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Sulfite Reductase (NADPH)Oxidoreductases Acting on Sulfur Group DonorsSulfite Reductase (Ferredoxin)Hydrogensulfite ReductaseSulfitesSulfite OxidaseThiosulfatesDesulfovibrio vulgarisSulfatesSulfur-Reducing BacteriaOxidoreductasesNADPH OxidaseSulfurDeltaproteobacteriaSulfidesDesulfovibrioSulfite DehydrogenaseOxidation-ReductionNADPNitrate ReductasesChromatiumChromatiaceaeHydroxymethylglutaryl CoA ReductasesIron-Sulfur ProteinsMetalloproteinsRibonucleotide ReductasesMolecular Sequence DataThermoproteaceaeNADH, NADPH OxidoreductasesNitrite ReductasesCytochrome-B(5) ReductaseThermococcalesHemeFerredoxin-NADP ReductaseGlutathione ReductaseFerredoxinsFMN ReductaseElectron Spin Resonance SpectroscopyThioredoxin-Disulfide ReductaseCytochrome ReductasesAmino Acid SequenceNADPH-Ferrihemoprotein ReductasePhylogenyGeologic SedimentsElectron TransportEscherichia coliAnaerobiosisKineticsSpectrophotometryDNA, BacterialSequence Analysis, DNAMolybdenumArchaeaTetrahydrofolate DehydrogenaseRNA, Ribosomal, 16SBase SequenceGenes, BacterialMethaneCloning, MolecularCysteineNitrate Reductase (NADH)Sequence Homology, Amino AcidMethylenetetrahydrofolate Reductase (NADPH2)MutationMolecular WeightAlcohol OxidoreductasesPteridinesBacterial ProteinsMethionine Sulfoxide ReductasesHydroxymethylglutaryl-CoA Reductase InhibitorsQuinone ReductasesCoenzymesRibonucleoside Diphosphate ReductaseSpectrum AnalysisBacteriaModels, MolecularSeawaterDihydropteridine ReductaseOxidoreductases Acting on CH-CH Group DonorsThioredoxin Reductase 1Sequence AlignmentCrystallography, X-RaySalmonella typhimuriumProtein ConformationEnoyl-(Acyl-Carrier-Protein) Reductase (NADH)Sulfur OxidesDNA, RibosomalNADElectrophoresis, Polyacrylamide GelPolymerase Chain ReactionFlavin MononucleotideSuperoxidesTemperatureCatalysisFlavin-Adenine DinucleotideReactive Oxygen Species3-Oxoacyl-(Acyl-Carrier-Protein) ReductaseSubstrate SpecificityMevalonic AcidLovastatin
NitriteFerredoxinOxidoreductaseFlavoproteinProteinEnzymesEnterobacteriaGlutathioneYeastElectronCytochromeAnaerobicNADHReductionSiRHPProducesSulfurReactionHUMANDomainComplexFamilyAlternativeNicotinamide adenine dOxidaseNitrate reductaseNitrite reductaseEscherichiaNADH or NADPHSubunitSubunitsCharacterizationSulfideElectronEnzymeMonooxygenaseSubstrateGeneExpressionFound
Nitrite3
  • Nitrite/Sulfite reductase ferredoxin-like domain [Interproscan]. (ntu.edu.sg)
  • Fd acts simultaneously as a bottleneck and as a hub which distributes high-energy electrons to a multitude of enzymes, which include nitrite reductase, sulphite reductase, fatty acid desaturase, glutamine-2-oxoglutarate amino transferase (GOGAT), redox complexes such as cytochrome b 6 /f for cyclic electron transport (CET) and thioredoxins 2 . (nature.com)
  • Nitrite reductases. (lookformedical.com)
Ferredoxin2
  • This enzyme is different from EC 1.8.1.2 , assimilatory sulfite reductase (NADPH), and EC 1.8.7.1 , assimilatory sulfite reductase (ferredoxin), which are involved in sulfate assimilation. (genome.jp)
  • The dominant pathway in chloroplasts is, however, the one that produces NADPH, by the activity of ferredoxin NADP + oxidoreductase (FNR). (nature.com)
Oxidoreductase2
  • Sulfite reductase (NADPH) (EC 1.8.1.2, sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase, NADPH-sulfite reductase, NADPH-dependent sulfite reductase, H2S-NADP oxidoreductase, sulfite reductase (NADPH2)) is an enzyme with systematic name hydrogen-sulfide:NADP+ oxidoreductase. (wikipedia.org)
  • NADPH-dependent diflavin oxidoreductase 1 OS=Cryptococcus neoformans var. (uu.nl)
Flavoprotein1
  • This enzyme catalises the following chemical reaction hydrogen sulfide + 3 NADP+ + 3 H2O ⇌ {\displaystyle \rightleftharpoons } sulfite + 3 NADPH + 3 H+ Sulfite reductase is an iron flavoprotein (FAD and FMN). (wikipedia.org)
Protein1
  • The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. (genome.jp)
Enzymes1
  • In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. (lookformedical.com)
Enterobacteria1
  • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. (wikipedia.org)
Glutathione1
  • Most of parameters involved in ROS and MG metabolisms had similar variation trends and degrees between the Mg-deficient lower leaves and roots, but several parameters (namely glutathione S-transferase, sulfite reductase, ascorbate and dehydroascorbate) displayed the opposite variation trends. (biomedcentral.com)
Yeast1
Electron1
  • Assimilatory NADPH-dependent sulfite reductase (SiR) is the enzyme responsible for the six-electron reduction of sulfite to sulfide. (fsu.edu)
Cytochrome1
  • SiRFP is a homologous to cytochrome P-450 reductase (CYP), each of which has three main domains: NADPH/FAD-binding domain, FMN-binding domain and a connecting domain that is responsible of the relative orientation of the other two domains. (fsu.edu)
Anaerobic1
  • 12509) anaerobic ribonucleoside-triphosphate reductase CP001857 CDS Arcpr_0011 12741. (go.jp)
NADH1
Reduction1
  • In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1 in the right to left direction), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2 in the left to right direction) [1]. (genome.jp)
SiRHP1
  • In the SiR holoenzyme electrons flow from NADPH to FAD to FMN in SiRFP and from the FMN cofactor to SiRHP. (fsu.edu)
Produces1
  • The pentose phosphate pathway is a process of glucose turnover that produces NADPH as reducing equivalents and pentoses as essential parts of nucleotides. (easyomics.org)
Sulfur1
  • The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. (genome.jp)
Reaction1
  • Mehler reaction, or water-water cycle, allows functionality of the CET and subsequent synthesis of ATP needed for the Calvin cycle, which finally oxidizes NADPH to re-establish LET 5 . (nature.com)
HUMAN1
  • Gamma-interferon-inducible lysosomal thiol reductase is upregulated in human melanoma. (harvard.edu)
Domain1
  • Third, the linker between the FMN-binding domain and FAD/NADPH binding domain is also an intrinsically disorder region that orients the FMN-domain relative to rest of the complex. (fsu.edu)
Complex1
  • Dative anchoring of a piano‐stool complex within ribonuclease S resulted in an artificial imine reductase. (ward-lab.ch)
Family1
  • After that, aldo-keto reductase family 1 member C4 is used to create 3a,7a-dihydroxy-5b-cholestane. (smpdb.ca)
Alternative1
Nicotinamide adenine d2
  • Sulfite reductase (NADPH) (EC 1.8.1.2, sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase, NADPH-sulfite reductase, NADPH-dependent sulfite reductase, H2S-NADP oxidoreductase, sulfite reductase (NADPH2)) is an enzyme with systematic name hydrogen-sulfide:NADP+ oxidoreductase. (wikipedia.org)
  • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. (wikipedia.org)
Oxidase2
  • A NADPH-dependent oxidase that reduces hydrogen sulfite to HYDROGEN SULFIDE . (nih.gov)
  • The calcium channel modulator 2-APB hydrolyzes in physiological buffers and acts as an effective radical scavenger and inhibitor of the NADPH oxidase 2. (uniklinikum-saarland.de)
Nitrate reductase1
  • 4Fe-4S dicluster domain, Respiratory nitrate reductase beta C-terminal [Interproscan]. (ntu.edu.sg)
Nitrite reductase1
  • Fd acts simultaneously as a bottleneck and as a hub which distributes high-energy electrons to a multitude of enzymes, which include nitrite reductase, sulphite reductase, fatty acid desaturase, glutamine-2-oxoglutarate amino transferase (GOGAT), redox complexes such as cytochrome b 6 /f for cyclic electron transport (CET) and thioredoxins 2 . (nature.com)
Escherichia3
  • The two-component alkanesulfonate monooxygenase system from Escherichia coli is comprised of an FMN reductase (SsuE) and a monooxygenase enzyme (SsuD) that together catalyze the oxidation of alkanesulfonate to the corresponding aldehyde and sulfite products. (auburn.edu)
  • 10. The flavoprotein component of the Escherichia coli sulfite reductase: expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors. (nih.gov)
  • 17. Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli. (nih.gov)
NADH or NADPH2
  • It catalyzes the reduction of free flavins, FMN, FAD or riboflavin by NADH or NADPH. (rhea-db.org)
  • Cannot use NADH or NADPH. (cansar.ai)
Subunit1
  • The reaction is inhibited by molecular oxygen and greatly stimulated by Fe(2+)-acceptors such as ferrozine or the iron-free form of ribonucleotide reductase subunit R2. (rhea-db.org)
Subunits3
  • This reaction combines the enzymatic reactions of phosphoadenylyl-sulfate reductase (thioredoxin) (yeast protein Met16p, EC 1.8.4.8) and sulfite reductase (NADPH) (subunits Met5p and Met10p, EC 1.8.1.2). (nih.gov)
  • The enzyme sulfite reductase (NADPH) (subunits Met5p and Met10p, EC 1.8.1.2, part of reaction v4) actually uses NADPH, and the authors assume equilibration of NADH and NADPH. (nih.gov)
  • The deduced amino acid sequences of these two ORFs are highly homologous with those of α and β subunits of sulfite reductase from E. coli. (ncl.edu.tw)
Characterization1
  • 5. Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA. (nih.gov)
Sulfide2
  • This mutant strain could grow on minimal medium with sulfide, but not on minimal medium with sulfite. (ncl.edu.tw)
  • Catalyzes the reduction of sulfite to sulfide using reduced F420 as the electron source. (cansar.ai)
Electron5
  • Results from isotope studies with the [4(R)-2H]NADPH substrate demonstrates the rate-limiting step in flavin reduction is electron transfer from NADPH to FMN. (auburn.edu)
  • 4. Electron transfer in flavocytochrome P450 BM3: kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase. (nih.gov)
  • 6. Stopped-flow kinetic studies of electron transfer in the reductase domain of neuronal nitric oxide synthase: re-evaluation of the kinetic mechanism reveals new enzyme intermediates and variation with cytochrome P450 reductase. (nih.gov)
  • 7. Electron transfer in human methionine synthase reductase studied by stopped-flow spectrophotometry. (nih.gov)
  • 9. Interflavin one-electron transfer in the inducible nitric oxide synthase reductase domain and NADPH-cytochrome P450 reductase. (nih.gov)
Enzyme2
  • In single-enzyme kinetic assays, SsuE followed an ordered sequential mechanism, with NADPH as the first substrate to bind and NADP+ as the last product to dissociate. (auburn.edu)
  • These results suggest that both the SsuD enzyme and alkanesulfonate substrate are required to ensure that the FMN reductases reaction proceeds to form the ternary complex with the subsequent generation of reduced flavin. (auburn.edu)
Monooxygenase2
  • In this study, a hydroxylase system consisting of an FADH(2)-utilizing monooxygenase (GTNG_3160) and an FAD reductase (GTNG_3158), as well as a bifunctional riboflavin kinase/FMN adenylyltransferase (GTNG_3159), encoded in the anthranilate degradation gene cluster in Geobacillus thermodenitrificans NG80-2 were functionally characterized in vitro. (rhea-db.org)
  • Based on the steady-state and pre-steady-state kinetic analyses of SsuE, a reaction mechanism has been elucidated for the flavin reductase catalyzed reaction in the alkanesulfonate monooxygenase system. (auburn.edu)
Substrate1
  • The Km value was 15.8 microM for NADPH and 434 micron for NADH, indicating that NADPH is the preferred substrate. (nih.gov)
Gene2
  • Nucleotide sequence anaiysis of the upstream region ofcytochrome P450 BM3 gene in Bacillus megatenum revealed a region about 250 bp long, which was similar to the sulfite reductases of E. coli and Salmonella typhimurium. (ncl.edu.tw)
  • was available, we decided to clone, sequence, and characterize the sulfitereductase gene from B. megaterium. (ncl.edu.tw)
Expression1
  • Complementation of this ORF2 mutation with an expression vector, which constitutively expressed ORF2, restored the ability to grow on minimal medium with sulfite. (ncl.edu.tw)
Found1