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Open AccessJournal ArticleDOI

On the structure and function of nitrogenase from Clostridium pasteurianum W5

TLDR
The EPR spectrum of AzoFd and that of the combination of the two nitrogenase components undergoes characteristic changes upon addition of MgATP2− as mentioned in this paper.
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This article is published in Biochemical and Biophysical Research Communications.The article was published on 1972-09-26 and is currently open access. It has received 41 citations till now. The article focuses on the topics: Low protein & Tetramer.

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Isolation of an iron-molybdenum cofactor from nitrogenase

TL;DR: The FeMoCo might be used as a model for synthesizing catalysts for chemical nitrogen fixation and knowledge of the structure of this cofactor should be useful for understanding the role of molybdenum at the active site of nitrogenase, role of ligands close to moly bdenum in electron and proton transfer, and the catalytic mechanism of nitrogen fixation.
Journal ArticleDOI

Catalytic formation of a nitrogenase iron-sulfur cluster.

TL;DR: In vitro results support the proposal that NifS activity provides the inorganic sulfide necessary for in vivo formation of the nitrogenase metalloclusters.
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Nitrogenase. IV. Simple method of purification to homogeneity of nitrogenase components from Azotobacter vinelandii.

TL;DR: Extracts of Azotobacter vinelandii have been fractionated by simple techniques to obtain highly purified components of nitrogenase, which form aggregated species upon exposure to air.
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Electron-Paramagnetic-Resonance Studies on Nitrogenase

TL;DR: The results indicate that the role of the azoferredoxin · ATP complex may not be confined solely to the function of an electron carrier for the nitrogenase reaction.
References
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Journal ArticleDOI

Determination of serum proteins by means of the biuret reaction.

TL;DR: An investigation of the biochemical changes following experimental liver injury felt the need of a simple, rapid, and accurate method for determining the protein fractions in small amounts of serum and began with Kingsley’s biuret procedure.
Journal ArticleDOI

A micro biuret method for protein determination; determination of total protein in cerebrospinal fluid.

TL;DR: A rapid and convenient colorimetric method for the determination of small amounts of protein, based on the biuret reaction and readings at 330 mμ, is described.
Journal ArticleDOI

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

TL;DR: Experiments suggest that a definite association of two Fe proteins and one FeMo protein is functional in the active enzyme complex, and the idea that there are two distinct sites on nitrogenase, one concerned with N(2) activation and the other with activated electron transport is suggested.
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