Spectroelectrochemistry of Fe<sup>III</sup>- and Co<sup>III</sup>-mimochrome VI artificial enzymes immobilized on mesoporous ITO electrodes

Vitale, Rosa; Lista, L.; Lau-Truong, Stéphanie; Tucker, Ryan T.; Brett, Michael; Limoges, Benoı̂t; Pavone, Vincenzo; Lombardi, Angela; Balland, Véronique

doi:10.1039/c3cc48489k

Cited by 18 publications

(19 citation statements)

References 25 publications

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“…Two linear dependences of v 0 versus θ 222 with different slopes are observed for Fe III ‐MC6* in the 0–20 and 20–50 % TFE regions (Figure B, ▵). By assuming that the catalytic performances of mimochromes are not only related to the helical content of the peptide chain but also to the overall structural topology, we propose that the small increase in the v 0 value up to 20 % observed for Fe III ‐MC6* only correlates with the random coil↔helix transition of the peptide chains.…”

Section: Figuresupporting

confidence: 68%

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Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

et al. 2018

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Rational design provides an attractive strategy to tune and control the reactivity of bioinspired catalysts. Although there has been considerable progress in the design of heme oxidase mimetics with active-site environments of ever-growing complexity and catalytic efficiency, their stability during turnover is still an open challenge. Herein, we show that the simple incorporation of two 2-aminoisobutyric acids into an artificial peptide-based peroxidase results in a new catalyst (Fe -MC6*a) with higher resistance against oxidative damage and higher catalytic efficiency. The turnover number of this catalyst is twice as high as that of its predecessor. These results point out the protective role exerted by the peptide matrix and pave the way to the synthesis of robust bioinspired catalysts.

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Section: Figuresupporting

confidence: 68%

“…To tackle this challenge, we developed heme‐protein mimetics (mimochromes) by structure‐based design . Through a miniaturization process, we embedded the metalloporphyrin into a small peptide scaffold and systematically screened the effect of amino‐acid substitutions on function .…”

Section: Figurementioning

confidence: 99%

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

et al. 2018

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“…Within the efforts of exploiting our miniaturized hemeenzymes for practical applications, we have started investigating the behaviors of MCs upon immobilization onto different surfaces [47][48][49]. To this aim, we have evaluated two main strategies: physical adsorption and covalent binding.…”

Section: Introductionmentioning

confidence: 99%

Clickable artificial heme‐peroxidases for the development of functional nanomaterials

Zambrano

Chino

Renzi

et al. 2020

Biotech and App Biochem

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Artificial metalloenzymes as catalysts are promising candidates for their use in different technologies, such as bioremediation, biomass transformation, or biosensing. Despite this, their practical exploitation is still at an early stage. Immobilized natural enzymes have been proposed to enhance their applicability. Immobilization may offer several advantages: (i) catalyst reuse; (ii) easy separation of the enzyme from the reaction medium; (iii) better tolerance to harsh temperature and pH conditions. Here, we report an easy immobilization procedure of an artificial peroxidase on different surfaces, by means of click chemistry. FeMC6*a, a recently developed peroxidase mimic, has been functionalized with a pegylated aza‐dibenzocyclooctyne to afford a “clickable” biocatalyst, namely FeMC6*a‐PEG4@DBCO, which easily reacts with azide‐functionalized molecules and/or nanomaterials to afford functional bioconjugates. The clicked biocatalyst retains its structural and, to some extent, its functional behaviors, thus housing high potential for biotechnological applications.

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“…Starting from Co(III)‐MC1 and Co(III)‐MC4 NMR structures, Fe(III)‐MC6 was then designed with the specific purpose of introducing a peroxidase‐like activity . The MC6 model features an asymmetric five‐coordinated Fe(III)‐heme active site within the helix‐heme‐helix Mimochrome scaffold (Figure ).…”

Section: Models and Methodsmentioning

confidence: 99%

“…Indeed the MC6‐catalyzed oxidation of organic compounds (ABTS, guaiacol) in mild conditions with the “clean” oxidant H 2 O 2 , the nitration of phenols and tyrosine amino acid coupling were in fact already reported . A functional Fe(III)‐MC6‐adsorbed mesoporous In‐Sn oxide electrode able to perform the electrochemical reduction of O 2 was also proposed, suggesting a possible use of Fe(III)‐MC6 in electrochemical biosensors. Furthermore, Fe(III)‐MC6 in conjugation with antibodies could be employed in high‐sensitivity immunochemical detection assays.…”

Section: Introductionmentioning

confidence: 93%

Unveiling the structure of a novel artificial heme‐enzyme with peroxidase‐like activity: A theoretical investigation

Perrella¹,

Raucci²,

Chiariello³

et al. 2018

Biopolymers

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Fe(III)-Mimochrome VI (MC6) is a recently reported artificial heme-peptide conjugate system with a high peroxidase-like activity. By design, its structure features a five-coordinated Fe(III)-deuteroporphyrin active site, embedded in a compact α-helix-heme-α-helix "sandwich" motif. Up to now, no detailed MC6 structural characterization is available. In this work we propose a theoretical investigation based on molecular dynamics (MD) simulations and hybrid quantum mechanics/molecular mechanics (QM/MM) optimizations, aimed to shed light on several Fe(III)-MC6 structural features and to validate the de novo designed fold. Key structural elements were analyzed to achieve indirect insight relevant to understand Fe(III)-MC6 catalytic performances in solution. Extensive MD simulations showed a partial stability of the "sandwich" fold in water solution. The smaller peptide chain bonded to the heme revealed a high conformational freedom, which promoted the exposition of the heme distal side to the solvent. Regarding the accessibility of water molecules, even in Fe(III)-MC6 "closed" structure the heme cavity appeared hydrated, suggesting an easy accessibility by exogenous ligands. Fe(III)-MC6 structure in both high and low spin states was then further characterized through hybrid QM/MM optimizations. In particular, an accurate description of the active site structure was obtained, allowing a direct comparison of Fe(III)-MC6 coordination environment with that observed in the Horseradish Peroxidase crystal structures. Our results suggest a structural similarity between Fe(III)-MC6 and the natural enzyme. This study supports the interpretation of data from experimental Fe(III)-MC6 structural and functional characterization and the rational design of new artificial mimics with improved catalytic performances.

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Spectroelectrochemistry of Fe^III- and Co^III-mimochrome VI artificial enzymes immobilized on mesoporous ITO electrodes

Cited by 18 publications

References 25 publications

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

Clickable artificial heme‐peroxidases for the development of functional nanomaterials

Unveiling the structure of a novel artificial heme‐enzyme with peroxidase‐like activity: A theoretical investigation

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Spectroelectrochemistry of FeIII- and CoIII-mimochrome VI artificial enzymes immobilized on mesoporous ITO electrodes

Cited by 18 publications

References 25 publications

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

Clickable artificial heme‐peroxidases for the development of functional nanomaterials

Unveiling the structure of a novel artificial heme‐enzyme with peroxidase‐like activity: A theoretical investigation

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Spectroelectrochemistry of Fe^III- and Co^III-mimochrome VI artificial enzymes immobilized on mesoporous ITO electrodes