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J. Biol. Chem., Vol. 277, Issue 24, 21786-21791, June 14, 2002

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The Presence of an Iron-Sulfur Cluster in Adenosine 5'-Phosphosulfate Reductase Separates Organisms Utilizing Adenosine 5'-Phosphosulfate and Phosphoadenosine 5'-Phosphosulfate for Sulfate Assimilation^*

Stanislav Kopriva^§, Thomas Büchert^¶, Günter Fritz, Marianne Suter^**, Rüdiger Benda, Volker Schünemann, Anna Koprivova^§§, Peter Schürmann^¶¶, Alfred X. Trautwein, Peter M. H. Kroneck^¶, and Christian Brunold^**

From the  Institute of Forest Botany and Tree Physiology, Albert-Ludwigs-University, D-79085 Freiburg, Germany, ^¶ Fachbereich Biologie, Universität Konstanz, D-78457 Konstanz, Germany,  Biochemisches Institut, Universität Zürich, CH-8057 Zürich, Switzerland, ^** Institute of Plant Sciences, University of Berne, CH-3013 Bern, Switzerland,  Institut für Physik, Medizinische Universität zu Lübeck, D-23538 Lübeck, Germany, ^§§ Plant Biotechnology, Albert-Ludwigs-University, D-79104 Freiburg, Germany, and ^¶¶ Laboratoire de Biochimie, University of Neuchâtel, CH-2000 Neuchâtel, Switzerland

It was generally accepted that plants, algae, and phototrophic bacteria use adenosine 5'-phosphosulfate (APS) for assimilatory sulfate reduction, whereas bacteria and fungi use phosphoadenosine 5'-phosphosulfate (PAPS). The corresponding enzymes, APS and PAPS reductase, share 25-30% identical amino acids. Phylogenetic analysis of APS and PAPS reductase amino acid sequences from different organisms, which were retrieved from the GenBank^TM, revealed two clusters. The first cluster comprised known PAPS reductases from enteric bacteria, cyanobacteria, and yeast. On the other hand, plant APS reductase sequences were clustered together with many bacterial ones, including those from Pseudomonas and Rhizobium. The gene for APS reductase cloned from the APS-reducing cyanobacterium Plectonema also clustered together with the plant sequences, confirming that the two classes of sequences represent PAPS and APS reductases, respectively. Compared with the PAPS reductase, all sequences of the APS reductase cluster contained two additional cysteine pairs homologous to the cysteine residues involved in binding an iron-sulfur cluster in plants. Mössbauer analysis revealed that the recombinant APS reductase from Pseudomonas aeruginosa contains a [4Fe-4S] cluster with the same characteristics as the plant enzyme. We conclude, therefore, that the presence of an iron-sulfur cluster determines the APS specificity of the sulfate-reducing enzymes and thus separates the APS- and PAPS-dependent assimilatory sulfate reduction pathways.

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