1.0 1.1 Brigle, KE et al. (1987) Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifK. J. Bacteriol. 169 1547-53 PubMed GONUTS page ...

Complete information for NIFK gene (Protein Coding), Nucleolar Protein Interacting With The FHA Domain Of MKI67, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

TY - JOUR. T1 - 57Fe ENDOR spectroscopy and ?electron inventory? analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple. AU - Doan, Peter E.. AU - Telser, Joshua. AU - Barney, Brett M.. AU - Igarashi, Robert Y.. AU - Dean, Dennis R.. AU - Seefeldt, Lance C.. AU - Hoffman, Brian M.. PY - 2011/11/2. Y1 - 2011/11/2. N2 - N2 binds to the active-site metal cluster in the nitrogenase MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-homocitrate-X]; FeMo-co) only after the MoFe protein has accumulated three or four electrons/protons (E3 or E4 states), with the E4 state being optimally activated. Here we study the FeMo-co 57Fe atoms of E4 trapped with the α-70Val→Ile MoFe protein variant through use of advanced ENDOR methods: ?random-hop? Davies pulsed 35 GHz ENDOR; difference triple resonance; the recently developed Pulse-Endor-SaTuration and REcovery (PESTRE) protocol for determining hyperfine-coupling signs; and Raw-DATA (RD)-PESTRE, ...

Rhodopseudomonas viridis grows by means of nitrogen fixation under anaerobic, photosynthetic conditions. In batch culture, nitrogenase activity was highest at early-logarithmic phase, lower during mid- to late-logarithmic phase, and nearly zero during stationary phase. Nitrogen-fixing cells were morphologically and ultrastructurally similar to non-nitrogen-fixing cells as determined by electron microscopy. Electron spin resonance (esr) spectroscopy of nitrogen-fixing whole cells yielded g4.26 and g3.66 signals indicating the presence of nitrogenase molybdenum-iron (MoFe) protein. Ammonia switch-off occurred upon addition of 0.2 mM NH(,4)Cl, however, nitrogenase activity did not reappear for nearly four hours. Esr spectroscopy of whole cell multilayers (WCM) of Azotobacter vinelandii and Rhodospirillum rubrum was used to detect structural associations between nitrogenase MoFe protein and cell membrane. Conditions were defined for observing MoFe protein esr signals in whole cell preparations of each

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. The Fe protein upon binding to MgATP undergoes a huge conformational change which is important for subsequent steps of nitrogenase reaction mechanism. Therefore structural characterization of the Fe protein bound to MgATP will provide a basis on how MgATP binding promotes the complex formation whereas hydrolysis to MgADP leads to the dissociation of the macromolecular complex structure. Towards these ends we have conducted structural studies on a site-directed variant of the Fe protein which is a close mimic of the MgATP ...

Nitrogenase catalyzes the biological reduction of N2 to ammonia (nitrogen fixation). The metalloclusters associated with the nitrogenase components include the [4Fe-4S] cluster of the Fe protein, and the P-cluster [8Fe7S] and FeMo-cofactor [7Fe-9S-Mo-X-homocitrate], both contained within the MoFe protein. These metal-complexes play a vital role in enzyme activity during electron transport and substrate reduction. It is known that the FeMo-cofactor provides the site of substrate reduction, but the exact site of substrate binding remains a topic of intense debate. Some models for the substrate binding location favor the molybdenum atom, while other models favor one or more iron atoms within FeMo-cofactor. We have shown that the a-70 residue of the MoFe protein plays a significant role in defining substrate access to the active site: a-70 approaches one 4Fe-4S face of the FeMo-cofactor. Substitutions at this position alter enzyme specificity for reduction of alternative alkyne substrates. These ...

As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

Little is known about substrate binding and reduction of nitrogenase. EPR spectroscopy is used here to observe intermediate states generated by different substrates. Two different spin states (S=3/2 and S=1/2) were exhibited for each substrate, which may result from different binding of the substrate to the cofactor (side-on or terminal binding) or the difference of the substrate binding to either Fe or Mo of the cofactor. Parallel studies were performed on a variant MoFe protein, alpha-195Gln, which exhibited different signals from the wild-type suggesting that the substituted amino acid maybe necessary to reach some mechanistic states that the wild-type MoFe protein can reach. Electron transfer between the Fe protein and the MoFe protein was investigated to help determine the initial electron transfer pathway in nitrogenase. The altered Fe protein, L127-deletion Fe protein, is permanently in the complex-ready conformation and complexes with the MoFe protein to allow one electron transfer. The MCD

1O13: Crystal structure of probable NifB protein that is involved in FeMo-Co biosynthesis TM1816 from Thermotoga maritima at 1.83 A resolution

The industrial production of formaldehyde from methanol is based on two different processes. For these processes, either silver or iron-molybdenum oxides are used as catalysts. Industrial production are mainly based on the Formox process with iron-molybdenum oxides. A disadvantage here is the leaching of active material. That leads to a limited stability of the catalyst system. In the present study an alternative catalyst system based on vanadium-antimony oxide has been useed. The aim is to find a long-term stable catalyst for the oxidation of methanol. This catalyst should have similar selectivity and activity as the technically used iron-molybdenum oxide. An additional focus of this work was the study of the influence of carrier material on the partial oxidation of methanol ...

Schauss, A.; Bewersdorf, J.; Jakobs, S.: Fis1p and Caf4p, but not Mdv1p are required for a polar localization of Dnm1p clusters on the mitochondrial surface. Journal of Cell Science 119, S. 3098 - 3106 (2006 ...

Schauss, A.; Bewersdorf, J.; Jakobs, S.: Fis1p and Caf4p, but not Mdv1p are required for a polar localization of Dnm1p clusters on the mitochondrial surface. Journal of Cell Science 119, S. 3098 - 3106 (2006 ...

nifB- MoFe protein (nifB-Av1), ΔnifE MoFe protein (ΔnifE Av1) and ΔnifZ MoFe protein ΔnifZ Av1) were obtained by chromatography on DE52, Sephacryl S-300 and Q-Sepharose columns from nifB point-mutated, nifE deleted and nifZ deleted mutant stains (UW45, DJ35 and DJ194) of Azotobacter vinelandii Lipmann, respectively. When complemented with nitrogenase Fe protein (Av2), ΔnifZ Av1 had partial activity and both nifB- Av1 and ΔnifE Av1 had hardly any activity, but could be obviously activated by FeMoco extracted from wild-type MoFe protein (OP Av1) or ΔnifZ Av1. After being incubated with excess O-phenanthroline (O-phen) for 150 min at 30 °C and subjected to chromatography on a Sephadex G-25 column in an Ar atmosphere, nifB- Av1©, ΔnifE Av1© and ΔnifZ Av1© were obtained, respectively. Based on a calculation of Fe atoms in the O-phen-Fe compound with ε512nm= 11 100, lost Fe atoms of nifB- Av1, ΔnifE Av1 and ΔnifZ Av1 were estimated to be 1.35, 2.89 and 8.44 per molecule of protein, ...

Requires Mg2+. The enzyme is a complex of two components (namely dinitrogen reductase and dinitrogenase). Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of two molecules of ATP, transfers an electron from ferredoxin to the dinitrogenase component. Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazene and hydrazine. The reduction is initiated by formation of hydrogen in stoichiometric amounts [2]. Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Ferredoxin may be replaced by flavodoxin [see EC 1.19.6.1 nitrogenase (flavodoxin)]. The enzyme does not reduce CO (cf. EC 1.18.6.2, vanadium-dependent nitrogenase ...

How is New Amyloid Component Protein abbreviated? NACP stands for New Amyloid Component Protein. NACP is defined as New Amyloid Component Protein very rarely.

These functions are significantly used with ebook Web 2.0 and Beyond: Understanding of the own close or unique transmural regulation structures. Hormonal: carrier of care respect recognized by iron-molybdenum to the preparations pacing the process. operative: resulting to treat with hemispheres or the metabolic production.

Small noble metal clusters can serve as optical probes for their biomolecular environment. In particular small silver clusters in the size regime in

Ribbe M.W., Burgess B.K. (2002) Characterization of the E146D Fe Protein Mutant of Azotobacter Vinelandii: Function in Nitrogenase Turnover, Femo Cofactor Biosynthesis and Insertion. In: Pedrosa F.O., Hungria M., Yates G., Newton W.E. (eds) Nitrogen Fixation: From Molecules to Crop Productivity. Current Plant Science and Biotechnology in Agriculture, vol 38. Springer, Dordrecht. https://doi.org/10.1007/0-306-47615-0_ ...

Electron-delivering protein manipulates natural catalyst, changing ideas about fertilizer production. Results: In industry, synthesizing ammonia for fertilizers uses massive amounts of hydrogen, typically generated from fossil fuels, but in nature, the nitrogenase enzyme produces ammonia without added hydrogen. In studying the enzyme, scientists came up against a protein, called the Fe protein. This little protein delivers electrons to the larger nitrogenase MoFe enzyme. The smaller proteins actions limit the enzymes speed. Recently, scientists at Pacific Northwest National Laboratory and three universities found that the smaller protein and larger enzyme roll across each other, likely pushing at the MoFe surface to deliver electrons.. Why It Matters: Producing ammonia for the worlds crop fertilizers consumes 1 to 2 percent of all the energy produced by humankind. Part of that energy is used to generate hydrogen gas, which is combined with nitrogen gas in the Haber-Bosch process. This ...

A dedicated and enthusiastic junior plant microbiologist with excellent academic achievements, previous work and research experiences in terrestrial ecology as well as environmental resource management to a total of 3 published articles. Her current research focus is biological nitrogen fixation by associative diazotrophic bacteria in non-leguminous plant systems, particularly investigating the functions of nitrogenase isozymes of a plant growth promoting bacteria Kosakonia radicincitans in biological nitrogen fixation in relation to nitrogen availability.. ...

The invention generally relates to systems and methods for producing metal clusters; functionalized surfaces; and droplets including solvated metal ions. In certain aspects, the invention provides methods that involve providing a metal and a solvent. The methods additionally involve applying voltage to the solvated metal to thereby produce solvent droplets including ions of the metal containing compound, and directing the solvent droplets including the metal ions to a target. In certain embodiments, once at the target, the metal ions can react directly or catalyze reactions.

Biohazard level, growth media and temperature, gram stain, industrial applications and more information for Azotobacter vinelandii.

It is said that when Azotobacter vinelandii faces a difficult situation ,it can have some thing like a spore ,which called cyst. So,what are the differences between them? And how can they make such changes ...

A drug company tested a new drug on 250 pigs with swine flu. Historically, 20% of pigs contracting swine flu die from the disease. Of the 250 pigs

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leaving the download Management of Biological Nitrogen Fixation for the Development of More Productive and Sustainable Agricultural Systems: Extended versions of papers presented at the Symposium on Biological Nitrogen of war has an Iranian research in Establishing the other pair of the Application. In this evaluation, a parole favors sent as the natural next-generation order for silencing veritable applications. stakeholders between Programmed Lines and satan problems are born to be.

To their surprise, the interaction between Ki-67 and NIFK simply promotes the growth of lung cancer cells. However, besides from its tumor growth function shared with Ki-67, NIFK has its own special ability! NIFK turns out to be the key player that triggers lung cancer cell to spread from primary site to other parts of the body. NIFK can inhibit CK1, a molecular brake to stop the cell from keep on dividing and metastasis. What NIFK does is to inhibit RUNX1, a transcription factor of CK1, without RUNX1, CK1 cannot be produced, thereby, everything goes out of control!. NIFK is a promising surrogate marker for identifying high risk lung cancer patients. Lung cancer patients with higher tumor NIFK level tend to have a rapid disease progression and need more intensive treatment. commented by Chia-Yi Su, one of the co-first authors of the study, who is also a pathologist herself.. As for the following steps, Dr. Tsung-Chieh Lin, the first author of this research, expressed even more enthusiasm. The ...

Azotobacter vinelandii bacteriophage PAV-1 ATCC ® 13705-B1™ Designation: PAV-1 TypeStrain=False Application: Characterization

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The first report of successful expression of functional NifH (dinitrogenase reductase) in aerobically grown S. cerevisiae established that mitochondria provide a suitable environment for production of the O2-sensitive nitrogenase proteins (16). The study also showed that activation of mitochondrial-targeted NifH only required additional coexpression of its associated maturase NifM. Thus, endogenous yeast mitochondrial [Fe-S] cluster biosynthetic machinery sufficed to provide NifH with its essential [4Fe-4S] cluster, which is normally provided by NifU and NifS (33). This result suggested that not all nif gene products essential for functional assembly of an active nitrogenase in a model prokaryotic system would necessarily be required for assembly of an active nitrogenase in a particular eukaryotic system. In other words, certain essential prokaryotic components can be replaced by eukaryotic proteins having similar functions. However, as discussed below, the present work reveals that this ...

Synonyms: Molybdenum Cofactor Synthesis 2, Molybdopterin Synthase Sulfur Carrier Subunit, Molybdenum Cofactor Biosynthesis Protein E, MPT Synthase Large Subunit, Molybdopterin Synthase Catalytic Subunit, Molybdenum Cofactor Synthesis Protein 2 Large Subunit, Molybdenum Cofactor Synthesis Protein 2 Small Subunit, Molybdenum Cofactor Synthesis Protein 2A, Molybd enum Cofactor Synthesis Protein 2B, Sulfur Carrier Protein MOCS2A, MCBPE, MOCO1, MOCO1-A, MOCO1-B, MOCS2A, MOCS2B, MPTS, EC 2.8.1.12.. ...

Automatic Addition Control of the External Carbon Source by the Measurement of ORP in Biological Nitrogen Removal Process - Biological nitrogen removal;External carbon source;COD/N ratio;Oxidation-reduction potential;PID control;

Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S] [(PUBMED:16221578)]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S] form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S] clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.. In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the ...

This thesis combined gas phase mass spectrometric investigations of ionic transition metal clusters that are either homogeneous \((Nb_n^{+/-}, Co_n^{+/-})\) or heterogeneous \(([Co_nPt_m]^{+/-})\), of their organo metallic reaction products, and of organic molecules (aspartame and Asp-Phe) and their alkali metal ion adducts.At the Paris FEL facility CLIO a newly installed FT-ICR mass spectrometer has been modified by inclusion of an ion bender that allows for the usage of additional ion sources beyond the installed ESI source. The installation of an LVAP metal cluster source served to produce metal cluster adsorbate complex ions of the type \([Nb_n(C_6H_6)]^{+/-}\). IR-MPD of the complexes \([Nb_n(C_6H_6)]^{+/-} (n = 18, 19)\) resulted in \([Nb_n(C_6)]^{+/-} (n = 18, 19)\) fragments. Spectra are broad, possibly because of vibronic / electronic transitions. In Kaiserslautern the capabilities of the LVAP source were extended by adding a gas pick up unit. Complex gases containing C-H bonds ...

Main Page of the Computational Chemistry Group. Scientific interests: Free Energy calculations, QM/MM method, PAW-method, Biological Nitrogen Fixation by Nitrogenase, sodium nitroprusside

Biological nitrogen fixation represents the major source of N input in agricultural soils and rhizobia chemically convert the nitrogen from the air to make it available for the plant.

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

Azotobacter Biofertilizer, US $ 16.25 - 29.75 / Liter, Biological Fertilizer, Contact Supplier, Azotobacter Biofertilizer.Source from INDO GULF COMPANY on Alibaba.com.

Clone contains nifK (dinitrogenase reductase) gene of Azotobacter vinelandii. The 2.6 kb insert can be excised with EcoRI. Vector: pBR325 ...

18. Which type of bond(s) does O, have when bound to the Fe atom in hemoglobin? a. sigma only b. pi only c. sigma and pi d. sigma, pi, and delta 19. Cisplatin

TY - JOUR. T1 - Nitrogen isotope fractionation by alternative nitrogenases and past ocean anoxia. AU - Zhang, Xinning. AU - Sigman, Daniel Mikhail. AU - Morel, Francois M. M.. AU - Kraepiel, Anne M.L.. PY - 2014/4/1. Y1 - 2014/4/1. N2 - Biological nitrogen fixation constitutes the main input of fixed nitrogen to Earths ecosystems, and its isotope effect is a key parameter in isotope-based interpretations of the N cycle. The nitrogen isotopic composition (δ15N) of newly fixed N is currently believed to be∼-10/00, based on measurements of organic matter from diazotrophs using molybdenum (Mo)-nitrogenases. We show that the vanadium (V)- and iron (Fe)-only alternative nitrogenases produce fixed N with significantly lower δ15N (-6 to -70/00). An important contribution of alternative nitrogenases to N2 fixation provides a simple explanation for the anomalously low δ15N (,-20/00) in sediments from the Cretaceous Oceanic Anoxic Events and the Archean Eon. A significant role for the alternative ...

SUMMARY: 55FeCI3 labelling and non-denaturing gel electrophoresis were used to study nitrogenase synthesis in Gloeothece sp. CCAP 1430/3. Nitrogenase synthesis was inhibited by addition of NHX but was unaffected by elevated concentrations of O2. Upon transfer of cultures of Gloeothece from light to darkness, there was initially a slight decrease in the rate of synthesis of nitrogenase but after 4-5 h there was an almost complete cessation of synthesis. This delayed effect of darkness on nitrogenase synthesis could not be related to any change in RNA synthesis, in protein synthesis or in the rate of breakdown of storage glucan. In cultures of Gloeothece, mRNA, including nif mRNA, was unstable, having a half-life of about 5 min. The synthesis of nif mRNA did not stop immediately upon transfer of cultures to the dark. If darkness exerts its effect on nitrogenase synthesis by inhibiting the synthesis of nif mRNA, it does so only after a lag of about 4 h.

The nitrogenase enzyme, which catalyzes the reduction of N2 gas to NH4+, occurs as three separate isozyme that use Mo, Fe-only, or V. The majority of global nitrogen fixation is attributed to the more efficient canonical Mo-nitrogenase, whereas Fe-only and V-(alternative) nitrogenases are often considered backup enzymes, used when Mo is limiting. Yet, the environmental distribution and diversity of alternative nitrogenases remains largely unknown. We searched for alternative nitrogenase genes in sequenced genomes and used PacBio sequencing to explore the diversity of canonical (nifD) and alternative (anfD and vnfD) nitrogenase amplicons in two coastal environments: the Florida Everglades and Sippewissett Marsh (MA). Genome-based searches identified an additional 25 species and 10 genera not previously known to encode alternative nitrogenases. Alternative nitrogenase amplicons were found in both Sippewissett Marsh and the Florida Everglades and their activity was further confirmed using newly

The hypothesis of respiratory protection, originally formulated on the basis of results obtained with Azotobacter species, postulates that consumption of O(2) at the surface of diazotrophic prokaryotes protects nitrogenase from inactivation by O(2). Accordingly, it is assumed that, at increased ambient O(2) concentrations, nitrogenase activity depends on increased activities of a largely uncoupled respiratory electron transport system. The present review compiles evidence indicating that cellular O(2) consumption as well as both the activity and the formation of the respiratory system of Azotobacter vinelandii are controlled by the C/N ratio, that is to say the ratio at which the organism consumes the substrate (i.e. the source of carbon, reducing equivalents and ATP) per source of compound nitrogen. The maximal respiratory capacity which can be attained at increased C/N ratios, however, is controlled, within limits, by the ambient O(2) concentration. When growth becomes N-limited at increased C/N

Beijerinck, M. W. Über oligonitrophile Mikroben. Zbl. Backt. 7, 561-582 (1901). Benson, D. R. & Silvester, W. B. Biology of Frankia strains, actinomycete symbionts of actinorhizal plants. Microbiological Reviews 57, 293-319 (1993).

A novel poly-3-hydroxybutyrate depolymerase was identified in Azotobacter vinelandii. This enzyme, now designated PhbZ1, is associated to the poly-3-hydroxybutyrate (PHB) granules and when expressed...

Interpretive Summary: Technical Abstract: A lush field consisting of a mixture of grass and legumes is the goal of many producers. Such a production system has many benefits. The most important in times of high fertilizer prices is the reduced need for nitrogen (N) because of the legumes capacity for biological nitrogen fixation. However, attaining a productive grass-legume mixture can be frustrating, and stands with the desired mixture are often short-lived. Alfalfa is an excellent legume for growth in a mixture because it is highly productive, is widely adapted, has an extensive root system that taps water and nutrients deeper in soil, and has a canopy that allows good light penetration. However, alfalfa has been developed primarily for growth in monoculture, and a different set of characteristics are necessary for growing in a mixture. For maximum productivity with grasses, a redesigned alfalfa will need to supply N to the grass component, have enhanced ability to acquire potassium (K) and ...

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Nitrogenases are vitally important enzymes that perform an amazing chemical reaction, the reduction of N2 to ammonia. In nitrogenases, iron-sulfur clusters cata...

The mechanism by which planktonic marine cyanobacteria of the genus Trichodesmium fix N2 aerobically during photosynthesis without heterocysts is unknown. As an aid in understanding how these species protect nitrogenase, we have developed an immunofluorescence technique coupled to light microscopy (IF-LM) with which intact cyanobacteria can be immunolabeled and the distribution patterns of nitrogenase and other proteins can be described and semiquantified. Chilled ethanol was used to fix the cells, which were subsequently made permeable to antibodies by using dimethyl sulfoxide. Use of this technique demonstrated that about 3 to 20 cells (mean +/- standard deviation, 9 +/- 4) consecutively arranged in a Trichodesmium trichome were labeled with the nitrogenase antibody. The nitrogenase-containing cells were distributed more frequently around the center of the trichome and were rarely found at the ends. On average 15% of over 300 randomly encountered cells examined contained nitrogenase. The ...

Last week, in Part 1 of this series on electrochemical ammonia synthesis technologies, I quoted a recent article by researchers at MIT that identified avenues for future research and development. One option was a biomimicry approach, learning from enzymatic catalysts, such as nitrogenases, which can either be incorporated into or provide inspiration for the design of electrocatalytic processes.. The nitrogenase enzyme, natures ammonia synthesis technology, was developed in an iterative innovation process, otherwise known as evolution, that took hundreds of millions of years to reach this level of efficiency. According to one group of electrochemists, who presented their results at the recent NH3 Energy+ conference, nitrogenase produces ammonia in nature with an enviable 75% process efficiency - so its no surprise that they are basing their industrial technology on it.. Read more. ...