Characterization of recombinant Desulfovibrio gigas ferredoxin. | - CCMAR -

Journal Article

TitleCharacterization of recombinant Desulfovibrio gigas ferredoxin.
Publication TypeJournal Article
AuthorsRodrigues, P, Graça, F, Macedo, AL, Moura, I, Moura, JJ
Year of Publication2001
JournalBiochem Biophys Res Commun
Volume289
Issue2
Date Published2001 Nov 30
Pagination630-3
ISSN0006-291X
KeywordsCloning, Molecular, Desulfovibrio, Dimerization, Electron Spin Resonance Spectroscopy, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Ferredoxins, Iron, Magnetic Resonance Spectroscopy, Oxygen, Polymerase Chain Reaction, Recombinant Proteins, Spectrophotometry, Sulfur, Temperature, Ultraviolet Rays
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.
DOI10.1006/bbrc.2001.6016
Sapientia

http://www.ncbi.nlm.nih.gov/pubmed/11716522?dopt=Abstract
Alternate JournalBiochem. Biophys. Res. Commun.
PubMed ID11716522
CCMAR Authors
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