Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein (Q41699478)

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scientific article published on November 1999

Language	Label	Description	Also known as
English	Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein	scientific article published on November 1999

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scholarly article

1 reference

Europe PubMed Central

7 October 2017

Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein (English)

1 reference

Europe PubMed Central

7 October 2017

Azotobacter vinelandii

object named as

Azotobacter vinelandii

1 reference

based on heuristic

inferred from title

author name string

Jung YS

1

1 reference

Europe PubMed Central

7 October 2017

Gao-Sheridan HS

2

1 reference

Europe PubMed Central

7 October 2017

Christiansen J

3

1 reference

Europe PubMed Central

7 October 2017

Dean DR

4

1 reference

Europe PubMed Central

7 October 2017

Burgess BK

5

1 reference

Europe PubMed Central

7 October 2017

language of work or name

0 references

publication date

1 November 1999

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Europe PubMed Central

7 October 2017

number of pages

9

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

7 October 2017

274

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Europe PubMed Central

7 October 2017

45

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Europe PubMed Central

7 October 2017

32402-32410

1 reference

Europe PubMed Central

7 October 2017

An electron transport factor from Clostridiumpasteurianum

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Iron-sulfur clusters: nature's modular, multipurpose structures

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Structural and Functional Aspects of Metal Sites in Biology

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Ironminus signSulfur Proteins with Nonredox Functions

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An iron-sulfur cluster plays a novel regulatory role in the iron-responsive element binding protein

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Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress

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Redox control of gene expression involving iron-sulfur proteins. Change of oxidation-state or assembly/disassembly of Fe-S clusters?

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SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form

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Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription

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Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding

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DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen.

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X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution

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Two open reading frames (ORFs) identified near the hydrogenase structural genes in Azotobacter vinelandii, the first ORF may encode for a polypeptide similar to rubredoxins

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The FeSII protein of Azotobacter vinelandii is not essential for aerobic nitrogen fixation, but confers significant protection to oxygen-mediated inactivation of nitrogenase in vitro and in vivo.

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Regulation of Nitrogen Fixation by Fe-S Protein II in Azotobacter vinelandii

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Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii

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Circular dichroism and magnetic circular dichroism of Azotobacter vinelandii ferredoxin I.

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Azotobacter vinelandii mutS: nucleotide sequence and mutant analysis

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The ORF encoding a putative ferredoxin-like protein downstream of the vnfH gene in Azotobacter vinelandii is involved in the vanadium-dependent alternative pathway of nitrogen fixation

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Characterization of the gene for the Fe-protein of the vanadium dependent alternative nitrogenase of Azotobacter vinelandii and construction of a Tn5 mutant

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Expression of the nifBfdxNnifOQ region of Azotobacter vinelandii and its role in nitrogenase activity.

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Nucleotide sequence and genetic analysis of the nifB-nifQ region from Azotobacter vinelandii

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Discovery of a novel ferredoxin from Azotobacter vinelandii containing two [4Fe-4S] clusters with widely differing and very negative reduction potentials

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Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement

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Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation

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Delta T 14/Delta D 15 Azotobacter vinelandii ferredoxin I: creation of a new CysXXCysXXCys motif that ligates a [4Fe-4S] cluster

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Overexpression of ferredoxin I in Azotobacter vinelandii

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A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes

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Large-scale purification of high activity Azotobacter vinelandii nitrogenase

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Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase

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Expression and spectroscopic characterization of the hydrogenosomal [2Fe-2S] ferredoxin from the protozoan Trichomonas vaginalis.

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Antagonistic involvement of FIS and H-NS proteins in the transcriptional control of hns expression.

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Molecular cloning and sequence analysis of human placental ferredoxin

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Extensive ligand rearrangements around the [2Fe-2S] cluster of Clostridium pasteurianum ferredoxin.

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Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli

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Design and functional expression in Escherichia coli of a synthetic gene encoding Clostridium pasteurianum 2[4Fe-4S] ferredoxin

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Observation of holoprotein molecular ions of several ferredoxins by electrospray-ionization-mass spectrometry

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Assembly of a [2Fe-2S]2+Cluster in a Molecular Variant ofClostridium pasteurianumRubredoxin†

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Identifiers

10.1074/JBC.274.45.32402

1 reference

Europe PubMed Central

7 October 2017

1 reference

Europe PubMed Central

7 October 2017

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