ferredoxin glutathione reductase The System: A Journey from Cyanobacteria to Higher Eukaryotes is made up of highly conserved domains such as two Rossmann fold domains Thioredoxin and Glutaredoxin Systems as – where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Ferredoxin—NADP(+) reductase - Wikipedia

Name: ferredoxin glutathione reductase The System: A Journey from Cyanobacteria to Higher Eukaryotes is made up of highly conserved domains such as two Rossmann fold domains Thioredoxin and Glutaredoxin Systems as – where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Ferredoxin—NADP(+) reductase - Wikipedia
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FerredoxinNADP(+) reductase Wikipedia Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling ferredoxin glutathione reductase Thioredoxin and Glutaredoxin Systems as Potential Targets for the Development of New Treatments Generation and scavenging of superoxide radical and hydrogen peroxide, Download Scientific Diagram The role of glutathione reductase and related enzymes on cellular redox homoeostasis network ScienceDirect

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This reduction, combined with enrichment analysis revealing alterations in tryptophan metabolism, is consistent with growing experimental evidence showing a significant dysregulation of the tryptophan-kynurenine pathway in PD 34,35