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Fig. 38 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 38. Reduction of (9S,13S)-12-oxophytodienoic acid by 12-oxophytodienoic acid reductase 3. The preferred electron donor for this reaction is NADH, which is also the case for most old yellow enzyme homologs characterized thus far. Although the exact role of the other homologs in plant biochemistry is currently unknown, we hypothesize that they carry out similar C– –C-bond reductions in as yet unidentified substrates.
Fig. 32 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 32. Last step in abscisic acid biosynthesis catalyzed by abscisic aldehyde oxidase. Note that substrate oxidation occurs at the Moco and electrons are transferred to the FAD cofactor via two iron-sulfur-clusters, i.e. the same reaction mechanism as found in xanthine dehydrogenase. Reoxidation of reduced FAD occurs by dioxygen generating hydrogen peroxide.
Fig. 31 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 31. Reaction of zeaxanthin epoxidase. The enzyme catalyzes the consecutive epoxidation (monooxygenation) of both β-ionone rings in all-trans- zeaxanthin at the expense of reduced NAD(P)H. Dioxygen is cleaved during the reaction with one oxygen atom introduced into the substrate and the other one being released as water.
Fig. 26 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 26. Reaction catalyzed by protoporphyrinogen IX oxidase. The conversion of protoporphyrinogen IX to protoporphyrin IX, the last common step in heme and chlorophyll biosynthesis, requires three consecutive two-electron oxidations. Regeneration of the reduced FAD cofactor occurs by reoxidation with dioxygen leading to the production of hydrogen peroxide.
Fig. 21 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 21. Oxidation of L-aspartate to iminoaspartate initiates NADþ biosynthesis. The reduced FAD cofactor is reoxidized by dioxygen or fumarate leading to the production of either hydrogen peroxide or succinate (not shown).
Fig. 19 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 19. Reaction catalyzed by squalene epoxidase. The reducing equivalents are delivered by NADPH, and therefore, the enzyme was assigned to subclass A of flavin-dependent monooxygenases (Paul et al., 2021). Similar to zeaxanthine epoxidase the enzyme forms an unusual epoxide (see Fig. 31).
Fig. 18 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 18. Reaction catalyzed by dihydrooroate dehydrogenase. In the pyrimidine-half reaction the FMN cofactor is reduced by transfer of a hydride to the N(5)-position of the isoalloxazine ring (highlighted in red) followed by proton abstraction from the 5-position of dihydroorotate. A. thaliana dihydrooroate dehydrogenase belongs to the class 2 enzymes that are localized in the inter membrane space and associated with the inner mitochondrial membrane. Thus, reoxidation occurs by two successive one-electron transfer steps from the reduced FMN to CoQ (shown here as a single step). For a detailed discussion on the reaction mechanism see Palfey (2013). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 35 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 35. Reaction catalyzed by 3-β-hydroxysterol Δ24-reductase. The top reaction shows the formal reduction of the side chain double bond in the conversion of 24-methylenecholesterol to campesterol. The middle and bottom reactions depict the reduction of different side chains as present in isofucosterol, dolichosterone and 6-deoxodolichosterone. In the case of the human ortholog, NADPH serves as the reducing agent for the reduction of the FAD (Waterham et al., 2001).
Fig. 27 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 27. Reaction of 7-hydroxymethyl chlorophyll a reductase. Based on the structure of the enzyme, ferredoxin serves as the electron donor for a proton-activated electron transfer pathway (for mechanistic details see Wang and Liu, 2016). The hydroxymethyl-group subjected to reduction is highlighted in red. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 37 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 37. Reaction of cytokinin dehydrogenase. Note that the electron acceptor for the reoxidation of the covalently bound FAD cofactor remains unknown. However, quinones efficiently oxidize the reduced FAD, and thus, are likely candidates as electron acceptors, at least for some of the cytokinin dehydrogenases (Fr´ebortov´a et al., 2004).
Fig. 39 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 39. Reaction catalyzed by indole cyanohydrin oxidase (AtBBE3/ FOX1). The product of the reaction is further hydroxylated to 4-hydroxyindole- 3-carbonyl nitrile, a cyanogenic metabolite involved in pathogen defense. According to the analysis by (Zafred et al., 2015), the enzyme should be able to react with dioxygen directly and thus the reoxidation of the reduced FAD would produce hydrogen peroxide (see also discussion below).
Fig. 30 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 30. Reaction of lycopene cyclases in A. thaliana. Lycopene ε-cyclase generates a single ε-ring, whereas the β-cyclase introduces two β-rings at both ends of the all-trans lycopene. The β-cyclase may also add a β-ring at the 1′-end of δ-carotene (not shown). All of these reactions employ reduced FAD as the catalytically active cofactor, which is probably generated at the expense of NAD (P)H, similar to carotene cis-trans isomerase (see Fig. 29).
Fig. 17 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 17. Reduction of 5,10-methylene tetrahydrofolate to 5-methyl-tetrahydrofolate by methylenetetrahydrofolate reductase. In the plant enzyme, NADH is used to reduce the FAD cofactor. The reaction proceeds via hydride transfer, probably to the carbon (highlighted in red) and subsequent protonation of the nitrogen (reductive cleavage). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 34 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 34. Postulated reaction catalyzed by indole-3-butyryl-CoA dehydrogenase. This conversion of indole-3-butyryl-CoA to indole-3-butenoyl-CoA constitutes the first step toward the release of indole-3-acetic acid from indole butyric acid through side chain shortening. Due to its peroxisomal localization, it is likely that reoxidation of the reduced FAD is achieved by direct reaction with dioxygen to yield hydrogen peroxide (Zolman et al, 2007, 2008).
Fig. 16 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 16. Reaction catalyzed by chorismate synthase. The 1,4-anti-elimination of the 6(proR)-hydrogen and phosphate converts 5-enolpyruvylshikimate 3-phosphate to chorismate, the final metabolite of the common shikimate pathway. In the case of bacteria and plants, the required reduced FMN is probably produced by unidentified NAD(P)-dependent FMN reductases and then taken up by chorismate synthase.
Fig. 15 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 15. Reactions catalyzed by glutamate synthase. In the first reaction step, catalyzed by the glutaminase, ammonia is released from the amide group of L-glutamine yielding L-glutamate (top reaction). The ammonia (shown in red) then attacks the keto group of α-ketoglutarate to form an imine intermediate (bottom reaction), which is then reduced by FMN, as shown on the right side. Note that two molecules of L-glutamate are generated, one as a result of the glutaminase reaction and another one as a result of the glutamate synthase reaction. In plants, the FMN cofactor is either reduced by NADH or reduced ferredoxin (see also text for references). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 13 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 13. Reaction of farnesylcysteine lyase. In the first step the proS- hydrogen (shown in red) is transferred as a hydride to the FAD cofactor, which is reoxidized by dioxygen to yield hydrogen peroxide as a by-product. The thiocarbenium is nucleophilically attacked by water generating a hemithioacetal intermediate, which subsequently decomposes to the products farnesal and L-cysteine. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 12 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 12. Back-conversion reactions catalyzed by FAD-dependent polyamine oxidases. The oxidative cleavage of spermine to putrescine occurs in two consecutive steps via spermidine. In the initial oxidation of the -N-C-bond to the imine, the FAD cofactor is reduced and reoxidation occurs by direct reaction with dioxygen producing hydrogen peroxide. The imine is subsequently hydrolyzed to the amine and the aldehyde products.
Fig. 10 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 10. α,β-dehydrogenation of acyl-CoA derivatives as the first step of fatty acid degradation (β-oxidation). Note that the reduced FAD is directly reoxidized by dioxygen to yield hydrogen peroxide. The peroxisomal acyl-CoA oxidases catalyze the first step in β-oxidation by mediating the dehydrogenation of acyl-CoAs of different chain lengths to the corresponding enoyl-CoAs.
Fig. 8 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 8. Reaction catalyzed by D-2-hydroxyglutarate dehydrogenase. The oxidation of D-2-hydroxyglutarate yields α-ketoglutarate and reduced FAD. As a client of ETF, the electrons of the reduced FAD are eventually transferred to the mitochondrial mETC via ETF-QO.
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