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Review
. 2019 Feb 18:10:166.
doi: 10.3389/fpls.2019.00166. eCollection 2019.

Consequences of Oxidative Stress on Plant Glycolytic and Respiratory Metabolism

Sébastien Dumont  1 , Jean Rivoal  1
Affiliations
Review

Consequences of Oxidative Stress on Plant Glycolytic and Respiratory Metabolism

Sébastien Dumont et al. Front Plant Sci. .

Abstract

Reactive oxygen species (ROS) and reactive nitrogen species (RNS) are present at low and controlled levels under normal conditions. These reactive molecules can increase to high levels under various biotic and abiotic conditions, resulting in perturbation of the cellular redox state that can ultimately lead to oxidative or nitrosative stress. In this review, we analyze the various effects that result from alterations of redox homeostasis on plant glycolytic pathway and tricarboxylic acid (TCA) cycle. Most documented modifications caused by ROS or RNS are due to the presence of redox-sensitive cysteine thiol groups in proteins. Redox modifications include Cys oxidation, disulfide bond formation, S-glutathionylation, S-nitrosylation, and S-sulfhydration. A growing number of proteomic surveys and biochemical studies document the occurrence of ROS- or RNS-mediated modification in enzymes of glycolysis and the TCA cycle. In a few cases, these modifications have been shown to affect enzyme activity, suggesting an operational regulatory mechanism in vivo. Further changes induced by oxidative stress conditions include the proposed redox-dependent modifications in the subcellular distribution of a putative redox sensor, NAD-glyceraldehyde-3P dehydrogenase and the micro-compartmentation of cytosolic glycolytic enzymes. Data from the literature indicate that oxidative stress may induce complex changes in metabolite pools in central carbon metabolism. This information is discussed in the context of our understanding of plant metabolic response to oxidative stress.

Keywords: S-glutathionylation; S-nitrosylation; TCA cycle; glycolysis; oxidative stress; plant; redox post-translational modifications; respiration.

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Figures

FIGURE 1
FIGURE 1
Different redox modifications of protein Cys thiols and their reversibility. Protein thiol oxidation can lead to a variety of redox modifications. The scheme presents the relations between the different redox modifications and the reversibility of these modifications. Sulfonic acid (–SO3H) formation is considered to be irreversible as well as sulfinic acid (–SO2H) except in the case of certain peroxiredoxins which sulfinic acid Cys residue can be reduced by sulfiredoxin using and ATP-dependent mechanism. See text for details. ROS, reactive oxygen species; RNS, reactive nitrogen species; H2S, hydrogen sulfide; GSSG, oxidized glutathione; GSH, reduced glutathione; ASC, ascorbate; GRX, glutaredoxin; TRX, thioredoxin; SRX, sulfiredoxin; R-SH, reduced thiol; R-S-, thiolate anion; R-SOH, sulfenic acid; R-SNO, protein S-nitrosylation; R-SSG, protein S-glutathionylation Cys; R-SSH, protein S-sulfhydration; R-SS-R, disulfide bond.
FIGURE 2
FIGURE 2
Impact of oxidative stress on glycolytic and TCA cycles enzymes activity. Enzymes which activity has been shown to be affected by redox modification are shown in a metabolic scheme that also includes subcellular localization. Red and green, respectively, indicate inhibition and activation under oxidative conditions. Enzymes and metabolites abbreviations: FBA, fructose-1,6-bisphosphate aldolase; TPI, triosephosphate isomerase; GapC, glyceraldehyde 3-phosphate dehydrogenase; Eno2, enolase 2; ADH, alcohol dehydrogenase; ACO, aconitase; IDH, isocitrate dehydrogenase; MDH, malate dehydrogenase; FUM, fumarase; CSY, citrate synthase. Metabolites: F1,6P, fructose-1,6-bisphosphate; DHAP, dihydroxyacetone phosphate; G3P, glyceraldehyde 3-phosphate; 1,3DPGA, 1,3-bisphosphoglycerate; 2-PGA, 2-phosphoglycerate; PEP, phosphoenolpyruvate; ACH, acetaldehyde; ETOH, ethanol.
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