(Q39870738)

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Nitrogenase

scientific article published on June 1974

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scholarly article

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Europe PubMed Central

15 September 2017

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Europe PubMed Central

Nitrogenase (English)

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Europe PubMed Central

15 September 2017

author name string

Eady RR

1

1 reference

Europe PubMed Central

15 September 2017

Postgate JR

2

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Europe PubMed Central

15 September 2017

language of work or name

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publication date

1 June 1974

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Europe PubMed Central

15 September 2017

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Europe PubMed Central

15 September 2017

249

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Europe PubMed Central

15 September 2017

805-810

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Europe PubMed Central

15 September 2017

460

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Europe PubMed Central

15 September 2017

https://scigraph.springernature.com/pub.10.1038/249805a0

0 references

Nitrogenase of Klebsiella pneumoniae. Inhibition of acetylene reduction by magnesium ion explained by the formation of an inactive dimagnesium-adenosine triphophate complex.

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Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins

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Control of Nitrogenase Synthesis in Klebsiella pneumoniae

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Nitrogenase of Klebsiella pneumoniae: electron-paramagnetic-resonance studies on the catalytic mechanism

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Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae

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Mössbauer spectroscopy of the nitrogenase proteins from Klebsiella pneumoniae. Structural assignments and mechanistic conclusions

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The binding of ATP and ADP by nitrogenase components from Clostridium pasteurianum

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Nitrogenase of Klebsiella pneumoniae: evidence for an adenosine triphosphate-induced association of the iron-sulphur protein

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Nitrogenase from Clostridium pasteurianum. Changes in optical absorption spectra during electron transfer and effects of ATP, inhibitors and alternative substrates

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Nitrogenase of Klebsiella pneumoniae: interaction with viologen dyes as measured by acetylene reduction

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Nitrogenase of Klebsiella pneumoniae. Interaction of the component proteins studied by ultracentrifugation

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Biological Nitrogen Fixation

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Comparative biochemistry of nitrogen fixation

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Purification and Properties of the Constituents of the Nitrogenase Complex from Clostridium pasteurianum

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Purification and some properties of molybdoferredoxin, a component of nitrogenase from Clostridium pasteurianum.

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Purification of the nitrogenase proteins from Clostridium pasteurianum

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Isolation by crystallization of the MoFe protein of Azotobacter nitrogenase

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Nitrogenase. IV. Simple method of purification to homogeneity of nitrogenase components from Azotobacter vinelandii

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Properties of azoferredoxin purified from nitrogen-fixing extracts of Clostridium pasteurianum

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The Effect of ATP upon the Oxygen Sensitivity of Nitrogenase from Azotobacter chroococcum

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Properties of a soluble nitrogenase in Azotobacter

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Effect of non-haem iron proteins and cytochrome C from Azotobacter upon the activity and oxygen sensitivity of Azobacter nitrogenase.

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Nitrogenase. II. Changes in the EPR signal of component I (iron-molybdenum protein) of Azotobacter vinelandii nitrogenase during repression and derepression

1 reference

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Evidence for a catalytic-centre heterogeneity of molybdoferredoxin from Clostridium pasteurianum

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Assessment of Compositional Relatedness between Proteins

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Estimation of primary sequence homology from amino acid composition of evolutionary related proteins

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Electron paramagnetic resonance studies on nitrogenase. I. The properties of molybdoferredoxin and azoferredoxin

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Electron paramagnetic resonance of nitrogenase and nitrogenase components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP.

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The purification and some properties of the molybdenum-iron protein of Chromatium nitrogenase

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Structural investigation of nitrogenase components from Clostridium pasteurianum and comparison with similar components of other organisms

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Measurement of the oxidation reduction potential of the EPR detectable active centre of the molybdenum iron protein of Chromatium nitrogenase

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Oxidation reduction properties of nitrogenase from Clostridium pasteurianum W5.

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Electron paramagnetic resonance studies on nitrogenase. II. Interaction of adenosine 5'-triphosphate with azoferredoxin

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An effect of magnesium adenosine 5'-triphosphate on the structure of azoferredoxin from Clostridium pasteurianum.

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Chemical characterization of high potential iron proteins from Chromatium and Rhodopseudomonas gelatinosa

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Electron transport to nitrogenase in Azotobacter chroococcum: Azotobacter flavodoxin hydroquinone as an electron donor

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The nitrogen fixation system of photosynthetic bacteria II. Chromatium nitrogenase activity linked to photochemically generated assimilatory power

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ATP hydrolysis and electron transfer in the nitrogenase reaction with different combinations of the iron protein and the molybdenum-iron protein

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On the structure and function of nitrogenase from Clostridium pasteurianum W5.

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Electron paramagnetic resonance studies on nitrogenase. 3. Function of magnesium adenosine 5'-triphosphate and adenosine 5'-diphosphate in catalysis by nitrogenase.

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Evidence from mossbauer spectroscopy for the role of iron in nitrogen fixation

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Pyruvate-supported acetylene and sulfate reduction by cell-free extracts of Desulfovibriodesulfricans

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Reduction of N2 by complementary functioning of two components from nitrogen-fixing bacteria

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Chromosomal integration of Klebsiella nitrogen fixation genes in Escherichia coli

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Some properties of purified nitrogenase of Azotobacter chroococcum

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Resolution of Nitrogenase of Mycobacterium flavum 301 into Two Components and Cross Reaction with Nitrogenase Components from Other Bacteria

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Nitrogenase Activity in Heterocysts of Blue–Green Algae

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Soluble Nitrogenase from Vegetative Cells of the Blue–Green Alga Anabaena cylindrica

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Characteristics of nitrogenase activity in broken cell preparations of the blue-green alga Gloeocapsa sp. LB 795.

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Kinetics of acetylene and CN- reduction by the N2-fixing system of Rhizobium lupini

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Compatibility of the components of nitrogenase from soybean bacteroids and free-living nitrogen-fixing bacteria

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Differentiation in Nostoc muscorum: nitrogenase is synthesized in heterocysts

1 reference

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Subunit structure of azoferredoxin from Clostridium pasteurianum W5

1 reference

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inferred from DOI database lookup

Inhibition of nitrogenase-catalyzed reductions

1 reference

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inferred from DOI database lookup

Identifiers

10.1038/249805A0

1 reference

Europe PubMed Central

15 September 2017

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1 reference

Europe PubMed Central

15 September 2017

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