title: Observation of holoprotein molecular ions of several ferredoxins by electrospray-ionization-mass spectrometry.
abstract: Several ferredoxins containing [4Fe-4S] or [2Fe-2S] active sites have been analyzed by electrospray-ionization-mass spectrometry. For these acidic proteins, low pH conditions must be implemented in order to ensure strong signals in positive-ionization mode. Under such conditions the iron-sulfur active sites were lost in most cases. In contrast, the holoproteins were preserved under negative-ionization mode conditions: they were weakly but sufficiently ionized and information about their cofactor content could be obtained. The experimental conditions set up here should provide a useful basis for the detailed characterization of more complex iron-sulfur proteins.
authors.affiliation: Laboratoire de Spectrométrie de Masse des Protéines, Institute de Biologie Structurale (CEA-CNRS), Grenoble, France.
authors.forename: Y
authors.initials: Y
authors.lastname: Pétillot
authors.forename: E
authors.initials: E
authors.lastname: Forest
authors.forename: J
authors.initials: J
authors.lastname: Meyer
authors.forename: J M
authors.initials: JM
authors.lastname: Moulis
mesh_terms: D005288:Ferredoxins / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods*
chemical_list: D005288:Ferredoxins