Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii. - Wikidata - awgldk - TriplyDB

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

http://www.wikidata.org/entity/Q34352409

about

Decoupled genomic elements and the evolution of partner quality in nitrogen-fixing rhizobia Selenol binds to iron in nitrogenase iron-molybdenum cofactor: an extended x-ray absorption fine structure study Differential accumulation of nif structural gene mRNA in Azotobacter vinelandii.Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii.ApoNifH functions in iron-molybdenum cofactor synthesis and apodinitrogenase maturation.N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.Analysis of Azotobacter vinelandii strains containing defined deletions in the nifD and nifK genes.Requirement of NifX and other nif proteins for in vitro biosynthesis of the iron-molybdenum cofactor of nitrogenase.The genes encoding the delta subunits of dinitrogenases 2 and 3 are required for mo-independent diazotrophic growth by Azotobacter vinelandii.In Azotobacter vinelandii hydrogenase, substitution of serine for the cysteine residues at positions 62, 65, 294, and 297 in the small (HoxK) subunit affects H2 oxidation [corrected]The hoxZ gene of the Azotobacter vinelandii hydrogenase operon is required for activation of hydrogenase Isolation and characterization of nitrogenase MoFe protein from the mutant strain pHK17 of Klebsiella pneumoniae in which the two bridging cysteine residues of the P-clusters are replaced by the non-coordinating amino acid alanine.Altered nitrogenase MoFe proteins from Azotobacter vinelandii. Analysis of MoFe proteins having amino acid substitutions for the conserved cysteine residues within the beta-subunit Site-directed mutagenesis of the Klebsiella pneumoniae nitrogenase. Effects of modifying conserved cysteine residues in the alpha- and beta-subunits.Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe protein.Enterococcus faecalis sufCDSUB complements Escherichia coli sufABCDSE.

P2860

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P2860

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

http://www.wikidata.org/entity/Q34352409

description

1987 nî lūn-bûn

@nan

1987 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1987 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1987年の論文

@ja

1987年論文

@yue

1987年論文

@zh-hant

1987年論文

@zh-hk

1987年論文

@zh-mo

1987年論文

@zh-tw

1987年论文

@wuu

name

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@ast

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@en

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@nl

type

label

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@ast

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@en

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@nl

prefLabel

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@ast

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@en

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@nl

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PNAS.84.20.7066

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

@en

P2093

Brigle KE

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Cantwell JS

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Dean DR

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Newton WE

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Setterquist RA

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Weiss MC

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P2860

DNA sequencing with chain-terminating inhibitors

High resolution two-dimensional electrophoresis of proteins

A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments

Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase

Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle.

Isolation of an iron-molybdenum cofactor from nitrogenase.

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.

Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae.

Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii

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

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7066-7069

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scholarly article

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10.1073/PNAS.84.20.7066

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20

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84

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16593879

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299230

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