@article {2668,
	title = {Spectroscopic studies of the oxidation-reduction properties of three forms of ferredoxin from Desulphovibrio gigas},
	journal = {Biochim Biophys Acta},
	volume = {490},
	number = {2},
	year = {1977},
	note = {<p>0006-3002 (Print)0006-3002 (Linking)Journal Article</p>
},
	month = {Feb 22},
	pages = {311-21},
	abstract = {<p>Electron paramagnetic resonance spectra were recorded of three forms of Desulphovibrio gigas ferredoxin, FdI, FdI{\textquoteright} and FdII. The g = 1.94 signal seen in dithionite-reduced samples is strong in FdI, weaker in FdI{\textquoteright} and very small in FdII. The g = 2.02 signal in the oxidized proteins is weak in FdI and strongest in FdII. It is concluded that most of the 4Fe-4S centres in FdI change between states C- and C2-; FdI{\textquoteright} contain both types of centre. There is no evidence that any particular centre can change reversibly between all three oxidation states. Circular dichroism spectra show differences between FdI and FdII even in the diamagnetic C2- state. The redox potentials of the iron-sulphur centres of the three oligomers (forms) are different. After formation of the apo-protein of FdII and reconstitution with iron and sulphide, the protein behaves more like FdI, showing a strong g = 1.94 signal in the reduced states.</p>
},
	keywords = {*Ferredoxins/metabolism, Binding Sites, Circular Dichroism, Desulfovibrio/*metabolism, Dithionite, Electron Spin Resonance Spectroscopy, Oxidation-Reduction, Protein Binding, Protein Conformation},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=189829 },
	author = {Cammack, R. and Rao, K. K. and Hall, D. O. and Moura, J. J. and Xavier, A. V. and Bruschi, M. and Legall, J. and Deville, A. and Gayda, J. P.}
}
