and have medi-cation be adjusted accordingly. The benefit of electrochemical biosensors is that it eliminates the need for electron donators such as NADPH and cytochrome P450 reductase (CPR) [8]. An enzymatic biosensor will be able to mimic the body's natural metabolism of these drugs or substrates, however, not much literature is available for CYP biosensors for TB drug detection.…”

Section: Introductionmentioning

confidence: 99%

“…It would be preferable for the mediators to have fast and reversible oxidation-reduction reaction couples, for the electron transfers process to be reproducible [12]. The fast electron transfer processes occurring at the electrode surface can be integrated with catalytic reaction on the electrode surface, thereby making it possible to create sensor devices as analytical tools [8,13]. In this work, biosensors developed with CYP3A4 enzyme that is incorporated into copper polypropyleneimine metallodendrimer (CuPPI), were used to detect isoniazid, ethambutol, rifampicin and pyrazinamide in buffer and spiked real samples.…”

Section: Introductionmentioning

confidence: 99%

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Metallodendrimer‐sensitised Cytochrome P450 3A4 Electrochemical Biosensor for TB Drugs

et al. 2020

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A cytochrome P450 3A4 (CYP3A4) based enzymatic biosensor was developed with the incorporation of a first-generation copper polypropyleneimine (CuPPI) metallodendrimer for the detection of anti-tuberculosis (anti-TB) drugs. The development of an electrochemical phenotype biosensor for this purpose is still vital since it aids in the ongoing fight against TB by determining metabolic profile. This allows TB treatment to be tailored on an individual patient basis, minimise adverse drug reactions and improve quality of life in TB patients. This simple biosensor was constructed via physical adsorption of CuPPI onto a gold electrode with subsequent electrostatic attachment of CYP3A4. The biosensor was successful in detecting all four first line anti-TB drugs i. e. isoniazid, ethambutol, pyrazinamide and rifampicin with limits of detection ranging from 0.02244 to 0.1072 nM in 0.1 M phosphate buffer. The developed biosensor was then applied towards "real samples" in the form of spiked synthetic urine and plasma. Calibration curves were carried out in the complex matrices, which were diluted with 0.1 M PB. These yielded good LOD in the range of ultra-low micromolar concentration i. e. 0.165-0.884 μM across all drugs. Recovery studies were also successful when detecting the real tablets in both plasma and urine with results ranging from 91.5 % to 108.5 %.

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From electrochemistry to enzyme kinetics of cytochrome P450

Cited by 70 publications

References 92 publications

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Disclosing the redox metabolism of drugs: The essential role of electrochemistry

Metallodendrimer‐sensitised Cytochrome P450 3A4 Electrochemical Biosensor for TB Drugs

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