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| http://dx.doi.org/10.1016/j.kint.2023.01.029 | DOI Listing |
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Glycolate oxidase persulfidation mediates the salicylic acid-modulated GC switch to regulate photorespiratory H2O2 levels.
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State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, College of Life Sciences, South China Agricultural University, Guangzhou 510642, China.
Glycolate oxidase (GLO)-derived hydrogen peroxide (H2O2) is a main H2O2 source in plants and plays crucial roles in various biological functions. However, the mechanisms regulating H2O2 homeostasis are still not fully understood. We previously proposed a distinct mechanism, in which salicylic acid (SA) physically modulates photorespiratory H2O2 levels by impacting the interaction between GLO and catalase (CAT) (GC switch) in plants.
View Article and Find Full Text PDFEndogenous NO fluctuations in Arabidopsis leaves influence peroxisomal activities and ROS, NADPH, and HS metabolism.
Plant Sci
October 2025
Department of Stress, Development and Signaling in Plants, Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Estación Experimental del Zaidín (Spanish National Research Council, CSIC), C/Profesor Albareda, 1, Granada 18008, Spain.
Nitric oxide (NO) is a gasotransmitter that exerts signaling functions in plants. Using 30-day-old Arabidopsis thaliana plants wild type and transgenic lines with different NO content (Atnoa1 and Atnox1/cue1), the biochemical analysis of key components in the metabolism of ROS, NADPH, NO, and HS in leaves indicates that the imbalance of endogenous cellular NO triggered differential changes in many of the analyzed biochemical parameters including the protein profile of S-glutathionylation, S-nitrosation, tyrosine and tryptophan nitration. It was remarkable the differences observed in the antioxidant enzyme catalase and the HO-generating glycolate oxidase, two key peroxisomal enzymes involved in the ROS metabolism of these organelles, as well as the gene expression of the polyamine oxidase 4 (POD4) which encodes for the peroxisomal HO-generating POD4.
View Article and Find Full Text PDFSingle-nuclei sequencing of Moricandia arvensis reveals bundle sheath cell function in the photorespiratory shuttle of C3-C4 intermediate Brassicaceae.
J Exp Bot
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Institute of Plant Biochemistry, Cluster of Excellence on Plant Science (CEPLAS), Heinrich-Heine-University, Universitätsstraße 1, D-40225 Düsseldorf, Germany.
Spatially confined gene expression determines cell identity and is fundamental to complex plant traits. In the evolutionary transition from C3 to the more efficient C4 photosynthesis, restricting the glycine decarboxylase reaction to bundle sheath cells initiates a carbon concentrating mechanism via the photorespiratory glycine shuttle. This evolutionary step is generally thought to play an essential role in the progression from ancestral C3 to C4 photosynthesis.
View Article and Find Full Text PDFThe green algae CO concentrating mechanism and photorespiration jointly operate during acclimation to low CO.
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Aix-Marseille Université, CEA, CNRS, BIAM, UMR7265, Institut de Biosciences et Biotechnologies Aix-Marseille, CEA Cadarache, Saint-Paul-lez-Durance, France.
Due to low availability of CO in aquatic environment, microalgae have evolved a CO concentrating mechanism (CCM). It has long been thought that operation of CCM would suppress photorespiration by increasing the CO concentration at the Rubisco active site, but experimental evidence is scarce. To better explore the function of photorespiration in algae, we first characterized a Chlamydomonas reinhardtii mutant defected in low-CO inducible 20 (LCI20) and show that LCI20 is a chloroplast-envelope glutamate/malate transporter playing a role in photorespiration.
View Article and Find Full Text PDFGlycolate oxidase from Rhodococcus jostii RHA1: An accessory enzyme for lignin bioconversion with bacterial DyP-type peroxidases.
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Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom.
Accessory enzymes have been identified in lignin-degrading fungi and bacteria that can generate hydrogen peroxide, which is used as a co-substrate by lignin-oxidising peroxidases. This article describes a glycolate oxidase enzyme from lignin-degrading bacterium Rhodococcus jostii RHA1, which functions as an efficient accessory enzyme for degradation of polymeric lignin substrates by bacterial DyP-type peroxidases. The article describes: (1) enzyme purification; (2) assays for enzyme activity; (3) analysis of substrate specificity; (4) assays for enzyme combinations with bacterial DyP-type peroxidases; (5) analysis of low molecular weight products obtained using enzyme combinations.
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