Micellar histidinate hematin complex as an artificial peroxidase enzyme model: Voltammetric and spectroscopic investigations

Moosavi‐Movahedi, Ali Akbar; Semsarha, Farid; Heli, H.; Nazari, Kamran; Ghourchian, Hedayatollah; Hong, Jun; Hakimelahi, G. H.; Saboury, Ali Akbar; Sefidbakht, Yahya

doi:10.1016/j.colsurfa.2008.01.047

Cited by 38 publications

(55 citation statements)

References 38 publications

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“…(Hydroxy[3,3'-(3,7,12,17-tetramethyl-8,13-divinyl-2,18-porphyrindiyl-κ 2 N 21 ,N 23 )dipropanoato (2-)]iron) is a heme derivative phorphyrin coordinating an iron (III) center which is part of the core of the catalytic centers in several heme proteins as cytochrome c, myoglobin and hemoglobin [28,29]. This work presents the biomimetic behavior of the hematin sensor prepared by direct adsorption of hematin on an electrochemically pre-treated glassy carbon electrode in sodium bicarbonate.…”

Section: Hematinmentioning

confidence: 99%

Biomimetic behavior and nanomolar detection of hydrogen peroxide on an electrochemically pre-treated hematin modified glassy carbon electrode

Buoro

Bacil

Sanz

et al. 2017

Sensors and Actuators B: Chemical

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Section: Hematinmentioning

confidence: 99%

Biomimetic behavior and nanomolar detection of hydrogen peroxide on an electrochemically pre-treated hematin modified glassy carbon electrode

Buoro

Bacil

Sanz

et al. 2017

Sensors and Actuators B: Chemical

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“…Biomimetic chemistry attempts to improve the performance of chemical reactions and catalysts by imitating enzymatic processes (Yatsimirsky 2004; Silavi, Divsalar & Saboury 2012). Robust biocatalysts may be formed by encapsulating a prosthetic group in hydrophobic pocket-like micelles (Moosavi-Movahedi et al 2008; Wang et al 2010), vesicles (Murakami, Hisaeda & Ohno 1984; Murakami, Hisaeda & Ohno 1987; Murakami, Hisaeda & Ohno 1990; Murakami, Hisaeda & Ohno 1991) and macrocyclic compounds (Bender & Komiyama 1978; D’Souza & M. L. Bender 1978; Tabushi & Yamamura 1983; Diederich 1988; Murakami, Kikuchi, Hisaeda & Hayashida 1996) that mimic the polypeptide envelope protecting the catalytic center of the natural enzymes. Artificial enzymes could be biomimetically constructed from native proteins as host for prosthetic active sites to simulate the catalytic functions exhibited by natural enzymes (Quilez, Lauzon, Desfosses, Mansuy & Mahy 1996; Grinbergs, O’Brien & Hrkal 1999; Monzani et al 2001).…”

Section: Introductionmentioning

confidence: 99%

Caseoperoxidase, mixed β-casein–SDS–hemin–imidazole complex: a nano artificial enzyme

Moosavi-Movahedi

Gharibi

Hadi-Alijanvand

et al. 2015

Journal of Biomolecular Structure and Dynamics

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A novel peroxidase-like artificial enzyme, named “caseoperoxidase”, was biomimetically designed using a nano artificial amino acid apo-protein hydrophobic pocket. This four-component nano artificial enzyme containing heme-imidazole-β-casein-SDS exhibited high activity growth and kcat performance towards the native horseradish peroxidase (HRP) demonstrated by the steady state kinetics using UV-Vis spectrophotometry. The hydrophobicity and secondary structure of the caseoperoxidase were studied by ANS fluorescence and circular dichroism spectroscopy. Camel β-casein (Cβ-casein), with a flexible structure and exalted hydrophobicity, was selected as an appropriate apo-protein for the heme active site using a homology modeling method. Heme docking into the newly obtained Cβ-casein structure indicated one heme was mainly incorporated with Cβ-casein. The presence of a main electrostatic site for the active site in the Cβ-casein was also confirmed by experimental methods through Wyman binding potential and isothermal titration calorimetry. The existence of Cβ-casein protein in this biocatalyst lowered the suicide inactivation, and indicated that the obtained structure has a good protective role for the heme active-site. Additional further experiments confirmed the retention of caseoperoxidase structure and function as an artificial enzyme.

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“…This can be attributed to the very "inert" physical shape of solid electrodes comparing to redox enzymes and to the restricted potential window available on conventional carbon based electrodes. Alternative options consist to develop modified electrodes with interfaces mimicking the enzyme biocatalytic structure [13,14], to immobilize an enzyme onto the electrode surface [15][16][17] or to use electrodes with extended electrochemical potential domains such as the boron doped diamond electrode [18].…”

Section: Introductionmentioning

confidence: 99%

Utility of Screen Printed Electrodes for in Vitro Metabolic Stability Assays: Application to Acetaminophen and its Thioconjugates

et al. 2011

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Screen printed electrodes (SPEs), in addition to their utility in the electrochemical quantification of compounds of pharmacological interest may be used (i) for studying the redox pattern of drug candidates by cyclic voltammetry, (ii) for electrochemical synthesis in microvolumes (microelectrosynthesis) at a selected applied potential with subsequent off-line LC-MS identification of the generated products, and (iii) for monitoring enzymatic reactions in microvolumes of samples. The resulting data are of valuable predictive value for in vitro metabolic stability assays. Acetaminophen (APAP) was used as relevant model drug compound to illustrate potential applications of SPEs in pharmaceutical research. The electrooxidation of APAP was studied, in the absence and presence of endogenous thiols, in microvolume sample by cyclic voltammetry and by microelectrolysis at a carbon based SPE (CSPE) and the generated products were identified off-line by liquid chromatography coupled to mass spectrometry (LC-MS).

show abstract

Micellar histidinate hematin complex as an artificial peroxidase enzyme model: Voltammetric and spectroscopic investigations

Cited by 38 publications

References 38 publications

Biomimetic behavior and nanomolar detection of hydrogen peroxide on an electrochemically pre-treated hematin modified glassy carbon electrode

Biomimetic behavior and nanomolar detection of hydrogen peroxide on an electrochemically pre-treated hematin modified glassy carbon electrode

Caseoperoxidase, mixed β-casein–SDS–hemin–imidazole complex: a nano artificial enzyme

Utility of Screen Printed Electrodes for in Vitro Metabolic Stability Assays: Application to Acetaminophen and its Thioconjugates

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