Kinetic and thermodynamic analysis of Cu2+-dependent reductive inactivation in direct electron transfer-type bioelectrocatalysis by copper efflux oxidase

Adachi, Taiki; Mazurenko, Ievgen; Mano, Nicolas; Kitazumi, Yuki; Kataoka, Keisuke; Kano, Kenji; Sowa, Keisei; Lojou, Élisabeth

doi:10.1016/j.electacta.2022.140987

Cited by 3 publications

(3 citation statements)

References 48 publications

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“…In addition, laccase, a Cu 2+ -dependent enzyme, exhibits pH sensitivity significantly influenced by Cu 2+ concentration [41,42]. Our study extensively explored pH and Cu 2+ concentration effects on laccase enzymatic activity.…”

Section: Optimization Of Magnolol Synthesis Through the Molac14 Enzymementioning

confidence: 99%

Identification and Validation of Magnolol Biosynthesis Genes in Magnolia officinalis

Yang,

Li,

Zong

et al. 2024

Molecules

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Bacterial infections pose a significant risk to human health. Magnolol, derived from Magnolia officinalis, exhibits potent antibacterial properties. Synthetic biology offers a promising approach to manufacture such natural compounds. However, the plant-based biosynthesis of magnolol remains obscure, and the lack of identification of critical genes hampers its synthetic production. In this study, we have proposed a one-step conversion of magnolol from chavicol using laccase. After leveraging 20 transcriptomes from diverse parts of M. officinalis, transcripts were assembled, enriching genome annotation. Upon integrating this dataset with current genomic information, we could identify 30 laccase enzymes. From two potential gene clusters associated with magnolol production, highly expressed genes were subjected to functional analysis. In vitro experiments confirmed MoLAC14 as a pivotal enzyme in magnolol synthesis. Improvements in the thermal stability of MoLAC14 were achieved through selective mutations, where E345P, G377P, H347F, E346C, and E346F notably enhanced stability. By conducting alanine scanning, the essential residues in MoLAC14 were identified, and the L532A mutation further boosted magnolol production to an unprecedented level of 148.83 mg/L. Our findings not only elucidated the key enzymes for chavicol to magnolol conversion, but also laid the groundwork for synthetic biology-driven magnolol production, thereby providing valuable insights into M. officinalis biology and comparative plant science.

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Section: Optimization Of Magnolol Synthesis Through the Molac14 Enzymementioning

confidence: 99%

Identification and Validation of Magnolol Biosynthesis Genes in Magnolia officinalis

Yang,

Li,

Zong

et al. 2024

Molecules

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“…[43] Recently, it has been demonstrated that the direct electron transfer-type bioelectrocatalytic activity of CueO is inhibited by the presence of Cu(II) in the electrolyte. [44] In this process, it is suggested that Cu(II) (a sixth copper ion) coordinates to histidine residues close to the Cu T2 / Cu T3 cluster and is electrochemically reduced, inducing conformational changes near the catalytic center, which inhibits the dynamic transitions of the Cu T2 / Cu T3 cluster and Cu T1 center needed to the catalytic cycle. [44] This emphasizes the importance of the 3D arrangement of the catalytic site and the dynamics to the enzyme activity.…”

Section: Multicopper Oxidasesmentioning

confidence: 99%

“…Some variants of CueO have been designed to show increased onset potential for O 2 reduction to water, becoming attractive catalysts for the cathode of biofuel cells [43] . Recently, it has been demonstrated that the direct electron transfer‐type bioelectrocatalytic activity of CueO is inhibited by the presence of Cu(II) in the electrolyte [44] . In this process, it is suggested that Cu(II) (a sixth copper ion) coordinates to histidine residues close to the Cu T2 /Cu T3 cluster and is electrochemically reduced, inducing conformational changes near the catalytic center, which inhibits the dynamic transitions of the Cu T2 / Cu T3 cluster and Cu T1 center needed to the catalytic cycle [44] .…”

Section: Some Remarkable Metalloenzymesmentioning

confidence: 99%

Insights from Enzymatic Catalysis: A Path towards Bioinspired High‐Performance Electrocatalysts

2023

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Enzymes, especially some metalloenzymes, are exceptional catalysts for redox reactions with technological applications in several fields, including energy conversion systems and producing fuels and value‐added chemicals. Because of that, they have inspired the development of synthetic catalysts to obtain high‐performance materials. However, several fundamental aspects should be better understood to achieve this goal, such as enzyme catalysis and the role of the three‐dimensional catalytic site. Therefore, this review addresses key structural and activity aspects of some remarkable metalloenzymes and discusses three‐dimensional catalysis as an approach to enzyme catalysis. Also, the case of the multicopper oxidase enzymes is shown as an example of how the three‐dimensional coordination environment of the copper ions in the active site can impact catalysis.

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Electrochemical investigations of the multicopper oxidase from Aquifex aeolicus under direct electron transfer with carbon electrodes

Moro,

Brissos,

Zanardi

et al. 2023

Electrochimica Acta

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Kinetic and thermodynamic analysis of Cu2+-dependent reductive inactivation in direct electron transfer-type bioelectrocatalysis by copper efflux oxidase

Cited by 3 publications

References 48 publications

Identification and Validation of Magnolol Biosynthesis Genes in Magnolia officinalis

Identification and Validation of Magnolol Biosynthesis Genes in Magnolia officinalis

Insights from Enzymatic Catalysis: A Path towards Bioinspired High‐Performance Electrocatalysts

Electrochemical investigations of the multicopper oxidase from Aquifex aeolicus under direct electron transfer with carbon electrodes

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