Generating monomeric 5-coordinated microperoxidase-11 using carboxylic acid functionalized silver nanoparticles: A surface-enhanced resonance Raman scattering analysis

Kalaivani, Govindasamy; Sivanesan, Arumugam; Kannan, Ayyadurai; Sevvel, Ranganathan

doi:10.1016/j.colsurfb.2016.07.017

Cited by 7 publications

(4 citation statements)

References 66 publications

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“…But also values in the low micromolar range were reported, e. g. for MP‐11 immobilized in an Au‐nanoparticle multilayer architecture or in a nanostructured polyurethane‐matrix . The high apparent K M for hydrogen peroxide obtained in the present study suggests a low affinity of MP‐11 on PDADMAC‐modified mpATO to its substrate that is presumably caused by the six‐coordinated low‐spin conformation of MP‐11 on PDADMAC‐modified mpATO leading to decreased substrate accessibility …”

Section: Resultssupporting

confidence: 53%

“…The RR spectrum of MP‐11 in solution in absence of PDADMAC shows the presence of two species. The positions of ν 4 at 1373 cm −1 , ν 3 at 1506 cm −1 , ν 2 at 1586 cm −1 and ν 10 at 1640 cm −1 are characteristic of an oxidized six‐coordinated low‐spin heme iron while the ν 3 band at 1480 cm −1 indicates the presence of six‐coordinated high‐spin species . In contrast, the RR spectra of MP‐11 in a mixed solution with PDADMAC as well as immobilized on PDADMAC‐modified mpATO demonstrate that in presence of the polyelectrolyte only the 6cLS species is formed confirming the results obtained by UV/Vis‐spectroscopy.…”

Section: Resultsmentioning

confidence: 92%

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Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase‐11 Immobilized on Mesoporous Antimony‐Doped Tin Oxide

et al. 2017

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The heme‐undecapeptide microperoxidase‐11 (MP‐11) was immobilized on mesoporous antimony‐doped tin oxide (ATO) thin‐film electrodes modified with the positively charged binding promotor polydiallyldimethylammonium chloride. Surface concentrations of MP‐11 of 1.5 nmol cm−2 were sufficiently high to enable spectroelectrochemical analyses. UV/Vis spectroscopy and resonance Raman spectroscopy revealed that immobilized MP‐11 adopts a six‐coordinated low‐spin conformation, as in solution in the presence of a polycation. Cathodic reduction of hydrogen peroxide at potentials close to +500 mV versus Ag/AgCl indicates that the reaction proceeds via a Compound I‐type like intermediate, analogous to natural peroxidases, and confirms mesoporous ATO as a suitable host material for adsorbing the heme‐peptide in its native state. A hydrogen peroxide sensor is proposed by using the bioelectrocatalytic properties of the MP‐11‐modified ATO.

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Section: Resultssupporting

confidence: 53%

Section: Resultsmentioning

confidence: 92%

Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase‐11 Immobilized on Mesoporous Antimony‐Doped Tin Oxide

et al. 2017

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“…This feature allows assessment of the impact of amino acid residues located on the proximal side of the heme ring on the studied reaction mechanism. MP-11 has been employed in numerous studies devoted to the development of heterogeneous biocatalysts/bioelectrocatalysts and spectroelectrochemical and bioelectronic sensors and devices. − Furthermore, MPs were the subject of intensive studies on their pH-dependent behavior in aqueous solution, − reactivity in catalytic oxidation of various substrates, − and substitution reactions with various ligands. − However, there are only a few reports available in the literature regarding the pH-dependent reactivity of MPs under alkaline conditions, where successive ionizations of H 2 O and HisH ligands result in the accumulation of [Fe III (OH)(HisH)] and [Fe III (OH)(His – )] species, respectively. , …”

Section: Introductionmentioning

confidence: 99%

Experimental and Computational Insight into the Mechanism of NO Binding to Ferric Microperoxidase. The Likely Role of Tautomerization to Account for the pH Dependence

et al. 2021

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According to the current paradigm, the metal− hydroxo bond in a six-coordinate porphyrin complex is believed to be significantly less reactive in ligand substitution than the analogous metal−aqua bond, due to a much higher strength of the former bond. Here, we report kinetic studies for nitric oxide (NO) binding to a heme-protein model, acetylated microperoxidase-11 (AcMP-11), that challenge this paradigm. In the studied pH range 7.4−12.6, ferric AcMP-11 exists in three acid− base forms, assigned in the literature as 2), and [(AcMP-11)Fe III (OH)(His − )] (3). From the pH dependence of the second-order rate constant for NO binding (k on ), we determined individual rate constants characterizing forms 1−3, revealing only a ca. 10-fold decrease in the NO binding rate on going from 1 (k on(1) = 3.8 × 10 6 M −1 s −1 ) to 2 (k on (2) = 4.0 × 10 5 M −1 s −1 ) and the inertness of 3. These findings lead to the abandonment of the dissociatively activated mechanism, in which the reaction rate can be directly correlated with the Fe−OH bond energy, as the mechanistic explanation for the process with regard to 2. The reactivity of 2 is accounted for through the existence of a tautomeric equilibrium between the major [(AcMP-11)Fe III (OH)(HisH)] (2a) and minor [(AcMP-11)Fe III (H 2 O)(His − )] (2b) species, of which the second one is assigned as the NO binding target due to its labile Fe−OH 2 bond. The proposed mechanism is further substantiated by quantum-chemical calculations, which confirmed both the significant labilization of the Fe−OH 2 bond in the [(AcMP-11)Fe III (H 2 O)(His − )] tautomer and the feasibility of the tautomer formation, especially after introducing empirical corrections to the computed relative acidities of the H 2 O and HisH ligands based on the experimental pK a values. It is shown that the "effective lability" of the axial ligand (OH − /H 2 O) in 2 may be comparable to the lability of the H 2 O ligand in 1.

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“…As a kind of peroxidase mimic, Heme-peptide has been researched for years because it is highly stable and can be easily synthesized. Heme-peptides are produced by covalently linking peptides to ferriporphyrin and have shown great potential for use in medical detection, as biocatalysts, sensitive sensors, and in other applications [14][15][16]. Microperoxidases (MPs) have been the most effective peroxidases among these heme-peptides.…”

Section: Introductionmentioning

confidence: 99%

Design and Characterization of a Novel Artificial Peroxidase

Yuan

Zhao

et al. 2019

Catalysts

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In this study, we reported on a novel mimetic peroxidase, deuterohemin–Ala–His–Glu, (Dh–A–H–E). The kinetic parameters of Dh–A–H–E suggested that it was a mimetic peroxidase and followed the ping–pong mechanism. Compared to horseradish peroxidase, Dh–A–H–E exhibited excellent stability when tested at different pH and temperatures, and using different organic solvents. Based on our above results, a new method using Dh–A–H–E has successfully been developed for the fast and quantitative detection of trace amounts of glucose.

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Generating monomeric 5-coordinated microperoxidase-11 using carboxylic acid functionalized silver nanoparticles: A surface-enhanced resonance Raman scattering analysis

Cited by 7 publications

References 66 publications

Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase‐11 Immobilized on Mesoporous Antimony‐Doped Tin Oxide

Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase‐11 Immobilized on Mesoporous Antimony‐Doped Tin Oxide

Experimental and Computational Insight into the Mechanism of NO Binding to Ferric Microperoxidase. The Likely Role of Tautomerization to Account for the pH Dependence

Design and Characterization of a Novel Artificial Peroxidase

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