@article {2562,
	title = {Spectroscopic studies on APS reductase isolated from the hyperthermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus},
	journal = {Biochem Biophys Res Commun},
	volume = {181},
	number = {1},
	year = {1991},
	note = {<p>0006-291X (Print)0006-291X (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Nov 27},
	pages = {342-7},
	abstract = {<p>Adenylyl sulfate (APS) reductase, the key enzyme of the dissimilatory sulfate respiration, catalyzes the reduction of APS (the activated form of sulfate) to sulfite with release of AMP. A spectroscopic study was carried out with the APS reductase purified from the extremely thermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus DSM 4304. Combined ultraviolet/visible spectroscopy and low temperature electron paramagnetic resonance (EPR) studies were used in order to characterize the active centers and the reactivity towards AMP and sulfite of this enzyme. The A. fulgidus APS reductase is an iron-sulfur flavoprotein containing two distinct [4Fe-4S] clusters (Centers I and II) very similar to the homologous enzyme from Desulfovibrio gigas. Center I, which has a high redox potential, is reduced by AMP and sulfite, and Center II has a very negative redox potential.</p>
},
	keywords = {*Oxidoreductases Acting on Sulfur Group Donors, Archaea/*enzymology, Binding Sites, Electron Spin Resonance Spectroscopy, Hot Temperature, Oxidation-Reduction, Oxidoreductases/chemistry/isolation \& purification/*metabolism, Spectrophotometry, Sulfates/metabolism},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=1659811 },
	author = {Lampreia, J. and Fauque, G. and Speich, N. and Dahl, C. and Moura, I. and Truper, H. G. and Moura, J. J.}
}
