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Oxidoreducatses occupy one-third of all enzymatic activities registered in the BRaunschweig ENzyme DAtabase (BRENDA). This group of enzymes are playing a vital role in plant growth and metabolism. Oxidoreducatses (EC 1) is the largest class of enzyme that includes dehydrogenases, oxygenase, peroxidise, oxidases and other enzymes that catalyse oxidation–reduction reaction by transferring electrons, hydrogen, or oxygen from a reductant molecule to an oxidant molecule. These enzymes play an important role in photosynthesis, aerobic and anaerobic respiration, amino acid metabolism and fatty acid metabolism. Besides metabolism these enzymes are also involve in providing defence against pathogens by activating signal transduction pathways. Here we have discussed in details about the sub-classes of oxidoreductase ezymes according to the reaction they catalyse and their importance in metabolism and defence against plant pathogen attack.
Department of Biotechnology, MSSSoA, Centurion University of Technology and Management, India
Priyabrata Sen
Department of Agricultural Biotechnology, Assam Agricultural University, Jorhat, India
*Address all correspondence to: panchashreedas@gmail.com
1. Introduction
Enzymes facilitate the biochemical reaction by lowering down the activation energy. In biochemistry, the enzymes are classified in six major classes according to the biochemical reaction it catalyses or the substrate it uses. Each class of the enzyme is named by the International Union of Biochemistry and Molecular Biology through EC (Enzyme Commission) number. Oxidoreductases are the enzymes that involved in different parts of natural lifecycle such as plants, animals and microorganisms. In plant biochemistry, oxidoreductase is the large group of enzymes having EC 1 nomenclature and it catalyses the oxidation and reduction reactions in plants. It mainly involves in transfer of electron molecule from one molecule (electron donor or reductant) to another (electron acceptor or oxidant). The oxidoreductases includes oxidase, oxygenase, peroxidase, dehydrogenase and other enzymes that catalyse biochemical reactions that involves in insertion of oxygen, transfer of hydride ions, transfer of electrons and protons [1]. These enzymes mainly utilise FAD (flavin adenine dinucleotide), Fd (ferredoxin) FMN (flavin mononucleotide), NAD (nicotinamide adenine dinucleotide), NADP (nicotinamide adenine dinucleotide phosphate), Coenzyme B, Coenzyme Q etc. for catalysing biochemical reactions in living cells [2]. Plants mainly use this class of enzymes for the metabolism process such as synthesis or degradation of biomolecules to sustain throughout the life span. In case of plants these enzymes also involves in metabolism of exogenous molecules such as herbicides [3]. The oxidoreductases have important roles in aerobic as well as anaerobic respiration, photosynthesis, electron transport chain, pentose phosphate pathway and photorespiration [4]. These enzymes also involve in amino acid metabolism. Oxidoreductases present in plant plasma membrane involves in maintaining the redox potential through proton pumping, nutrient uptake regulation, regulation of ion channels, reduction of iron and regulation of ion channels. Some oxidoreductase enzymes are also involved in signal transduction pathways and poses defence against pathogen attack.
This large group of enzyme comprises with number of enzymes that catalyses the transmission of electron from a donor (reduction) to an acceptor (oxidation) molecules with the help of cofactors to facilitate metabolism and provide defence against pathogens in plants (Table 1) [5]. In this review we mainly focused on the classification of oxidoreductase enzymes and their role in metabolism and defence in plants.
EC number
Description
Example
EC 1.1
Act on the CH-OH group of donors- The enzymes act on primary alcohols, secondary alcohols and hemi-acetals
Act on the aldehyde or oxo group of donors- The enzymes oxidise aldehydes to the corresponding acid. The oxo group of aliphatic compounds can be oxidised by addition of water and cleavage of a carbon–carbon bond and for aromatic compounds it can be done by addition of the elements of water and dehydrogenation.
Act on the CH-CH group of donors- The enzyme catalyses chemical reactions that introduce a double-bond into the substrate by direct dehydrogenation at a carbon–carbon single bond
Act on single donors with incorporation of molecular oxygen- It contains oxygenases that catalyses the incorporation of molecular oxygen to the substrate
Act on paired donors, with incorporation or reduction of molecular oxygen- The subclass includes enzymes that act on two hydrogen donors and oxygen is incorporate into one or both of the donors during biochemical reaction.
It contains enzymes acting on superoxide as acceptor with a single sub-subclass
Superoxide dismutase, superoxide reductase
EC 1.16
Oxidising metal ions- The enzymes of this subclass involve in oxidising metal ions to higher valency state
Mercury(II) reductase, aquacobalamin reductase
EC 1.17
Act on CH or CH2 groups- The enzymes of this subclass involve in oxidative conversion of the -CH2- group of donors to -CHOH- (or -CH- to -COH-) and sugars to deoxysugars.
Oxidoreductase is having biological importance due to its abundance in the living organisms. This large class of enzyme is classified in several subclasses according to the reaction it catalyses, the three dimensional structure. These enzymes can be either oxidases or dehydrogenases. The oxidases utilises molecular oxygen as electron or hydrogen acceptor and dehydrogenases acts as electron or hydrogen donor for the NAD+/NADP+ or a flavin enzymes. The other subclasses of oxidoreductases include peroxidases, hydroxylases, oxygenases, and reductases. Peroxidases catalyse the reduction of hydrogen peroxide in peroxisome. Hydroxylases mainly acts by adding hydroxyl groups to its substrates. Oxygenases involves in incorporating molecular oxygen into organic substrates. Reductases mostly act as oxidases involves in reduction reaction. All of the enzymes belonging to this class are playing essential role in plant lifecycle and stress signalling.
The oxidoreducatase enzymes are securing EC 1 in the enzyme classification given by the International Union of Biochemistry and Molecular Biology and it is having 24 sub-classes [6].
3.1 Oxidoreductase enzymes involved in photosynthesis
Photosynthesis is the most important biochemical process completed in chloroplast of plant cell for conversion of light energy into chemical energy. In this process the green plants absorbs light energy, water (H2O) and carbon dioxide (CO2) to form oxygen and energy-rich organic compound. The photosystem I (PS I) and photosystem II (PS II) are involved in the light reaction of photosynthesis. PS II liberates the hydrogen molecules from water at the time of photolysis and frees molecular oxygen. After that the liberated electrons in this process are transferred to plastoquinol, Cytochrome b6 complex and finally to plastocyanin. At this point the PS I take electrons from plastocyanin and transfer it to iron-containing compound ferredoxin. Upon taking the electrons, ferredoin becomes reduced ferredoxin. The Ferredoxin-NADP+ reductase, an enzyme belongs to the class oxidoreductase, catalyses the biochemical reaction of formation of NADPH from NADP+(Nicotinamide adenine dinucleotide phosphate) during photosynthesis [7, 8]. The enzyme Ferredoxin-NADP+ reductase transfer an electron from each of two reduced ferredoxin molecules to a single molecule of the two electron carrier NADPH and after completion of the reaction ferredoxin becomes oxidised (Figure 1). This FNR enzyme utilises a flavin cofactor FAD (flavin adenine dinucleotide), the iron–sulphur protein ferredoxin as donor and NADP+ as acceptor.
Figure 1.
Chemical reaction catalysed by FNR (Ferredoxin-NADP+ reductase).
Plants utilise Ferredoxin-Thioredoxin reductase (FTR), a member of oxidoreductase class of enzymes, to regulate the carbon fixation in photosynthetic organisms [9]. FTR helps the plants to regulate the carbohydrate metabolism based on availability of light. During day light the FTR reduces oxidised thioredoxin by reduced ferredoxin. This reduced thioredoxin activates certain carbohydrate synthesis enzymes such as chloroplast fructose-1,6-bisphosphatase, Sedoheptulose-bisphosphatase and phosphoribulokinase by cleaving disulfide bonds in enzymes [10]. This leads to carbohydrate synthesis during day time. At night, the ferredoxin remains oxidised and thus it cannot activate thioredoxin to promote carbohydrate biosynthesis and breakdown of carbohydrate starts (Figure 2).
Figure 2.
Chemical reaction catalysed by FTR (Ferredoxin-Thioredoxin reductase).
3.2 Oxidoreductase enzymes involved in chlorophyll biosynthesis
The chlorophyll biosynthesis is a fundamental metabolic process as it is the most important pigment for photosynthesis. The enzyme protochlorophyllide oxidoreductase (POR), a member of oxidoreductase classes of enzyme, is a key regulatory enzyme for chlorophyll biosynthesis that catalyses the light-induced reduction of protochlorophyllide (PChlide) into chlorophyllide (Chlide) in the presence of NADPH (reduced form of NADP) [11, 12, 13, 14]. The enzyme POR utilises NADPH (reduced nicotinamide adenine dinucleotide phosphate) as cofactor [11, 12, 13, 14]. There are two or more isoforoms of this POR enzyme has been identified in different plant species. In barley (Hordeum vulgare), POR A and POR B, the two distinct isozymes of POR are present [15]. Arabidopsis (Arabidopsis thaliana) is having three distinct isozymes of POR such as POR A, POR B and POR C [16, 17].
3.3 Oxidoreductase enzymes involved in glycolysis
Glycolysis is the carbohydrate catabolism pathway that converts glucose into pyruvate and produces NADH (reduced nicotinamide adenine dinucleotide) and ATP (adenosine triphosphate). This process contains two phases, preparatory phase and pay-off phase. In the first phase, glucose breaks down to form two trios sugar. So in the second phase of glycolysis each reaction occurs twice for each glucose molecule. In the pay-off phase Glyceraldehyde 3-phosphate dehydrogenase catalyses the oxidative conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate (1,3-BPG) and reduces NAD+ to NADH (Figure 3a). For maintaining the redox state of the cell there has to be a proper balance between NAD+/NADH. For aerobic respiration the oxidation of NADH occurs during tricarboxylic acid cycle (TCA) and for fermentation it occurs at the time of conversion of pyruvate to lactate by lactate dehydogenase enzyme (Figure 3b).
Figure 3.
Chemical reaction catalysed by oxidoreductase enzymes in glycolysis. (a) Chemical reaction catalysed by Glyceraldehyde 3-phosphate dehydrogenase. (b) Chemical reaction catalysed by lactate dehydrogenase.
3.4 Oxidoreductase enzymes involved in TCA cycle (Tricarboxylic acid cycle)
Tricarboxylic acid cycle (TCA) consists of a series of enzyme catalysed biochemical reactions. The precursor of TCA cycle comes from carbohydrate, protein and fats [18]. The product of glycolysis, pyruvate converts in acetyl-CoA to enter in TCA cycle. Except leucin and lysine, the other amino acids degraded to TCA cycle intermediates. Trough beta-oxidation of fatty acid, it converted into acetyl-CoA that enters into TCA cycle. During TCA cycle, a large number of NADH and FADH molecules are produced by different oxidoreductase enzymes [19]. Pyruvate dehydrogenase catalyses the conversion of pyruvate to acetyl-CoA that enter in the TCA cycle (Figure 4a). Isocitrate dehydrogenase involves in oxidative decarboxylation of isocitrate to α-ketoglutarate (Figure 4b). Another TCA cycle enzyme α-ketoglutarate dehydrogenase catalyse the generation of succinyl-CoA from α-ketoglutarate through oxidative decarboxylation (Figure 4c). Succinate dehydrogenase involves in oxidative conversion of succinate to fumarate (Figure 4d). Malate dehydrogenase enzyme of TCA cycle catalyses the conversion of malate to oxaloacetate through oxidation (Figure 4e).
Figure 4.
Chemical reaction catalysed by oxidoreductase enzymes in TCA cycle. (a) Chemical reaction catalysed by pyruvate dehydrogenase. (b) Chemical reaction catalysed by isocitrate dehydrogenase. (c) Chemical reaction catalysed by α-ketoglutarate dehydrogen. (d) Chemical reaction catalysed by succinate dehydrogen. (e) Chemical reaction catalysed by malate dehydrogen.
3.5 Oxidoreductase enzymes involved in ETC (electron transport chain) and Oxidative phosphorylation
Oxydative phosphorylation involves flow of electrons from a series of proteins and electron carriers within the mitochondrial membrane by ETC. Several biochemical reactions like glycolysis, TCA cycle, fatty acid oxidation and amino acid oxideation yields high energy-rich molecules NADH (reduced nicotinamide adenine dinucleotide) and FADH2 (reduced flavin adenine dinucleotide). This NADH and FADH2 have pair of electron with high transfer potential. In ETC the electrons of NADH and FADH2 are transferred to molecular oxygen through a series of electron carriers and the energy produced during this process leads to formation of ATP [20]. Different subclasses of oxidoreductase enzymes catalyse the oxidative phosphorylation reactions (Figure 5). The electron transport chain is consists of four complexes. NADH:quinone oxidoreductase or NADH dehydrogenase (complex I) contains FMN that accepts electrons and H+ from NADH and forms FMNH2. It also contains iron–sulphur protein that helps in transfer of electrons and H+ to Coenzyme Q. Succinate:quinine oxidoreductase or succinate dehydrogenase (complex II) contains iron and a bound FAD cofactor to oxidise succinate to fumarate and reduces ubiquinone. Coenzyme Q collects the electrons from complex I and Complex II and transfers them to complex III. Quilon:cytochrome c oxidoreductase (complex III) contains heme group, in which Fe3+ accepts electrons from Coenzyme Q (CoQ) to form Fe2+ and transfers the electrons to cytochrome C (CytC), that transfers the electrons to complex IV. Cytochrome C:oxygen oxidoreductase, an aa3-type enzyme (complex IV) contains heme group in which Fe3+ accepts electrons from cytochrome C to form Fe2+ and transfers electrons to oxygen that combines with hydrogen to form water molecule [21].
Figure 5.
Enzyme complex involved in ETC in mitochondria.
3.6 Oxidoreductase enzymes involved in amino acid metabolism
Amino acid dehydrogenases are involved in amino acid catabolism reaction [22]. This enzyme utilises NAD(P)+ as cofactor. Amino acid dehydrogenases catalyse the biochemical reaction by transferring the hydride from the Cα atom of an amino acid to NAD(P)+ and forms intermediate α-imino acid that finally hydrolyzed to α-keto acid and ammonium (Figure 6). Glutamate dehydrogenase and phenylalanine dehydrogenase are involved in oxidative deamination reaction for amino acid catabolism [23, 24]. Glutamate dehydrogenase and phenylalanine dehydrogenase catalyse deamination reaction of glutamate and phenylalanine respectively [23, 24].
Figure 6.
Chemical reaction catalysed by amino acid dehydrogenase.
3.7 Oxidoreductase enzymes involved in fatty acid metabolism
Oxidoreductase enzymes are involved in metabolism of fatty acids, especially in β-oxidation. The β-oxidation procedure of fatty acid catabolism occurs in cytoplasm of cell. Activation of acyl-CoA by acyl-CoA synthetases is seen to initiate β-oxidation in the membrane of the peroxisome [25, 26, 27]. The β-oxidation procedure of fatty acid catabolism occurs in cytoplasm of cell. The products of this pathway are acetyl-CoA, NADH and FADH. The pathway needs enzymes like acyl-CoA dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase that belongs to the oxidoreductase classes of enzyme [28]. Acyl-CoA dehydrogenases (ACAD) catalyse the oxidation of acyl-CoA to trans-2-enoyl-CoA with the help of FAD [25]. β-ketoacyl-ACP reductase and enoyl-ACP reductase are involved in de novo synthesis of fatty acid synthase are belongs to oxidoreductase class of enzymes [29]. NAD+ oxidoreductase is involved in α-oxidation in plants [30]. Acyl-CoA oxidases (ACOX) catalyse the oxidation of acyl-CoA to trans-2-enoyl-CoA [25].
4. Oxidoreductase enzymes involved in plant defence mechanism
The oxidoreductases involved in defence mechanism of plants are typically helping in ROS (reactive oxygen species) generation. In reaction to stressors, ROS serve as signalling molecules and activate signal transduction pathways. Accumulation of ROS (reactive oxygen species) at the site of pathogen infection leads to hypersensitive response that causes death of plant tissue at the site of infection to restrict further spread of pathogen infection [31, 32]. The pathogenesis-related (PR) genes are expressed more frequently as part of the hypersensitive response (HR), which also comprises the production of antimicrobial secondary metabolites and a type of localised cell death (LCD) at the infection site. Since electron utilisation in the chloroplast stroma shuts down during the HR, the photosynthetic electron transport chain undergoes excessive reduction, which is the initial contributor to ROS. The generation of ROS molecules are catalysed by NADPH-dependent oxidase system. In plants this system generates superoxide anion (O2−) and hydrogen peroxide (H2O2) in response to pathogen attack [33, 34]. Like NADPH-dependent oxidases, Germin-like oxalate oxidases, glycolate oxidases, Amine oxidases, class III peroxidise which belong to oxidoreductase class of enzymes are involve in ROS generation in response to pathogen attack [35, 36, 37, 38, 39]. All the enzymes associated with ROS production belongs to the class of oxidoreductase of enzyme [40].
The ROS are generated by cell organelles like chloroplast, mitochondria and peroxisome as by-product of aerobic respiration. The main parts of cells that are involved into generation of H2O2 are Cytoplasm, plasma membrane, apoplasts, endoplasmic reticulum, and extracellular matrix. H2O2 is a by-product of several metabolic pathways like glycolate oxidase reaction, fatty acid β-oxidation, electron transport chain, oxidative phosphorylation, transition metal ions, thymidine, and polyamine catabolism etc. [41, 42, 43, 44]. Enzymatic activities of plasma-membrane-localised NADPH oxidases, amine oxidases, and cell wall peroxidises are playing major role in ROS production [45].
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) are both significant signals in plants and vital regulators of a number of activities, including metabolism, growth and development, response to abiotic and biotic stressors, solute transport, autophagy, and programmed cell death (PCD). ROS plays a crucial role as signalling molecule in defence mechanism as well as in developmental process in all plants [46, 47, 48]. During biotic stress and abiotic stress condition, the cellular homeostasis of plants is disrupted and this lead towards higher production ROS [45, 46]. Increasing concentration of ROS can become a threat for living cell as it can lead to cell death. ROS may damage nucleic acids, proteins and activate apoptasis. So, high level of co-ordination between signalling and metabolic pathways for producing and scavenging ROS is needed during a stress condition is needed [44, 45].
The plant-pathogen interaction also involves generation of reactive nitrogen species (RNS) (NO, NO+, NO−, NO2 and ONOO−) at the site of infection [35]. This also acts as a signalling molecule during stress condition. ROS and RNS together involve in hypersensitive response as well as programmed cell death responses during pathogen infection [49].
Under normal condition, cellular concentration of ROS and RNS is low in plants. But during stress condition, both ROS and RNS act as a signalling molecule to activate plant defence responses against the stress. The rapid production of ROS develops oxidative stress to the plants. A high concentration of ROS and RNS can lead to cell death. To minimise the toxic action of ROS, plants posses antioxidant activities [33]. It is very much needed to maintain the equilibrium between production and metabolism of ROS and RNS. The detoxification of these substances is done enzymatic as well as non-enzymatic antioxidants [42]. Each and every cell compartments are having their own mechanism of scavenging excess amount of ROS and RNS.
The nonenzymatic antioxidants like ascorbate, glutathione, tocopherol etc. can directly detoxify ROS or reduce substrate for antioxidant enzymes. Ascorbate is an important compound to directly eliminate singlet oxygen and super oxide ions. Ascorbate also involves in reduction of H2O2 to water through ascorbate–glutathione cycle [50]. ROS oxidised glutathione to form oxidised glutathione. Glutathione and oxidised glutathione helps in maintaining redox balance of cellular components [42, 51]. α-tocopherol detoxifies peroxyl ions (HO2) in lipid bilayer and chloroplast membrane [52].
The enzymatic antioxidants like superoxide dismutase, catalase, peroxiredoxins and peroxidases are involved in ROS degradation. Superoxide dismutase catalyses the formation of molecular oxygen and hydrogen peroxide from super oxide anions. Catalase detoxifies H2O2 to water. The enzymes involved in ascorbate–glutathione cycle, i.e. glutathione reductase (GR), dehydroascorbate reductase (DHAR), monohydroascorbate reductase (MDAR) and ascorbate peroxidise (APX) help in generating soluble antioxidants [53]. In plants, the most important ROS scavenging mechanism is ascorbate–glutathione cycle [42].
The oxidoreductase enzymes involved in plant growth and defence against stress are enlisted in Tables 2 and 3.
Sl. no.
Plants
Gene
Stress condition
Reference
1.
Tea (Camellia sinensis)
glutathione S-transferase
pathogen and insect attack, cold spells, drought and salt stresses, nitrogen nutrition
Oxidoreductase is the largest class of enzyme that includes several enzymes having importance in plant metabolism as well as defence mechanism. Number of metabolic pathways like chlorophyll biosynthesis, photosynthesis, glycolysis, fatty acid metabolism, tricarboxylic acid cycle includes oxidoreductase enzymes that utilises NAD, FAD, or NADP as a cofactor (Figure 7). This large class of enzyme contributes in developing plant defence responses against biotic and abiotic stress. Antioxidant enzymes maintain redox balance in cellular components in stress condition.
Figure 7.
Summary of role of different oxidoresductases in plant metabolism and defence.
PD would like to acknowledge Department of Agricultural Biotechnology, Assam Agricultural University and Centurion University of Technology and Management for the support. PS would like to acknowledge Department of Agricultural Biotechnology, Assam Agricultural University for the support.
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Written By
Panchashree Das and Priyabrata Sen
Submitted: 29 April 2023Reviewed: 21 June 2023Published: 06 February 2024
Open access peer-reviewed chapter
