Spectroscopic studies on APS reductase isolated from the hyperthermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus

Jorge Lampreia, Guy Fauque, Norbert Speich, Christiane Dah1, Isabel Moura, Hans G. Truper, José J. G. Moura

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)342-347
Number of pages6
JournalBiochemical And Biophysical Research Communications
Volume181
Issue number1
DOIs
Publication statusPublished - 27 Nov 1991

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