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Adenylylsulphate reductase from the sulphate-reducing archaeon Archaeoglobus fulgidus: cloning and characterization of the genes and comparison of the enzyme with other iron–sulphur flavoproteins

Norbert Speich^1,

Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Meckenheimer Allee 168, 53115 Bonn, Germany
Institut für Molekulargenetik, FB Biologie, Philipps-Universität Marburg, 35037 Marburg, Germany
Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82143 Martinsried, Germany
Institut für Mikrobiologie, Universität Regensburg, Universitätsstr. 31, 93053 Regensburg, Germany

^*Author for correspondence: H. G. Trüper. Tel: +49 228 732320. Fax: +49 228 737576.

ABSTRACT

Adenylylsulphate (adenosine-5'-phosphosulphate, APS) reductase from the extremely thermophilic sulphate-reducing archaeon Archaeoglobus fulgidus is an iron-sulphur flavoprotein containing one non-covalently bound flavin group, eight non-haem iron and six labile sulphide atoms per molecule. Re-evaluation of the enzyme structure revealed the presence of two different subunits with molecular masses of 80 and 18.5 kDa. The subunits are arranged in an ₂β subunit structure. We have cloned and sequenced a 2.7 kb segment of DNA containing the genes for the and β subunits, which we designate aprA and aprB, respectively. The two genes are separated by 17 bp and localized in the order aprBA. While a putative promoter could not be identified in the vicinity of aprBA a probable termination signal was found just downstream of the translation stop codon of aprA. The codon usage for aprBA shows strong preferences for G and C in the third codon position. aprA encodes a 73.3 kDa polypeptide, which shows significant overall similarities with the flavoprotein subunits of the succinate dehydrogenases from Escherichia coli and Bacillus subtilis and the corresponding flavoprotein of E. coli fumarate reductase. Part of the homologous peptide stretches could be assigned to domains that are involved in the binding of the substrate or of the FAD prosthetic group. aprB encodes a 17.1 kDa polypeptide representing an iron-sulphur protein, seven cysteine residues of which are arranged in two clusters typical of ligands of the iron-sulphur centres in {[Fe₃S₄][Fe₄S₄]} 7-Fe ferredoxins.

Present address: Institut für Humangenetik, Philipps-Universität Marburg, Germany.

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