Contribution of substrate reorganization energies of electron transfer to laccase activity

Mehra, Rukmankesh; Kepp, Kasper Planeta

doi:10.1039/c9cp01012b

Cited by 13 publications

(7 citation statements)

References 63 publications

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“…The catalytic site is made of four copper atoms distributed at three different centers: the T1 Cu center, where the mono-electronic oxidation of the substrate takes place, and the mono-nuclear T2 and binuclear T3 centers, where O 2 reduction occurs ( Figure 6 a). The T1 Cu is coordinated by two histidines, one cysteine, and an axial ligand with a distorted tetrahedral geometry [ 131 , 132 ]. These enzymes are also referred to as “blue laccases’’ because the intense absorption at 600 nm due to an S(π)→Cu(d x2−y2 ) ligand-to-metal charge transfer state [ 115 ] gives the blue color to the protein.…”

Section: Laccases and Lignin Oxidationmentioning

confidence: 99%

“… It has been ascertained that observed K M values relate directly to the lifetime of the active substrate of the enzyme and estimated binding free energies [ 194 , 195 ] and kinetic data correlate with the DFT spin population of the substrate, in particular, the k cat value [ 32 , 169 , 215 ]. Reorganization energies for multi-copper oxidases can be computed at the DFT level [ 216 ] and those of laccases for the first mono-electronic ET from the substrate to T1 Cu relates inversely to the enzymatic activity [ 132 ] showing that this step could determine the laccase turnover. Finally, the literature shows that the full-QM cluster model and QM/MM level were able to reproduce redox potential variations of two mutants compared to the wild-type enzyme.…”

Section: Laccases and Lignin Oxidationmentioning

confidence: 99%

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Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes

Rovaletti

Gioia

Fantucci

et al. 2023

IJMS

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Molecular modeling techniques have become indispensable in many fields of molecular sciences in which the details related to mechanisms and reactivity need to be studied at an atomistic level. This review article provides a collection of computational modeling works on a topic of enormous interest and urgent relevance: the properties of metalloenzymes involved in the degradation and valorization of natural biopolymers and synthetic plastics on the basis of both circular biofuel production and bioremediation strategies. In particular, we will focus on lytic polysaccharide monooxygenase, laccases, and various heme peroxidases involved in the processing of polysaccharides, lignins, rubbers, and some synthetic polymers. Special attention will be dedicated to the interaction between these enzymes and their substrate studied at different levels of theory, starting from classical molecular docking and molecular dynamics techniques up to techniques based on quantum chemistry.

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Section: Laccases and Lignin Oxidationmentioning

confidence: 99%

Section: Laccases and Lignin Oxidationmentioning

confidence: 99%

Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes

Rovaletti

Gioia

Fantucci

et al. 2023

IJMS

View full text Add to dashboard Cite

show abstract

“…Triclosan is, however, the only shortlisted OC to bear a combination of halogen and phenolic substituents and, as such, the poor association between susceptibility score and the removal rate could arise from the idiosyncratic suppression of halogenic electron withdrawing effects by the donating and polymerisation inducing phenolic substituent [41]. More generally, such inconsistencies might be explained by the non-incorporation of additional known (e.g., reorganisation energy [42]) and ionisation potential [3] and unknown susceptibility criteria.…”

Section: Comparison Between the Susceptibility Scores Of Ocs And Their Removal By Oxidoreductase Treatmentmentioning

confidence: 99%

Organic Contaminant Biodegradation by Oxidoreductase Enzymes in Wastewater Treatment

2020

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Organic contaminants (OCs), such as pharmaceuticals, personal care products, flame retardants, and plasticisers, are societally ubiquitous, environmentally hazardous, and structurally diverse chemical compounds whose recalcitrance to conventional wastewater treatment necessitates the development of more effective remedial alternatives. The engineered application of ligninolytic oxidoreductase fungal enzymes, principally white-rot laccase, lignin peroxidase, and manganese peroxidase, has been identified as a particularly promising approach for OC remediation due to their strong oxidative power, broad substrate specificity, low energy consumption, environmental benignity, and cultivability from lignocellulosic waste. By applying an understanding of the mechanisms by which substrate properties influence enzyme activity, a set of semi-quantitative physicochemical criteria (redox potential, hydrophobicity, steric bulk and pKa) was formulated, against which the oxidoreductase degradation susceptibility of twenty-five representative OCs was assessed. Ionisable, compact, and electron donating group (EDG) rich pharmaceuticals and antibiotics were judged the most susceptible, whilst hydrophilic, bulky, and electron withdrawing group (EWG) rich polyhalogenated compounds were judged the least susceptible. OC susceptibility scores were in general agreement with the removal rates reported for experimental oxidoreductase treatments (R2 = 0.60). Based on this fundamental knowledge, and recent developments in enzyme immobilisation techniques, microbiological enzymic treatment strategies are proposed to formulate a new generation of biological wastewater treatment processes for the biodegradation of environmentally challenging OC compounds.

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“…However, some laccases with an altered catalytic site structure may appear “yellow“ or “white“ [ 8 , 9 , 10 ]. We refer to previous studies [ 1 , 7 , 8 , 11 , 12 ] for an explanation of the catalytic mechanism and the structure-activity relationships in Lacs.…”

Section: Introductionmentioning

confidence: 99%

Laccases and Tyrosinases in Organic Synthesis

Martı́nková

Křístková

Křen

2022

IJMS

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Laccases (Lac) and tyrosinases (TYR) are mild oxidants with a great potential in research and industry. In this work, we review recent advances in their use in organic synthesis. We summarize recent examples of Lac-catalyzed oxidation, homocoupling and heterocoupling, and TYR-catalyzed ortho-hydroxylation of phenols. We highlight the combination of Lac and TYR with other enzymes or chemical catalysts. We also point out the biological and pharmaceutical potential of the products, such as dimers of piceid, lignols, isorhamnetin, rutin, caffeic acid, 4-hydroxychalcones, thiols, hybrid antibiotics, benzimidazoles, benzothiazoles, pyrimidine derivatives, hydroxytyrosols, alkylcatechols, halocatechols, or dihydrocaffeoyl esters, etc. These products include radical scavengers; antibacterial, antiviral, and antitumor compounds; and building blocks for bioactive compounds and drugs. We summarize the available enzyme sources and discuss the scalability of their use in organic synthesis. In conclusion, we assume that the intensive use of laccases and tyrosinases in organic synthesis will yield new bioactive compounds and, in the long-term, reduce the environmental impact of industrial organic chemistry.

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Contribution of substrate reorganization energies of electron transfer to laccase activity

Abstract: Laccase substrate reorganization energies computed by DFT show that electronic structure changes of these substrates contribute to enzymatic proficiency.

Cited by 13 publications

References 63 publications

Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes

Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes

Organic Contaminant Biodegradation by Oxidoreductase Enzymes in Wastewater Treatment

Laccases and Tyrosinases in Organic Synthesis

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