• Sulfite reductase (ferredoxin) (EC 1.8.7.1, ferredoxin-sulfite reductase) is an enzyme with systematic name hydrogen-sulfide:ferredoxin oxidoreductase. (wikipedia.org)
  • In photosynthesis, final electron transfer from ferredoxin to NADP + is accomplished by the flavo enzyme ferredoxin:NADP + oxidoreductase (FNR). (nature.com)
  • The dominant pathway in chloroplasts is, however, the one that produces NADPH, by the activity of ferredoxin NADP + oxidoreductase (FNR). (nature.com)
  • The pulse of acetogenesis appears to have been collectively catalyzed by a number of different organisms and metabolisms, most prominently pyruvate:ferredoxin oxidoreductase. (frontiersin.org)
  • Prosthetic group of: formate dehydrogenase, purine hydroxylase, thiosulfate reductase. (wikipedia.org)
  • Growth on CO requires the enzyme carbon monoxide dehydrogenase (CODH) that catalyzes the reversible conversion between CO and CO 2 . (hindawi.com)
  • Sulfite oxidation by the quinone-reducing molybdenum sulfite dehydrogenase SoeABC from the bacterium Aquifex aeolicus. (cnrs.fr)
  • Structural evidence for a reaction intermediate mimic in the active site of a sulfite dehydrogenase. (cnrs.fr)
  • Enzymes that contain the molybdopterin cofactor include xanthine oxidase, DMSO reductase, sulfite oxidase, and nitrate reductase. (wikipedia.org)
  • An enzyme that catalyzes the oxidation of nitrite to nitrate. (lookformedical.com)
  • Nitrate reductase delta subunit [Interproscan]. (ntu.edu.sg)
  • The bifunctional CODH ( cdhAB-2 ) is predicted to play an ubiquitous role in the metabolism of CO, and a novel nitrate reductase-associated respiratory complex was induced specifically in the presence of sulfate. (hindawi.com)
  • 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)
  • With the finding of similar very high spin signals also in D. variabilis desulforubidin, it appears that the presence of a S = 9/2 Fe-S (super) cluster is common in all dissimilatory sulfite reductases. (wur.nl)
  • These observations are interpreted as supportive evidence against the previously proposed model of a bridged cubane/siroheme as the active site for dissimilatory sulfite reductases. (wur.nl)
  • The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. (genome.jp)
  • 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)
  • Multiple membrane-bound heterodisulfide reductase (DsrMK) could promote both energy-conserving and non-energy-conserving menaquinol oxidation. (hindawi.com)
  • 12509) anaerobic ribonucleoside-triphosphate reductase CP001857 CDS Arcpr_0011 12741. (go.jp)
  • DMSO reductase anchor subunit (DmsC) [Interproscan]. (ntu.edu.sg)
  • This enzyme catalises the following chemical reaction hydrogen sulfide + 6 oxidized ferredoxin + 3 H2O ⇌ {\displaystyle \rightleftharpoons } sulfite + 6 reduced ferredoxin + 6 H+ This sulfite reductase is an iron protein. (wikipedia.org)
  • In the last steps of this process transfer of energy-conserving electrons beyond photosystem I (PSI) is performed by a small iron-sulphur protein ferredoxin (Fd). (nature.com)
  • protein_coding" "AAC74185","ptsG","Escherichia coli","fused glucose-specific PTS enzymes: IIB component/IIC component [Ensembl]. (ntu.edu.sg)
  • Enoyl-(Acyl carrier protein) reductase [Interproscan]. (ntu.edu.sg)
  • protein_coding" "AAC74888","manY","Escherichia coli","mannose-specific enzyme IIC component of PTS [Ensembl]. (ntu.edu.sg)
  • An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. (nih.gov)
  • The presented method of preparing artificial haem proteins containing abiological metal porphyrins sets the stage for the generation of artificial enzymes from innumerable combinations of PIX-protein scaffolds and unnatural metal cofactors to catalyse a wide range of abiological transformations. (ward-lab.ch)
  • Molybdopterins are a class of cofactors found in most molybdenum-containing and all tungsten-containing enzymes. (wikipedia.org)
  • The only molybdenum-containing enzymes that do not feature molybdopterins are the nitrogenases (enzymes that fix nitrogen). (wikipedia.org)
  • In this case, the tungsten-selenium pair has been speculated to function analogously to the molybdenum-sulfur pairing of some molybdenum cofactor-requiring enzymes. (wikipedia.org)
  • Cyanothece may prove very important in biological hydrogen production, as it is missing the uptake hydrogenase enzyme. (up.ac.za)
  • This newly synthesized nano manganese-substituted CA enzyme was investigated for its role as a peroxidase, which could be an alternative for hydrogen peroxidases. (ward-lab.ch)
  • DMSO reductase, the metal is bound to two molybdopterin cofactors. (wikipedia.org)
  • The enzyme participates in sulfate assimilation. (expasy.org)
  • Nitrite reductases. (lookformedical.com)
  • A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (lookformedical.com)
  • An enzyme found primarily in BACTERIA and FUNGI that catalyzes the oxidation of ammonium hydroxide to nitrite. (lookformedical.com)
  • 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)
  • The position of these bands shifted upon oxidation and reduction of the enzymes. (wur.nl)
  • This subclass includes only those enzymes in which some other redox carrier is the acceptor. (lookformedical.com)
  • Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). (lookformedical.com)
  • The dyad of the Y-junction- and a flavin module unites diverse redox enzymes. (cnrs.fr)
  • 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)
  • Enzymes that use molybdopterin as cofactor or prosthetic group are given below. (wikipedia.org)
  • In addition we are investigating the mechanistic roles of Fe-S clusters in two rapidly emerging classes of Fe-S enzymes involved with disulfide reduction and radical generation. (uga.edu)
  • Photosynthetically active FNR (sometimes classified as autotrophic) is a member of the family of soluble monomeric enzymes that contain non-covalently bound FAD (flavin adenine dinucleotide) as the prosthetic group 3 . (nature.com)
  • Fe-S clusters are present in more than 300 different types of enzymes or proteins and play crucial roles in fundamental life processes such as respiration, photosynthesis and nitrogen fixation. (uga.edu)
  • In this study, a nano-enzyme system was designed in aqueous solutions at room temperature and under nitrogen atmosphere to use the CA enzyme without any pre-treatment and deformation in its structure. (ward-lab.ch)
  • Zn2+ ions, which are present in the active site of the enzyme, interact with the substrate molecules directly and cause catalytic effect. (ward-lab.ch)
  • Enzymes that contain metal ions-that is, metalloenzymes-possess the reactivity of a transition metal centre and the potential of molecular evolution to modulate the reactivity and substrate-selectivity of the system1. (ward-lab.ch)
  • This strategy could create artificial enzymes for abiological catalysis within the natural substrate binding site of an enzyme that can be subjected to directed evolution. (ward-lab.ch)
  • The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. (genome.jp)
  • The aim of my thesis is to study physical, chemical, and biological properties of multi- electron transferring enzymes, in a quest for possible new structures and functions of biological Fe-S clusters. (wur.nl)
  • One of these enzymes is a radical SAM, a family of enzymes often associated with C-X bond-forming reactions (X = S, N). This intermediate pyranopterin is then converted to the molybdopterin via the action of three further enzymes. (wikipedia.org)
  • Models for the active sites of enzymes molybdopterin-containing enzymes are based on a class of ligands known as dithiolenes. (wikipedia.org)
  • Here we report the formal replacement of iron in Fe-porphyrin IX (Fe-PIX) proteins with abiological, noble metals to create enzymes that catalyse reactions not catalysed by native Fe-enzymes or other metalloenzymes9,10. (ward-lab.ch)
  • Two enzyme-mediated reactions convert guanosine triphosphate to the cyclic phosphate of pyranopterin. (wikipedia.org)
  • The class of all enzymes catalyzing oxidoreduction reactions. (lookformedical.com)
  • Metal centers constitute the active sites of at least one third of all enzymes and determining the assembly mechanism of metallocenters and the electronic and structural properties of metal centers that confer selective and specific catalytic activity present fascinating challenges to inorganic chemists. (uga.edu)
  • Theoretical Study of the Mechanism of the Nonheme Iron Enzyme EgtB. (harvard.edu)
  • The enzyme belongs to the class of desulforubidins, as was deduced from its UV/vis absorption spectrum. (wur.nl)
  • Km and Vmax values for nano CA enzyme were found to be 0.442 mM and 1.6 × 10−3 mM min-1, respectively, whereas Km and Vmax values for free CA were found to be 0.471 mM and 1.5 × 10−3 mM min-1, respectively. (ward-lab.ch)
  • In addition to these, the Zn2+ ion present in the active site of the nano CA enzyme was replaced by rodium metal. (ward-lab.ch)
  • The novel concept ANADOLUCA (AmiNo Acid (monomer) Decorated and Light Underpinning Conjugation Approach) was used for this process, nano CA enzyme of size 93 nm was synthesized. (ward-lab.ch)
  • The activity of the synthesized nano CA was measured following the change in absorbance during the conversion of 4-nitrophenylacetate (NPA) to 4-nitrophenylate ion at 348 nm for a period of 10 min at 25 °C compared with free CA enzyme. (ward-lab.ch)
  • Tungsten-using enzymes typically reduce free carboxylic acids to aldehydes. (wikipedia.org)