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Topic: Nitrogenase


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  Maturation of Nitrogenase: a Biochemical Puzzle -- Rubio and Ludden 187 (2): 405 -- The Journal of Bacteriology
Purification and characterization of the inactive MoFe protein (NifB-Kpl) of the nitrogenase from nifB mutants of Klebsiella pneumoniae.
Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii.
Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase.
jb.asm.org /cgi/content/full/187/2/405   (0 words)

  
  Bibliography of
Synthesis of nitrogenase in mutants of the cyanobacterium Anabaena sp.
Purification and characterization of nitrogenase from a delta nifW strain of Azotobacter vinelandii.
In vitro synthesis of the iron-molybdenum cofactor of nitrogenase.
www.k-state.edu /bchem/gbg/ldlab/bibiol.html   (3940 words)

  
 Mo-nitrogenase component I
Allen, R.M., Chatterjee, R., Madden, M.S., Ludden, P.W. and Shah, V.K. Biosynthesis of the iron-molybdenum cofactor of nitrogenase.
Yousafzai, F.K., Buck, M. and Smith, B.E. Isolation and characterization of nitrogenase MoFe protein from the mutant strain pHK17 of Klebsiella pneumoniae in which the two bridging cysteine residues of the P­clusters are replaced by the non­coordinating amino acid alanine.
Kim, J., Woo, D. and Rees, D.C. X­ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0­Å resolution.
metallo.scripps.edu /PROMISE/NITROGENASE1.html   (0 words)

  
 Mo-nitrogenase component II
Component II has ATP­binding site(s) and one [Fe ] cluster per homodimer: it supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component I. The Fe protein alone binds but does not hydrolyse 2MgATP or 2MgADP and the binding of these nucleotides is competitive [2].
Kim, J. and Rees, D.C. Nitrogenase and biological nitrogen fixation.
Fu, W.G., Morgan, T.V., Mortenson, L.E. and Johnson, M.K. Resonance Raman studies of the [4Fe-4S] to [2Fe-2S] cluster conversion in the iron protein of nitrogenase.
metallo.scripps.edu /PROMISE/NITROGENASE2.html   (0 words)

  
 Nitrogenase
The enzyme nitrogenase catalyses the conversion of atmospheric, gaseous dinitrogen (N
In the next few pages I hope to provide some insight into the structure of Nitrogenase and the most reccently proposed mechanism of N
Next: An overview of the structure of nitrogenase.
www.geocities.com /nitrogenase653/Nitrogenase.htm   (360 words)

  
 Nitrogenase Structure
The complete reaction for the fixation of dinitrogen by nitrogenase is accepted as follows:
+ 2 NH Nitrogenase is a tetramer protein consisting of two identical Fe cluster and FeMo cluster subunits.
Next: An overview of the possible mechanisms of nitrogenase.
www.geocities.com /nitrogenase653/structure.htm   (0 words)

  
 Nitrogenase compound - Memory Alpha, the Star Trek Wiki
Nitrogenase compound - Memory Alpha, the Star Trek Wiki
Nitrogenase compound is a substance based on the enzyme nitrogenase.
In 2373, Captain Kathryn Janeway and Commander Chakotay were on a mission to collect nitrogenase compounds when their shuttle, the Sacajawea, crashed due to a magnetic storm.
memory-alpha.org /en/wiki/Nitrogenase_compound   (0 words)

  
 Dromgoole et al: Nitrogenase activity associate . . .
Abstract Nitrogenase activity, measured as acetylene reduction, was recorded at rates up to 1028 nmol.h \g * dry weight for Codium adhaerens (Cabr.) Ag.
In both species the ability to reduce acetylene is invariably associated with the presence of a heterocystous blue-green alga, Calothrix sp., epiphytic or embedded in the Codium thallus.
Nitrogenase and net photosynthesis of the Codium-Calothrix system have different steady-state responses to light intensity, and the kinetics of the two processes also differ in that nitrogenase is slow to respond to illumination or darkening.
www.rsnz.org /publish/nzjmfr/1978/2.php   (249 words)

  
 ASU News & Information from the Office of Media Relations and Public Information
Though biochemists have previously concluded that nitrogenase and enzymes involved in photosynthesis have structural similarities and thus appear to be related, these latter "uncharacterized" genes appear to reveal enzymes whose metabolic properties are as yet unknown.
The analysis suggests that the genes that code for neither nitrogenase nor enzymes in photosynthesis may be "relics," coding for metabolic pathways that are ancestral to both photosynthesis and nitrogen fixation.
Nitrogenase is a very complex enzyme system that actually breaks molecular nitrogen's triple bond -- one of the strongest bonds in nature," he said.
www.asu.edu /news/research/bacterial_genomes_040704.htm   (951 words)

  
 New Page 1
The process of nitrogen fixation involves the breaking of the triple bond between two nitrogen atoms with the addition of 6 electrons and 6 protons to form 2 molecules of ammonia.
Although nitrogenase catalyzes basically the reaction given in equation 1, the ability to accomplish such an energetically unfavorable reduction requires a substantial energy input in addition to the reductant which provides the electrons.
Protection of the nitrogenase complex from oxygen since it has been shown that the complex is sensitive to destruction by molecular oxygen.
www.auburn.edu /~locyrob/teaching/biol7240/nfix/nitrogenase.html   (278 words)

  
 Glycolytic Flux Is Adjusted to Nitrogenase Activity in Nodules of Detopped and Argon-Treated Alfalfa Plants -- Curioni ...
to the nodules is responsible for the decline in nitrogenase activity.
Drevon JJ, Hartwig UA (1997) Phosphorus deficiency increases the argon-induced decline of nodule nitrogenase activity in soybean and alfalfa.
Weisbach C, Hartwig UA, Heim I, Nösberger J (1996) Whole-nodule carbon metabolites are not involved in the regulation of oxygen permeability and nitrogenase activity in white clover nodules.
www.plantphysiol.org /cgi/content/full/119/2/445   (4965 words)

  
 Nitrogenase Activity in Alnus incana Root Nodules. Responses to O2 and Short-Term N2 Deprivation -- Lundquist 122 (2): ...
Silvester WB, Silvester JK, Torrey JG (1988) Adaptation of nitrogenase to varying oxygen tension and the role of the vesicle in root nodules of Alnus incana ssp.
Silvester WB, Winship LJ (1990) Transient responses of nitrogenase to acetylene and oxygen in actinorhizal nodules and cultured Frankia.
Tjepkema JD, Murry MA (1989) Respiration and nitrogenase activity in nodules of Casuarina cunninghamiana and cultures of Frankia sp.
www.plantphysiol.org /cgi/content/full/122/2/553   (4369 words)

  
 Nitrogen Fixation   (Site not responding. Last check: )
Nitrogenase has two readily separable components, dinitrogenase (also know as MoFe protein, or component 1) and dinitrogenase reductase (Fe protein or component 2).
Alternate nitrogenase enzymes are know that contain vanadium or iron in place of molybdenum.
The nitrogenase complex is not specific, acting to reduce a number of other compounds including acetylene, cyanide, and azide.
www.soils.agri.umn.edu /academics/classes/soil3612/Nitrogen_Fixation/Nitrogenase.htm   (318 words)

  
 Structural models for the metal centers in the nitrogenase molybdenum-iron protein -- Kim and Rees 257 (5077): 1677 -- ...
Structural models for the nitrogenase FeMo-cofactor and P-clusters are proposed based on crystallographic analysis of the nitrogenase molybdenum-iron (MoFe)-protein from Azotobacter vinelandii at 2.7 angstrom resolution.
Accumulation of 99Mo-containing Iron-Molybdenum Cofactor Precursors of Nitrogenase on NifNE, NifH, and NifX of Azotobacter vinelandii.
Accumulation of 55Fe-Labeled Precursors of the Iron-Molybdenum Cofactor of Nitrogenase on NifH and NifX of Azotobacter vinelandii.
www.sciencemag.org /cgi/content/abstract/257/5077/1677   (1053 words)

  
 Nitrogen fixation - EvoWiki
This indicates that the nitrogenase subunits are not tailor-made for the FeMo-co cluster.
What this system illustrates is that the 2 distinct functional components of nitrogenase systems (a reductase coupled to some energy source, and an enzyme for channeling binding nitrogen and channeling the electrons of the reductase to N2) can in fact have other cellular functions.
Additional clues to the early origins of this system are available from two distinct clades of nitrogenase paralogs: one group comprised of genes essential to photosynthetic pigment biosynthesis, and an additional group of uncharacterized genes present in methanogens and some photosynthetic bacteria.
wiki.cotch.net /index.php?title=Nitrogen_fixation&redirect=no   (2184 words)

  
 Botany online: Interactions of Plants and Bacteria — Nitrogen Fixation
Molybdenum nitrogenase (Mo­nitrogenase), which is found in all nitrogen fixing organisms, consists of two components: component I [nitrogenase molybdenum-iron (MoFe) protein, or dinitrogenase], and component II [nitrogenase iron (Fe) protein, or dinitrogenase reductase] [1; see list of reviews on structure and function of Mo­nitrogenase].
The electron transport chain of the plant cell has to be in tune with that of the nitrogenase, and finally.
Nitrogenase produces ammonia, a heavy cytotoxin, that the bacteria pass on to the plant cell.
www.biologie.uni-hamburg.de /b-online/e34/34b.htm   (1839 words)

  
 NITROGEN FIXATION
Nitrogenase is not very fast (the turnover number is around 50 moles/min per mole of Mo) and so about 2-5% of the total cell protein is nitrogenase.
Nitrogenase will reduce many small molecules with triple bonds in addition to nitrogen.
In practice nitrogenase is usually assayed by its ability to reduce acetylene, CHºCH, to ethylene, CH, which is easily detected by gas chromatography.
www.science.siu.edu /microbiology/micr425/425Notes/12-NitrFix.html   (1340 words)

  
 Biochemistry at Virginia Tech - Faculty
NITROGENASE CAUGHT IN ACTION: Intermediates in nitrogen fixation reaction are finally trapped.
Nitrogenase is the catalytic component of biological nitrogen fixation.
The laboratory is housed in the new Fralin Biotechnology Center and is equipped with state of the art facilities for fermentation, anaerobic purification and handling of oxygen sensitive proteins, recombinant DNA techniques, and computer-assisted molecular modelling of three-dimensional structures.
www.biochem.vt.edu /faculty.php?lname=Dean&view=yes   (547 words)

  
 Biological Nitrogen Fixation at the FeMo-cofactor of Nitrogenase
Biological Nitrogen Fixation at the FeMo-cofactor of Nitrogenase
The enzyme nitrogenase was the target of my Ph.D. work with Peter Blöchl.
Nitrogenase, a bacterial enzyme, is able to convert atmospheric nitrogen into ammonia and thus to break the strongest chemical bond in nature.
www.cse.scitech.ac.uk /ccg/j.kaestner/nitrogenase.html   (375 words)

  
 How Does Protein Architecture Facilitate the Transduction of ATP Chemical-Bond Energy into Mechanical Work? The Cases ...   (Site not responding. Last check: )
Nitrogenase catalyzes biological nitrogen fixation whereas BtuCD transports vitamin B12 across membranes.
The lowest-frequency modes of the nitrogenase iron protein and of the ATP binding-cassette transporter BtuCD protein are found to link the functionally critical domains, and these modes are suggested to be responsible for (at least the initial stages) large-scale ATP-coupled conformational changes.
Nitrogenase consists of two metalloproteins, a 64 kDa iron protein (Fe protein) and a 240 kDa molybdenum protein (MoFe protein) (Einsle et al., 2002; Howard and Rees, 1996; Eady, 1996).
findarticles.com /p/articles/mi_qa3938/is_200408/ai_n9421096   (874 words)

  
 Chapter 5 - Hydrogen production
Nitrogenase is responsible for nitrogen-fixation (11) and is distributed mainly among prokaryotes, including cyanobacteria, but does not occur in eukaryotes, under which microalgae are classified.
Hydrogen production catalyzed by nitrogenase occurs as a side reaction at a rate of one-third to one-fourth that of nitrogen-fixation, even in a 100% nitrogen gas atmosphere.
Since light energy is not required for water oxidation, the efficiency of light energy conversion to hydrogen gas by photosynthetic bacteria, is in principle much higher than that by cyanobacteria.
www.fao.org /docrep/w7241e/w7241e0g.htm   (2426 words)

  
 Nitrogenase gene diversity and microbial community structure: a cross-system comparison. | nodalpoint.org   (Site not responding. Last check: )
The phylogeny of nitrogenase includes branches that represent phylotypic groupings based on ribosomal RNA phylogeny, but also includes paralogous clades including the alternative, non-molybdenum, non-vanadium containing nitrogenases.
Extensive analysis of the distribution of nifH phylotypes among habitats indicates that there are characteristic patterns of nitrogen fixing microorganisms in termite guts, sediment and soil environments, estuaries and salt marshes, and oligotrophic oceans.
The broad analysis of nitrogenase genes provides a basis for developing molecular assays and bioinformatics approaches for the study of nitrogen fixation in the environment.
www.nodalpoint.org /node/1075   (294 words)

  
 BCH/PLS/PPA 609 | Lecture Twenty Two Web Notes
The actual N fixation is carried out by the prokaryote and is catalyzed by an enzyme system known as the nitrogenase complex composed of dinitrogenase and dinitrogenase reductase.
The nitrogenase, like RUBISCO, is a rather sluggish enzyme and diazotrophs usually produce large amounts, up to 10% of total cellular proteins.
Nitrogenase can catalyze the reduction of other substrates with structures similar to dinitrogen.
www.uky.edu /~dhild/biochem/22/lect22.html   (1934 words)

  
 Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter ...   (Site not responding. Last check: )
Ammonium-induced nitrogenase switch-off and ADP-ribosylation of NifH in the wild-type strain B10S (a) and the glnB–glnK mutant strain TD166 (b).
Yakunin, A. and Hallenbeck, P. Short-term regulation of nitrogenase activity by NH in Rhodobacter capsulatus: multiple in vivo nitrogenase response to NH addition.
Yakunin, A. and Hallenbeck, P. AmtB is necessary for NH -induced nitrogenase switch-off and ADP-ribosylation in Rhodobacter capsulatus.
mic.sgmjournals.org /cgi/content/full/149/8/2203   (5308 words)

  
 The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures -- Chan et al. 260 (5109): 792 -- Science
Structures recently proposed for the FeMo-cofactor and P-cluster pair of the nitrogenase molybdenum-iron (MoFe)-protein from Azotobacter vinelandii have been crystallographically verified at 2.2 angstrom resolution.
Nitrogen Fixation: The Mechanism of the Mo-Dependent Nitrogenase.
Nitrogenase MoFe-Protein at 1.16 A Resolution: A Central Ligand in the FeMo-Cofactor.
www.sciencemag.org /cgi/content/abstract/260/5109/792   (774 words)

  
 Title page for ETD etd-04282003-101336
Nitrogenase is a complex metal-containing enzyme that catalyzes the conversion of nitrogen gas to ammonia.
During nitrogenase catalysis the Fe protein and the molybdenum-iron protein associate and dissociate in a manner resulting in the hydrolysis of two molecules of MgATP and the transfer of at least one electron to the MoFe protein.
The role of nucleotide binding and hydrolysis in nitrogenase catalysis is one of the most fascinating aspects of nitrogenase function.
www.montana.edu /etd/available/sen_0805.html   (708 words)

  
 Response of the Endophytic Diazotroph Gluconacetobacter diazotrophicus on Solid Media to Changes in Atmospheric Partial ...
in an inhibition of nitrogenase activity (14, 21, 26).
Reis and Döbereiner (40) measured nitrogenase activity in liquid cultures of G.
Nitrogenase activity and regeneration of the cellular ATP pool in Azotobacter vinelandii adapted to different oxygen concentrations.
aem.asm.org /cgi/content/full/67/10/4694   (3897 words)

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