Characterization of Recombinant Desulfovibrio gigas Ferredoxin

descriptionPublicationkeyboard_double_arrow_right Article 01 Nov 2001 Portugal English Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 289, pages 630-633 (issn: 0006-291X,

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Authors: Rodrigues, Pedro; Graça, Fernando; Macedo, Anjos L.; Moura, Isabel; Moura, José J. G.;

doi: 10.1006/bbrc.2001.6016

pmid: 11716522

handle: 10400.1/4361

Characterization of Recombinant Desulfovibrio gigas Ferredoxin

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Abstract

Dg ferredoxin gene was cloned using the polymerase chain reaction (PCR), inserted into vector pT7-7, and overexpressed in Escherichia coli (E. coli) grown in aerobic media. The recombinant protein is a dimer and contains a [3Fe-4S] cluster per monomer. EPR and (1)H NMR data of recombinant and wild-type protein are compared.

Country

Portugal

Related Organizations

University of Algarve
Portugal
Centro de Biotecnologia e Química Fina
Portugal
Universidade Nova de Lisboa
Portugal
Universidade Nova de Lisboa
Portugal

Keywords

Magnetic Resonance Spectroscopy, Iron–sulfur cluster, Ultraviolet Rays, Iron, Electron Spin Resonance Spectroscopy, Temperature, Polymerase Chain Reaction, Recombinant Proteins, Oxygen, Paramagnetic protein, Spectrophotometry, Escherichia coli, Ferredoxins, Desulfovibrio, Electrophoresis, Polyacrylamide Gel, 3Fe–4S cluster, Cloning, Molecular, Dimerization, Ferredoxin, Ferredoxin gene, Sulfur

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