@article {2666,
	title = {NMR characterization of three forms of ferredoxin from Desulphovibrio gigas, a sulphate reducer},
	journal = {Biochim Biophys Acta},
	volume = {459},
	number = {2},
	year = {1977},
	note = {<p>0006-3002 (Print)0006-3002 (Linking)Journal Article</p>
},
	month = {Feb 7},
	pages = {278-89},
	abstract = {<p>A NMR and magnetic susceptibility study of the oxidized and reduced states of three different oligomers (forms) of a [4Fe-4S] ferrodoxin protein from Desulphovibrio gigas, FdI, FdI{\textquoteright}, and FdII was carried out. FdI and FdI{\textquoteright} are different trimers and FdII a tetramer of the same basic subunit. A probable assignment of the contact shifted resonances is indicated. Since the temperature dependences of the contact shifted responances associated with each [4Fe-4S] are not all similar a delocalized model for the spin densities on the 4Fe does not apply. The exchange rate between oxidized and reduced states is slow on the NMR time scale. The three oligomers are not magnetically equivalent. Using the "three state hypothesis" terminology it is shown that FdIox is predominantly in the C2- state and changes upon reduction into the C3- state, while FdIIox is in the C- state and changes into the C2- state. FdI{\textquoteright} does not easily fit into this classification. This study shows a similarity of magnetic behaviour between FdI and bacterial ferredoxins (e.g. Bacillus polymyxa) and between FdII and HiPIP from Chromatium sp. The influence of the quaternary structure on the stabilization of the different oxidation states of ferredoxins as well as on their redox potentials is discussed.</p>
},
	keywords = {*Ferredoxins/isolation \& purification, Desulfovibrio/*metabolism, Kinetics, Magnetic Resonance Spectroscopy, Mathematics, Oxidation-Reduction, Protein Conformation, Temperature},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=836818 },
	author = {Moura, J. J. and Xavier, A. V. and Bruschi, M. and Gall, J. L.}
}
