Electrospray-ionization mass spectrometry of molecular variants of a [2Fe-2S] ferredoxin.

doi:10.1006/bbrc.1995.1714

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Article

Electrospray-ionization mass spectrometry of molecular variants of a [2Fe-2S] ferredoxin.

Biochemical and biophysical research communications - 25 May 1995

Petillot Y, Golinelli M P, Forest E, Meyer J

Abstract excerpt

The [2Fe-2S] ferredoxin from Clostridium pasteurianum is a homodimeric protein of which each subunit contains one [2Fe-2S] cluster. In previous investigations, the five cysteine residues in positions 11, 14, 24, 56 and 60 had been mutated into serine or alanine. The wild type ferredoxin and sever...

Topics

Alanine
Apoproteins
Clostridium
Cysteine
Ferredoxins
Genetic Variation
Iron
Macromolecular Substances
Mass Spectrometry
Mutagenesis, Site-Directed
Protein Conformation
Recombinant Proteins
Serine
Sulfur

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