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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 several of its molecular variants have now been analyzed by electrospray-ionization mass spectrometry. In the negative-ion...

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Identifiers

PMID: 7763242
DOI: 10.1006/bbrc.1995.1714

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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