Article
Plant Sciences
Stefanie J. Mueller-Schuessele, Finja Bohle, Jacopo Rossi, Paolo Trost, Andreas J. Meyer, Mirko Zaffagnini
Summary: The study shows that the glutathione-dependent redox network in plastids is highly conserved in streptophytes, with some variability in scavenging and damage repair enzymes. Analysis of cysteine conservation indicates that S-glutathionylation in plastids plays a significant and yet under-investigated role in redox regulation and stress response. The research reveals that certain cysteine residues undergoing S-glutathionylation are completely conserved in model species from green algae to flowering plants, pointing to independent gains and losses of cysteines during land plant evolution.
Article
Biochemistry & Molecular Biology
Loick Christ, Jeremy Couturier, Nicolas Rouhier
Summary: This study discovered the redox properties of the Arabidopsis thaliana mitochondrial class II GRXS15 protein, showing that it is prone to oxidation and forms reversible oxidation forms. These forms may serve as catalytic intermediates of the oxidoreductase activity or as a protective mechanism, preventing irreversible oxidation and allowing Fe-S cluster binding upon reduction.
Article
Multidisciplinary Sciences
Jian Huang, Xiao Fan, Xueqin Jin, Sooyeon Jo, Hanxiong Bear Zhang, Akie Fujita, Bruce P. Bean, Nieng Yan
Summary: Cannabidiol (CBD), a nonpsychoactive compound found in cannabis, is effective in treating epilepsy and pain. Researchers have discovered that CBD interacts with Na(v)1.7 channels at sub-micromolar concentrations, providing insights into its therapeutic mechanisms. The identification of binding sites for CBD may lead to the development of improved compounds for medical use.
NATURE COMMUNICATIONS
(2023)
Article
Biochemistry & Molecular Biology
Jannik Zimmermann, Julian Oestreicher, Fabian Geissel, Marcel Deponte, Bruce Morgan
Summary: A novel high-throughput assay has been developed for rapid and semi-quantitative evaluation of glutathione-dependent oxidoreductase activity. This method combines genetic fusion constructs between glutathione transporter and redox-sensitive fluorescent protein, enabling rapid characterization of enzyme activity and structure-function relationships. The assay allows direct screening of glutaredoxin activity and efficient detection of enzyme activity with physiological substrates.
FREE RADICAL BIOLOGY AND MEDICINE
(2021)
Article
Biochemistry & Molecular Biology
Ioannis G. Riziotis, Antonio J. M. Ribeiro, Neera Borkakoti, Janet M. Thornton
Summary: Enzyme catalysis is controlled by a limited set of residues and co-factors. By utilizing three-dimensional templates, recurring catalytic modules that are involved in metal ion, co-factor, and substrate binding can be identified. Some of these convergent modules perform specific catalytic functions, while enzymes that have diverged during evolution retain specific regions of their active site.
JOURNAL OF MOLECULAR BIOLOGY
(2023)
Review
Biochemistry & Molecular Biology
Elizabeth Corteselli, Reem Aboushousha, Yvonne Janssen-Heininger
Summary: Glutathione plays a crucial role as an antioxidant and regulates biological processes through protein S-glutathionylation. Recent studies have implicated protein S-glutathionylation in the pathogenesis of various diseases, including idiopathic pulmonary fibrosis, and its association with oxidative stress and epithelial cell apoptosis.
Article
Cell Biology
Brian C. Seitz, Xheni Mucelli, Maira Majano, Zoey Wallis, Ashley C. Dodge, Catherine Carmona, Matthew Durant, Sharra Maynard, Linda S. Huang
Summary: This study explores the relationship between meiosis II spindle disassembly and cytokinesis. The results show that SPS1 and AMA1 genes play different roles in the disassembly of meiosis II spindles, and the phenotypic defects of these two genes are also different. In addition, AMA1 regulates the loss of Ase1 and Cin8, while SPS1 regulates the loss of Bim1.
MOLECULAR BIOLOGY OF THE CELL
(2023)
Article
Biochemistry & Molecular Biology
Claudio F. Costa, Celien Lismont, Serhii Chornyi, Hongli Li, Mohamed A. F. Hussein, Hans R. Waterham, Marc Fransen
Summary: Peroxisomes play a crucial role in cellular redox metabolism and communication. Our understanding of how the peroxisomal redox equilibrium is maintained, especially the function of glutathione in the peroxisome interior, remains limited. This study identifies a human peroxisomal enzyme, GSTK1, as a glutathione-consuming enzyme and demonstrates its role in peroxisomal glutathione regulation. The findings suggest that GSTK1 has GSH-dependent disulfide bond oxidoreductase activity.
Review
Chemistry, Inorganic & Nuclear
James A. Birrell, Patricia Rodriguez-Macia, Edward J. Reijerse, Maria Alessandra Martini, Wolfgang Lubitz
Summary: This review provides an overview of the research history and progress on hydrogenases, focusing on their structure, mechanism of action, and catalytic cycle. It compares the studies on the simple enzyme containing the active site H-cluster and enzymes containing additional iron-sulfur clusters.
COORDINATION CHEMISTRY REVIEWS
(2021)
Article
Biochemistry & Molecular Biology
Esha Sircar, Detcho A. Stoyanovsky, Timothy R. Billiar, Arne Holmgren, Rajib Sengupta
Summary: Intracellular reduced glutathione (GSH) is the most abundant intracellular thiol with concentrations ranging from 1-10 mM, playing a crucial role as a potent cellular antioxidant and denitrosylating agent against redox stress. Our study demonstrates GSH mediated denitrosylation of protein nitrosothiols in HepG2 cells using a unique spin-trapping mechanism and identifies two previously unknown substrates of GSH mediated S-denitrosylation.
NITRIC OXIDE-BIOLOGY AND CHEMISTRY
(2022)
Editorial Material
Cell Biology
Xinyu Gong, Lifeng Pan
Summary: The recruitment of ATG12-ATG5-ATG16L1 complex to phagophore, which is crucial in autophagosome formation, relies on the specific interaction between ATG16L1 and WIPI2. It has been found that ATG16L1 contains two distinct WIPI2-binding sites, WBS1 and the newly identified WBS2, and the binding mechanism between ATG16L1 WBS2 and WIPI2 is conserved across species. The integrity of these two WIPI2-binding sites in ATG16L1 is essential for normal autophagic flux.
Article
Biochemistry & Molecular Biology
Maria J. Ferreira, Tony A. Rodrigues, Ana G. Pedrosa, Luis Gales, Armindo Salvador, Tania Francisco, Jorge E. Azevedo
Summary: Despite high levels of H2O2 in mammalian peroxisomes, cysteine residues in intraperoxisomal proteins remain reduced. The permeability of the peroxisomal membrane to glutathione and the presence of a thiol-disulfide oxidoreductase in the organelle matrix are still unknown. Using an in vitro system, we found that the peroxisomal membrane is permeable to both reduced and oxidized glutathione, and no evidence of a robust thiol-disulfide oxidoreductase was found. Simulations suggest that glutathione plays a crucial role in protecting cysteine residues from oxidation by H2O2.
Article
Biochemistry & Molecular Biology
Ajanta Chatterji, Arne Holmgren, Rajib Sengupta
Summary: Ribonucleotide reductases play a crucial role in DNA synthesis and are essential for maintaining cellular functions. Research suggests that S-glutathionylation can regulate RNR activity, with studies exploring deglutathionylation mechanisms. Additionally, the study revealed the role of S-glutathionylation in DNA damage and repair processes.
MOLECULAR BIOLOGY REPORTS
(2021)
Review
Biochemistry & Molecular Biology
Yuh-Cherng Chai, John J. Mieyal
Summary: This Special Issue aims to advance the understanding of the roles of the GSH/Grx system in cellular homeostasis and disease processes. GSH is the most abundant non-enzymatic antioxidant/nucleophilic molecule in cells. The S-glutathionylation of proteins, a reversible post-translational modification, can act as a regulatory switch in cell signaling and redox homeostasis.
Article
Plant Sciences
Anil Kumar, Varun Kumar, Arvind Kumar Dubey, Mohd Akram Ansari, Shiv Narayan, Meenakshi, Sanoj Kumar, Vivek Pandey, Veena Pande, Indraneel Sanyal
Summary: The over-expression of the CaGrx gene led to elevated activity of glutaredoxin and induced antioxidant enzymes, antioxidants, and stress-responsive amino acids in Arabidopsis plants exposed to drought and salinity. This enhancement in the antioxidant defense system provided tolerance against both stresses, reducing stress markers, enhancing root growth and seed germination, and improving physiological parameters, chlorophylls, and carotenoids. Moreover, the increased activity of the cysteine biosynthesis enzyme led to elevated glutathione biosynthesis, maintaining the ascorbate-glutathione cycle under stress conditions.
PHYSIOLOGY AND MOLECULAR BIOLOGY OF PLANTS
(2021)
Article
Biochemistry & Molecular Biology
Benjamin Selles, Anna Moseler, Damien Caubriere, Sheng-Kai Sun, Morgane Ziesel, Tiphaine Dhalleine, Mathilde Heriche, Markus Wirtz, Nicolas Rouhier, Jeremy Couturier
Summary: This study reports the biochemical relationships between two cytosolic proteins from Arabidopsis thaliana, suggesting a potential unknown pathway of sulfur trafficking in plant cells.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Review
Plant Sciences
Sophie Hendrix, Nathalie Verbruggen, Ann Cuypers, Andreas J. Meyer
Summary: This work provides an overview of the interactions between trace metal homeostasis and heat stress responses in plants. Both deficiency and excess concentrations of trace metals can affect plant growth, development, and defense mechanisms. Heat stress, as a prevalent factor, negatively impacts crop yield and quality, posing a threat to food security. Understanding heat stress responses is crucial for optimizing plant growth and quality under unfavorable temperatures, with trace metals playing an important role in this process.
JOURNAL OF EXPERIMENTAL BOTANY
(2022)
Article
Plant Sciences
Wentao Yang, Philipp Gutbrod, Katharina Gutbrod, Helga Peisker, Xiaoning Song, Anna-Lena Falz, Andreas J. Meyer, Peter Doermann
Summary: In Arabidopsis, degradation of phytol involves alpha-oxidation by AtPAHX and AtHPCL, independent of alpha DOX1/alpha DOX2. Accumulation of phytol metabolites in mutants indicates interference with phytol degradation.
Correction
Biochemistry & Molecular Biology
Philippe Fuchs, Finja Bohle, Sophie Lichtenauer, Jose Manuel Ugalde, Elias Feitosa Araujo, Berivan Mansuroglu, Cristina Ruberti, Stephan Wagner, Stefanie J. Muller-Schussele, Andreas J. Meyer, Markus Schwarzlander
Article
Biochemistry & Molecular Biology
Robin Schumann, Lukas Lang, Marcel Deponte
Summary: This study focuses on the reduction reaction of PfAOP in malaria parasites with hydroperoxides and peroxynitrite, revealing chemical reaction rate constants and thermodynamic parameters through molecular docking and experimental measurements, and pointing out that conformational changes may be the rate-limiting step for the enzyme catalysis.
Article
Biochemistry & Molecular Biology
Marvin Haag, Jessica Kehrer, Cecilia P. Sanchez, Marcel Deponte, Michael Lanzer
Summary: In this study, the redox potential of P. falciparum-infected erythrocytes was measured using parasite-encoded roGFP2 variants. The results showed a sudden shift from a reducing to an oxidizing environment in the infected erythrocytes, which was independent of the presence of hemoglobin S.
Review
Plant Sciences
Damien Caubriere, Anna Moseler, Nicolas Rouhier, Jeremy Couturier
Summary: This review focuses on the biochemical, structural, and physiological roles of cysteine desulfurases in sulfur-dependent biosynthetic pathways in photosynthetic organisms, with particular emphasis on Arabidopsis isoforms. Cysteine desulfurases are highly conserved enzymes that catalyze the extraction of sulfur from cysteine, leading to the formation of persulfide groups on catalytic cysteine residues. The sulfur is then transferred to various targets, including iron-sulfur clusters and molybdenum cofactors. While there is extensive knowledge about cysteine desulfurases in some pathways, such as iron-sulfur cluster synthesis, our understanding of their involvement in other pathways, especially in photosynthetic organisms, is limited. This review summarizes the current knowledge of cysteine desulfurases and highlights gaps in understanding, emphasizing the need for future research in this area.
JOURNAL OF EXPERIMENTAL BOTANY
(2023)
Review
Plant Sciences
Luca Pedroletti, Anna Moseler, Andreas J. Meyer
Summary: Significant efforts have been made to examine the nature of the autonomous iron-sulfur (Fe-S) cluster assembly machinery in mitochondria. The synthesis and assembly of Fe-S clusters occur in two distinct steps, but the transfer and distribution among their respective apoproteins are still not well understood. This review explores the mitochondrial assembly machinery of Arabidopsis and highlights the demand for cluster replenishment and the essential salvage pathway in plant mitochondria.
JOURNAL OF EXPERIMENTAL BOTANY
(2023)
Review
Plant Sciences
Sophie Hendrix, Avilien Dard, Andreas J. Meyer, Jean-Philippe Reichheld
Summary: As sessile organisms, plants are susceptible to climate change, especially increasing temperature variations. They have developed sophisticated signalling mechanisms to respond to these environmental constraints. Reactive oxygen species (ROS) are produced in plants under stress conditions such as high temperatures and play a key role in signalling pathways. ROS can diffuse through cells and membranes, modify cellular redox status, and modulate the functions of target proteins. This review summarizes current knowledge on the functions of ROS and oxidoreductase systems in integrating high temperature signals and activating stress responses and developmental acclimation mechanisms.
JOURNAL OF EXPERIMENTAL BOTANY
(2023)
Article
Chemistry, Physical
Lukas Lang, Ann-Cathrin Wolf, Mareike Riedel, Lea Thibol, Fabian Geissel, Kristina Feld, Jannik Zimmermann, Bruce Morgan, Georg Manolikakes, Marcel Deponte
Summary: 1-Cys Prx is an enzyme that uses only one cysteine residue for the reduction of hydroperoxides, and it requires an external thiol for the reduction of a reactive sulfenic acid. This study compared the reaction mechanisms and kinetics of Prx5 and Prx6 enzymes from Plasmodium falciparum to investigate the hyperoxidation susceptibility and potential substrate promiscuity of 1-Cys Prx.
Article
Biochemistry & Molecular Biology
Eileen Bischoff, Lukas Lang, Jannik Zimmermann, Maximilian Luczak, Anna Maria Kiefer, Gereon Niedner-Schatteburg, Georg Manolikakes, Bruce Morgan, Marcel Deponte
Summary: Dimedone and its derivatives are selective probes for nucleophilic detection of sulfenic acids, but they also react with cyclic sulfenamides. Glutathione outcompetes dimedone as a nucleophile by several orders of magnitude. Therefore, the selectivity of dimedone labeling of cysteinyl residues inside living cells is challenged.
FREE RADICAL BIOLOGY AND MEDICINE
(2023)
Letter
Plant Sciences
Philippe Fuchs, Elisenda Feixes-Prats, Paulo Arruda, Elias Feitosa-Araujo, Alisdair R. Fernie, Christopher Grefen, Sophie Lichtenauer, Nicole Linka, Ivan de Godoy Maia, Andreas J. Meyer, Soeren Schilasky, Lee J. Sweetlove, Stefanie Wege, Andreas P. M. Weber, A. Harvey Millar, Olivier Keech, Igor Florez-Sarasa, Pedro Barreto, Markus Schwarzlaender
Summary: UCP2 is localized to the Golgi, unlike its close homolog UCP1, which is abundant in the mitochondria.
Article
Biochemistry & Molecular Biology
Philippe Fuchs, Finja Bohle, Sophie Lichtenauer, Jose Manuel Ugalde, Elias Feitosa Araujo, Berivan Mansuroglu, Cristina Ruberti, Stephan Wagner, Stefanie J. Mueller-Schuessele, Andreas J. Meyer, Markus Schwarzlaender
Summary: Redox processes are essential for cellular functions, and mitochondria play a key role in enhancing tolerance to reductive stress. The study on Arabidopsis mutants reveals that mitochondrial respiratory flexibility and retrograde signaling regulate mitochondrial respiratory capacity to aid cells in tolerating thiol-mediated reductive stress.
Article
Biochemistry & Molecular Biology
Zechariah Haber, Nardy Lampl, Andreas J. Meyer, Einat Zelinger, Matanel Hipsch, Shilo Rosenwasser
Summary: This study investigated the dynamics of chloroplastic glutathione redox potential in Arabidopsis, revealing fluctuations in oxidation levels in response to changing light intensities. It identified two regulated oxidative states of chl-E-GSH and suggested a role for PSI photoinhibition in regulating these dynamics. The findings also highlighted the link between daytime photoinhibition and nighttime GSH metabolism.