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Performance, kinetics, and mechanism of 1,2,3-trimethylbenzene biodegradation by a newly isolated marine microalga.

J Environ Manage

January 2025

Key Laboratory of Marine Environment and Ecology, Ministry of Education, Ocean University of China, Qingdao, 266100, China; College of Environmental Science and Engineering, Ocean University of China, Qingdao, 266100, China.

Article Synopsis
  • Recent marine pollution concerns revolve around the accidental spills of toxic C9 aromatics, particularly 1,2,3-trimethylbenzene (1,2,3-TMB), due to its high toxicity and resistance to degradation.
  • A marine diatom, Chaetoceros sp. QG-1, was isolated from Quangang, China, and demonstrated the highest degradation efficiency of 1,2,3-TMB at a concentration of 5 mg/L.
  • The study identified the degradation process, where 1,2,3-TMB is converted into less harmful compounds, involving key enzymes like 2OG Fe(II) oxygenase, thus supporting bioremediation efforts in polluted marine environments
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Fe(II)- and 2-oxoglutarate (2OG)-dependent dioxygenases use 2OG and O cofactors to catalyse substrate oxidation and yield oxidised product, succinate, and CO. Simultaneous detection of substrate and cofactors is difficult, contributing to a poor understanding of the dynamics between substrate oxidation and 2OG decarboxylation activities. Here, we profile 5-methylcytosine (C)-oxidising Ten-Eleven Translocation (TET) enzymes using MS and H NMR spectroscopy methods and reveal a high degree of substrate oxidation-independent 2OG turnover under a range of conditions.

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The 2-oxoglutarate carrier (OGC), pivotal in cellular metabolism, facilitates the exchange of key metabolites between mitochondria and cytosol. This study explores the influence of NADPH on OGC transport activity using proteoliposomes. Experimental data revealed the ability of NADPH to modulate the OGC activity, with a significant increase of 60% at 0.

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Biosynthesis of Piceatannol from Resveratrol in Grapevine Can Be Mediated by Cresolase-Dependent -Hydroxylation Activity of Polyphenol Oxidase.

Plants (Basel)

September 2024

Plant Proteomics and Functional Genomics Group, Department of Biochemistry and Molecular Biology and Soil Science and Agricultural Chemistry, Faculty of Science, University of Alicante, 03690 Alicante, Spain.

Piceatannol is a naturally occurring hydroxylated analogue of the stilbene phytoalexin resveratrol that can be found in grape fruit and derived products. Piceatannol has aroused great interest as it has been shown to surpass some human health-beneficial properties of resveratrol including antioxidant activity, several pharmacological activities and also bioavailability. The plant biosynthetic pathway of piceatannol is still poorly understood, which is a bottleneck for the development of both plant defence and bioproduction strategies.

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Methods for production and assaying catalysis of isolated recombinant human aspartate/asparagine-β-hydroxylase.

Methods Enzymol

September 2024

Chemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, United Kingdom. Electronic address:

Aspartate/asparagine-β-hydroxylase (AspH) is a transmembrane 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes the post-translational hydroxylation of aspartate- and asparagine-residues in epidermal growth factor-like domains (EGFDs) of its substrate proteins. Upregulation of ASPH and translocation of AspH from the endoplasmic reticulum membrane to the surface membrane of cancer cells is associated with enhanced cell motility and worsened clinical prognosis. AspH is thus a potential therapeutic and diagnostic target for cancer.

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