... Nitrogenase EC number 1.18.6.1 is the enzyme used by some organisms to fix atmospheric nitrogen ... associated with the homodimeric Fe protein . Nitrogenase is supplied reducing power when ... three cycles are sufficient to convert one molecule of N sub 2 sub to ammonia. Ultimately, nitrogenase ... in obtaining crystal s of nitrogen bound to nitrogenase. This is because the resting ... catalysis . Nitrogenase is able to reduce acetylene, but is inhibited by carbon monoxide, which .... ref Seefeldt LC, Dance IG, Dean DR. 2004. Substrate interactions with nitrogenase Fe versus .... L. Eady, R. R. Richardson, T. H. Miller, R. W. Hawkins, M. Postgate, J. R., 1986, The alternative nitrogenase .... One known exception is the nitrogenase of Streptomyces thermoautotrophicus , which is unaffected ... are unique in their ability to employ an oxygen labile nitrogenase under aerobic conditions. This ability ... Oelze J. 2000. Respiratory protection of nitrogenase in Azotobacter species Is a widely held hypothesis ... NH sub 3 sub , nitrogenase is also capable of catalyzing the following reactions ref name Burris1 cite ... of nitrogenase journal J Bacteriol volume 123 issue 2 pages 537&ndash 545 year 1975 url ... cite journal author G. N. Schrauzer title Nonenzymatic Simulation of Nitrogenase Reactions and the Mechanism ... inhibitor, of nitrogenase journal Biochemistry volume 34 issue 16 pages 5382&ndash 5389 year 1995 ..., Cyanate, and Carbon Disulfide by Nitrogenase Kinetic Characterization and EPR Spectroscopic ... of nitrogenase catalyzed ammonia formation by hydrogen journal Biochemistry volume 22 issue 22 ... inhibitors rapid equilibrium inhibitor ref name Seefeldt1 of nitrogenase. Vanadium nitrogenase ... that synthesize nitrogenase Free living diazotroph s, e.g. Cyanobacteria by means of differentiated ... sequence similarity to the three subunits of nitrogenase. This protein is present in gymnosperms ... ca Nitrogenasa cs Nitrogen za de Nitrogenase es Nitrogenasa fr Nitrog nase it Nitrogenasi nl Nitrogenase ... more details
author Rehder D. title Vanadium Nitrogenase journal Journal of Inorganic Biochemistry year 2000 volume ... palustris journal Nature Biotechnology year 2004 volume 22 issue 55 ref Vanadium nitrogenase ... when molybdenum is unavailable to the primary molybdenum nitrogenase pathway. ref name rehder An important component in nature s nitrogen cycle , vanadium nitrogenase in the presence of dinitrogen ..., U.S. researchers discovered that nitrogen deprived vanadium nitrogenase in the presence of carbon ... chemistryworld News 2010 August 05081001.asp accessdate 2010 08 05 title Nitrogenase Found to be a Two ... and others 2004 Most of the functions of vanadium nitrogenase match that of the more common molybdenum nitrogenase s and serve as an alternative pathway for nitrogen fixation in molybdenum deficient conditions. ref name eady cite journal author Eady R. R. title The Vanadium Nitrogenase of Azotobacter journal Polyhedron year 1989 volume 8 issue 13 14 pages 1695 1700 ref Like molybdenum nitrogenase ... of the active site of nitrogenase journal Coordination Chemistry Reviews year 2005 volume 249 issue 21 22 pages 2144 2155 ref Vanadium nitrogenase has an sub 2 sub sub 2 sub sub 2 sub protein subunit subunit structure while molybdenum nitrogenase has an sub 2 sub sub 2 sub structure. Though the structural genes encoding vanadium nitrogenase shows only about 15 conservation with molybdenum ... nitrogenase is less active in nitrogen fixing than moldybdenum nitrogenases because it converts ... as low as 5 C and its low temperature activity is 10 times higher than that of Mo Fe nitrogenase ... of Azotobacter chroococcum . Low temperature favours N2 reduction by vanadium nitrogenase. pmc 1135427 ... the molybdenum nitrogenase, small amounts of hydrazine , isonitriles , and acetylene which can be converted to ethylene and ethane can be produced during catalytic activity. Vanadium nitrogenase is easily ... by vanadium nitrogenase can be summarized as follows ref name rehder 2N sub 2 sub 12e sup sup ... more details
enzyme Name nitrogenase flavodoxin EC number 1.19.6.1 CAS number 9013 04 1 IUBMB EC number 1 19 6 1 GO code 0050142 image width caption In enzymology , a nitrogenase flavodoxin EC number 1.19.6.1 is an enzyme that catalysis catalyzes the chemical reaction 6 reduced flavodoxin 6 H sup sup N sub 2 sub n ATP math rightleftharpoons math 6 oxidized flavodoxin 2 NH sub 3 sub n ADP n phosphate The 4 substrate biochemistry substrates of this enzyme are reduced flavodoxin , hydrogen ion H sup sup , nitrogen N2 , and adenosine triphosphate ATP , whereas its 4 product chemistry products are oxidized flavodoxin , ammonia NH sub 3 sub , adenosine diphosphate ADP , and phosphate . This enzyme belongs to the family of oxidoreductase s, specifically those acting on reduced flavodoxin as dono with dinitrogen as acceptor. The systematic name of this enzyme class is reduced flavodoxin dinitrogen oxidoreductase ATP hydrolysing . This enzyme participates in nitrogen metabolism . It has 2 cofactor biochemistry cofactors molybdenum , and Iron sulfur . References reflist 1 cite journal author Zumft WG, Mortenson LE date 1975 title The nitrogen fixing complex of bacteria journal Biochim. Biophys. Acta. volume 416 pages 1&ndash 52 pmid 164247 issue 1 1.19 enzyme stub Other oxidoreductases Category EC 1.19.6 Category Molybdenum enzymes Category Iron sulfur enzymes Category Enzymes of unknown structure it Nitrogenasi flavodossina ja ... more details
region. nifH, nifK and nifD encode the nitrogenase s subunits, while nifE, nifN, nifU, nifS, nifV ... into the nitrogenase s subunits. nifF and nifJ encode proteins related to electron transfer taking ... in a metabolic way through a reversible ADP ribosylation of a specific arginine residue in the nitrogenase ... in the electron transfer flow and by so, inactivates nitrogenase s activity. The enzymes catalyzing ... more details
italic title Expert subject Microbiology date November 2008 Taxobox color lightgrey name Azotobacter regnum Bacterium Bacteria phylum Proteobacteria classis Gamma Proteobacteria ordo Pseudomonadales familia Pseudomonadaceae genus Azotobacter species A. vinelandii binomial Azotobacter vinelandii binomial authority Jacob Goodale Lipman Lipman ref cite book title Review of American Chemical Research volume 10 year 1904 editor William A. Noyes page http books.google.com books?id LAoSAAAAIAAJ&pg PA75 v onepage&q&f false 75 ref Azotobacter vinelandii is diazotroph that can fix nitrogen while grown aerobic organism aerobically . It is a genomics genetically tractable system that is used to study nitrogen fixation . These bacteria are easily cultured and grown. It is a free living N sub 2 sub fixer which is known to produce many phytohormone s and vitamin s in the soil. The nitrogenase enzyme holoenzyme of Azotobacter vinelandii has been characterised via x ray crystallography in both Adenosine diphosphate ADP tetrafluoroaluminate bound ref Schindelin, H., Kisker, C., Schlessman, J.L., Howard, J.B., Rees, D.C. 1997 Structure of ADP x AIF4 stabilized nitrogenase complex and its implications for signal transduction. Nature 387 370 376 ref and Mg Adenosine triphosphate ATP bound ref Chiu, H., Peters, J.W., Lanzilotta, W.N., Ryle, M.J., Seefeldt, L.C., Howard, J.B., Rees, D.C. 2001 MgATP Bound and nucleotide free structures of a nitrogenase protein complex between the Leu 127 Delta Fe protein and the MoFe protein. Biochemistry 40 641 650 ref states. The enzyme possesses molybdenum iron sulfido cluster Cofactor biochemistry cofactors FeMoCo as active site s, each bearing 2 pseudo cubic iron sulfido structures. References reflist External links http www.azotobacter.org Azotobacter vinelandii Genome Project http www.micron.ac.uk organisms Avi.html Current research on Azotobacter vinelandii at the Norwich Research Park Category Pseudomonadales Proteobacteria stub es Azotobacter vin ... more details
has the unique characteristic of encoding for a vanadium nitrogenase vanadium containing nitrogenase which produces as a byproduct of nitrogen fixation three times more hydrogen than the nitrogenase of other bacteria molybennum containing nitrogenase . The potential to manipulate R. palustris ... more details
. rubrum that, for the first time, post translational regulation of nitrogenase was demonstrated. Nitrogenase is modified by an ADP ribosylation in the arginine residue 101 Arg101 ref cite journal ... protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific .... ref cite journal author Neilson AH, Nordlund S title Regulation of nitrogenase synthesis ... more details
Unreferenced date August 2007 Heterocysts are specialized nitrogen fixation nitrogen fixing cells formed by some filamentous cyanobacteria , such as Nostoc punctiforme , Cylindrospermum stagnale and Anabaena Anabaena sphaerica , during nitrogen starvation. They fix nitrogen from dinitrogen N sub 2 sub in the air using the enzyme nitrogenase , in order to provide the cells in the filament with nitrogen for biosynthesis. Nitrogenase is inactivated by oxygen, so the heterocyst must create a microanaerobic environment. The heterocysts unique structure and physiology require a global change in gene expression . For example, heterocysts produce three additional cell wall s, including one of glycolipid that forms a hydrophobic barrier to oxygen produce nitrogenase and other proteins involved in nitrogen fixation degrade photosystem II , which produces oxygen up regulate glycolysis glycolytic enzymes produce proteins that scavenge any remaining oxygen contain polar plugs composed of cyanophycin which slows down cell to cell diffusion Cyanobacteria usually obtain a fixed carbon carbohydrate by photosynthesis . The lack of photosystem II prevents heterocysts from photosynthesizing, so the vegetative cells provide them with carbohydrate s, which is thought to be sucrose . The fixed carbon and nitrogen sources are exchanged through channels between the cells in the filament. Heterocysts maintain photosystem I, allowing them to generate Adenosine triphosphate ATP by light reactions cyclic photophosphorylation . Single heterocysts develop about every 9 15 cells, producing a one dimensional pattern along the filament. The interval between heterocysts remains approximately constant even though the cells in the filament are dividing. The bacterial filament can be seen as a multicellular organism with two distinct yet interdependent cell types. Such behavior is highly unusual in prokaryote s and may have been the first example of multicellular patterning in evolution . Once a heteroc ... more details
DISPLAYTITLE Rhodobium bacterium Taxobox color lightgrey name Rhodobium regnum Bacterium Bacteria phylum Proteobacteria classis Alpha Proteobacteria ordo Rhizobiales familia Rhodobiaceae genus Rhodobium subdivision ranks Species subdivision R. orientis br R. marina Rhodobium is a genus of purple bacteria purple non sulfur bacteria that reproduces by budding . The cells are rod shaped and reproduce by budding , as in many other members of the Rhizobiales . RNA trees separate it from the others, however, and it is given its own family. R. orientis , the type species, was isolated from seawater in 1995. It is capable of photosynthetic hydrogen production via the nitrogenase enzyme. References Hiraishi A, Urata K, Satoh T. 1995 . A new genus of marine budding phototrophic bacteria, Rhodobium gen. nov., which includes Rhodobium orientis sp. nov. and Rhodobium marinum comb. nov. International Journal of Systematic and Evolutionary Microbiology 45 226 234. DEFAULTSORT Rhodobium Bacterium Category Rhizobiales Proteobacteria stub ... more details
oxidoreductase ATP hydrolysing , Nitrogenase R00076 EC 2.7.11.19 4 Adenosine triphosphate ATP ... Hydrazine 2e sup sup 2H sup sup 2NH sub 3 sub Dinitrogen oxidoreductase ATP hydrolysing , Nitrogenase ... ATP hydrolysing , Nitrogenase R03042 EC 3.6.1.11 Polyphosphate nP sub i sub H sub 2 sub O Polyphosphate ... sup Hydrazine Dinitrogen oxidoreductase ATP hydrolysing , Nitrogenase R05185 EC 1.18.6.1 16 Adenosine ... hydrolysing , Nitrogenase R05186 EC 1.19.6.1 n Adenosine triphosphate ATP N sub 2 sub 6 Reduced flavodoxin ... sub Nitrogenase flavodoxin R05496 EC 1.18.6.1 Acetylene Reduced ferredoxin 2H sup sup Adenosine triphosphate ... oxidoreductase ATP hydrolysing , Nitrogenase See also div col colwidth 12em Adenosine triphosphate ... more details
enzyme Name protochlorophyllide reductase EC number 1.3.1.33 CAS number 68518 04 7 IUBMB EC number 1 3 1 33 GO code 0016630 image width caption In enzymology , a protochlorophyllide reductase EC number 1.3.1.33 is an enzyme that catalysis catalyzes the chemical reaction chlorophyllide a NADP sup sup math rightleftharpoons math protochlorophyllide NADPH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are chlorophyllide a and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are protochlorophyllide , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH CH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is chlorophyllide a NADP 7,8 oxidoreductase . Other names in common use include NADPH2 protochlorophyllide oxidoreductase , NADPH protochlorophyllide oxidoreductase , NADPH protochlorophyllide reductase , protochlorophyllide oxidoreductase , and protochlorophyllide photooxidoreductase . This enzyme participates in porphyrin and chlorophyll metabolism . There are two structurally unrelated proteins with this activity the light dependent and the dark operative. The light dependent reductase needs light to operate. The dark operative version is a completely different protein, consisting of three subunits that exhibit significant sequence similarity to the three subunits of nitrogenase ref Yuichi FujitaDagger and Carl E. Bauer 2000 . Reconstitution of Light independent Protochlorophyllide Reductase from Purified Bchl and BchN BchB Subunits. J. Biol. Chem., Vol. 275, Issue 31, 23583 23588. http www.jbc.org cgi content abstract 275 31 23583 ref . This enzyme might be evolutionary older but being similar to nitrogenase is highly sensitive to free oxygen and does not work if its concentration exceeds about 3 ref S.Yamazaki, J.Nomata, Y.Fujita 2006 Di ... more details
to grow, yet their nitrogenase is still debilitated if exposed to oxygen. Azotobacter vinelandii ... only a single photosystem which cannot split water. Nitrogenase is expressed under nitrogen limitation ... nodules that house the bacterial symbionts, and supplied at a rate that will not harm the nitrogenase ... more details
Unreferenced stub auto yes date December 2009 Image NodSm IV Ac,C16 2,S .svg right thumb 300px The structure of nod factor from Sinorhizobium meliloti . Nodulation Nod factors are signaling molecule s produced by bacteria known as rhizobia during the initiation of root nodule nodules on the root of legume s. A symbiosis is formed when legumes take up the bacteria. The rhizobia produce nitrogen for the plant, and the legumes produce leghemoglobin to carry away any oxygen that would inhibit nitrogenase activity. Nod factors structurally are lipochitooligosaccharides LCOs that consist of an acylation acylated chitin oligomeric backbone with various functional group substitutions at the terminal or non terminal residues. The number of N acetylglucosamine molecules vary among Nod factors however, generally the length of a chitin backbone is from 3 to 5. The exact chemical structure of the Nod factor that is recognised by the plant varies between bacterial species and is the basis for host symbiont specificity. Nod factors are recognized by a specific class of Receptor biochemistry receptor kinase s that have so called LysM protein domain domain s in their extracellular domains. The two LysM lysin motif receptor kinases NFR1 and NFR5 that appear to make up the Nod factor receptor were first isolated in the model organism model legume Lotus japonicus in 2003. They now have been isolated also from soybean and the model legume Medicago truncatula . NFR5 lacks the classical activation loop in the kinase domain . The NFR5 gene lacks intron s. DEFAULTSORT Nod Factor Category Legumes Category Oligosaccharides Category Signal transduction Category Plant physiology Biochemistry stub Botany stub es Factores NOD fr Facteur nod ... more details
chembox ImageFile Homocitric acid.png ImageSize 200px IUPACName 2 hydroxybutane 1,2,4 tricarboxylic acid OtherNames Homocitric acid br Homocitrate Section1 Chembox Identifiers CASNo 3562 74 1 PubChem 28371 SMILES OC O CCC O CC O O C O O Section2 Chembox Properties Formula C sub 7 sub H sub 10 sub O sub 7 sub MolarMass 206.15 g mol Appearance colorless solid Density MeltingPtC BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Homocitric acid is an organic compound with the formula HOC CO sub 2 sub H CH sub 2 sub CO sub 2 sub H C sub 2 sub H sub 4 sub CO sub 2 sub H . This tri carboxylic acid occurs naturally as a component of the iron molybdenum cofactor of certain nitrogenase proteins. ref Douglas C. Rees Great Metalloclusters in Enzymology Annual Reviews of Biochemistry 2002, volume 71, pp. 221 46. DOI 10.1146 annurev.biochem.71.110601.135406 ref Biochemists often refer to this cofactor as homocitrate, which is the conjugate bases that predominate in neutral aqueous solutions of this species. The molecule is related to citric acid by the addition of one methylene group, which is implied with the term homo. Unlike citric acid, homocitric acid is Chirality chemistry chiral . The acid exists in equilibrium with the lactone . Image Homocitrate2.png thumb 340px left br style clear left References references Category Hydroxy acids Category Chelating agents Category Tricarboxylic acids biochem stub ... more details
File Hodgson.JPG thumb Keith O. Hodgson. Keith O. Hodgson born 1947 ref http www.stanford.edu dept chemistry faculty hodgson Keith O. Hodgson , Stanford University faculty page, accessed 29 10 2010 ref is a Professor of Chemistry at Stanford university and the Stanford Synchrotron Radiation Lightsource . He received his B.S. in 1969 from the University of Virginia and his Ph.D. in 1972 from University of California at Berkeley. His principal research interests include inorganic, bioinorganic, structural and biophysical chemistry. His research group focuses on questions relating to how structure at different organizational levels relates to function. His research is done using a number of different x ray spectroscopic and scattering techniques such as x ray absorption spectroscopy XAS . One of his main area of focus is the active site of the enzyme nitrogenase, which is responsible for conversion of atmospheric dinitrogen to ammonia. Using XAS studies at the S, Fe and Mo edge, his group has worked to understand the electronic structure as a function of redox in this cluster. Other projects include the study of iron in dioxygen activation and oxidation and the role of copper in electron transport and in dioxygen activation. Over his career he has earned the following awards NATO Postdoctoral Fellow, E.T.H. Zurich 1972 73, Alfred P. Sloan Foundation Fellow, 1976 78 Sidhu Award for Contributions to X ray Diffraction, 1978 World Bank Lecturer, 1984, and the Ernest Orlando Lawrence Award in 2002. ref http www.sc.doe.gov lawrence html Laureates 2000s keitho.htm The Ernest Orlando Lawrence Award Keith O. Hodgson 2002 , US Department of Energy Office of Science, accessed 29 10 2010 ref References references External links http www.stanford.edu dept chemistry faculty hodgson Keith O. Hodgson , Stanford University faculty page Persondata Metadata see Wikipedia Persondata . NAME Hodgson, Keith ALTERNATIVE NAMES SHORT DESCRIPTION DATE OF BIRTH PLACE OF BIRTH DATE OF DEATH PLACE ... more details
ferredoxins is implicated in the nitrogenase . Some 4Fe 4S clusters bind substrates and are thus ... systems are common. Examples include both the 8Fe and the 7Fe clusters in nitrogenase . Carbon ... is responsible the clusters in the enzyme nitrogenase. The suf and isc systems are more general ... to nitrogenase journal Curr. Opin. Chem. Biol. year 2002 volume 6 pages 259 273 pmid 12039013 doi ... more details
occurs at high levels of metabolism during the fixation of nitrogen and, is though to protect the nitrogenase ... and an important enzyme nitrogenase . The process of nitrogen fixation requires an influx .... ref cite journal author Shank Yu, Demin O., Bogachev AV title Respiratory Protection nitrogenase ... shethna, which protects nitrogenase and is involved in protecting the cells from oxygen. Mutant s not producing ... F. title Role of the Azotobacter vinelandii Nitrogenase Protective Shethna Protein in Preventing ... 397 issue 2 pages 261 270 ref Nitrogenase Main NitrogenaseNitrogenase is the most important enzyme involved in nitrogen fixation. Azotobacter species have several types of nitrogenase. The basic one is molybdenum iron nitrogenase. ref cite journal author Howard J. B., Rees D. C. title How many ... contains vanadium nitrogenase vanadium it is independent of molybdenum ions ref cite journal doi 10.1128 ... R. W., Hawkins M., Postgate J. R. title The alternative nitrogenase of Azotobacter chroococcum ... active than the Mo Fe nitrogenase at low temperatures. So it can fix nitrogen at temperatures as low as 5 C and its low temperature activity is 10 times higher than that of Mo Fe nitrogenase ... chroococcum. Low temperature favours N2 reduction by vanadium nitrogenase. pmc 1135427 journal ... in maturation of Mo Fe nitrogenase plays the so called P cluster. ref cite journal author Hu Y., Fay A. W., Lee C. C., Ribbe M. W. title P cluster maturation on nitrogenase MoFe protein journal Proceedings ... pmc 1965529 doi 10.1073 pnas.0704297104 volume 104 issue 25 pages 10424 10429 ref Synthesis of nitrogenase ... L., Brown C. S., Ludden P. W., Rubio L. M. title Genes required for rapid expression of nitrogenase ... more details
sensitive nitrogenase an enzyme responsible for the fixation of atmospheric nitrogen. Leghemoglobin ... an oxygen concentration that is low enough to allow nitrogenase to function but high enough ... more details
Taxobox name Trichodesmium regnum Bacteria phylum Cyanobacteria ordo Oscillatoriales genus Trichodesmium subdivision ranks Species subdivision Trichodesmium contortum T. contortum br Trichodesmium erythraeum T. erythraeum br Trichodesmium hildebrandtii T. hildebrandtii br Trichodesmium tenue T. tenue br Trichodesmium thiebautii T. thiebautii sea sawdust directs here, hence bold for that Trichodesmium , also called sea sawdust , is a genus of Filamentation filamentous cyanobacteria . They are found in nutrient poor tropical and subtropical ocean waters particularly around Australia , where they were first described by Captain Cook . Trichodesmium nitrogen fixation fixes atmospheric nitrogen into ammonium, usable also for other organisms. While far from the only nitrogen fixing bacterium bacteria , they are among the most important of the marine varieties, and are being extensively studied for their role in nutrient cycling in the ocean. Unlike other nitrogen fixing bacteria, Trichodesmium does not have heterocyst s, nor any other specialised cells for this task. Furthermore, nitrogen fixation peaks at mid day, i.e. occurs during the same time as photosynthesis. Inhibitor studies even revealed that photosystem II activity is essential for nitrogen fixation in this organism. All this may seem contradictory at first glance, because the enzyme responsible for nitrogen fixation, nitrogenase , is irreversibly inhibited by oxygen. However, Trichodesmium utilises photosynthesis for nitrogen fixation by carrying out the Mehler reaction , during which the oxygen produced by PSII is reduced again after PSI. This regulation of photosynthesis for nitrogen fixation involves rapidly reversible coupling of their light harvesting antenna, the phycobilisome s, with PSI and PSII. Trichodesmium forms blooms and provides substrate for many small oceanic organisms bacteria , diatoms , dinoflagellates , protozoa , and copepods . References Kana TM 1993 Rapid oxygen cycling in Trichodesmium ... more details
enzymes are FeFe hydrogenase, NiFe hydrogenase and nitrogenase . ref name 13 These enzymes behaves ... of the hydrogen forming enzymes in Clostridium is very unique with little or no involvement of nitrogenase ... is a hundred times higher than NiFe hydrogenase and a thousand times higher than nitrogenase. FeFe ... production is due to catalysis by nitrogenase. The production of hydrogen by FeFe hydrogenase ... and nitrogenase in this bacteria is responsible for the production of hydrogen and require nitrogen .... ref name 13 To attain high production rates of hydrogen, the hydrogen production by nitrogenase ... acids circle and the produced electrons are transferred to the nitrogenase catalysed ... more details
for nitrogenase action are very susceptible to destruction by oxygen. In fact, many bacteria ... deficiency Nitrogenase Birkeland Eyde process Push pull technology References Reflist External links ... more details
Chembox ImageFile Molybdenum cofactor.svg ImageSize 200px IUPACName OtherNames Moco Section1 Chembox Identifiers CASNo 872689 63 9 PubChem 25202532 SMILES S C1 C S C N2 C OC1COP O O O NC3 C2C N C N N3 O.O Mo 2 O Section2 Chembox Properties C 10 H 12 Mo 1 N 5 O 8 P 1 S 2 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Image MoPtSyn.png thumb 300px right Some biosynthetic steps leading to molybdenum pterin, a molydopterin. Molybdenum cofactor is a Cofactor biochemistry cofactor required for the activity of enzyme s such as sulfite oxidase , xanthine oxidoreductase , and aldehyde oxidase . ref name pmid16261263 cite journal author Schwarz G title Molybdenum cofactor biosynthesis and deficiency journal Cell. Mol. Life Sci. volume 62 issue 23 pages 2792 810 year 2005 month December pmid 16261263 doi 10.1007 s00018 005 5269 y url issn ref ref name pmid18411266 cite journal author Smolinsky B, Eichler SA, Buchmeier S, Meier JC, Schwarz G title Splice specific functions of gephyrin in molybdenum cofactor biosynthesis journal J. Biol. Chem. volume 283 issue 25 pages 17370 9 year 2008 month June pmid 18411266 doi 10.1074 jbc.M800985200 url issn ref It is a coordination complex formed between molybdopterin which, despite the name, does not contain molybdenum and an oxide of molybdenum . Molydopterins, in turn, are synthesized from guanosine triphosphate see synthetic route at right . Molybdenum cofactor functions directly in ethylbenzene dehydrogenase , glyceraldehyde 3 phosphate ferredoxin oxidoreductase , and respiratory arsenate reductase In animals and plants these enzymes use molybdenum bound at the active site in a tricyclic molybdenum cofactor . All molybdenum using enzymes so far identified in nature use this cofactor, save for the phylogenetically ancient molybdenum nitrogenase s, which fix nitrogen in some bacteria and cyanobacteria . ref http pathway.gramene.org META NEW IMAGE?type COMPOUND&object CPD 4 Str ... more details
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