Adenylylsulfate reductases from archaea and bacteria are 1:1 αβ‐heterodimeric iron–sulfur flavoenzymes – high similarity of molecular properties emphasizes their central role in sulfur metabolism

FEBS Letters

Stetter, Karl O.¹  Büchert, Thomas²  Fritz, Günter²  Huber, Harald¹  Kroneck, Peter M.H.² 

[1] Lehrstuhl für Mikrobiologie, Universität Regensburg, D-93040 Regensburg, Germany;Fakultät für Biologie, Universität Konstanz, D-78457 Konstanz, Germany

关键词: Adenylylsulfate reductase;    Iron–sulfur flavoenzyme;    Sulfur metabolism;    APS reductase;    adenylylsulfate reductase;    APS;    adenosine-5′-phosphosulfate;   

DOI  :  10.1016/S0014-5793(00)01500-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Highly active adenylylsulfate (APS) reductase was isolated under N₂/H₂ from sulfate-reducing and sulfide-oxidizing bacteria and archaea. It was a 1:1 αβ-heterodimer of molecular mass ≈95 kDa, and two subunits (α≈75, β≈20 kDa). The specific activity was 11–14 μmol (min mg)⁻¹; cofactor analysis revealed 0.96±0.05 FAD, 7.5±0.1 Fe and 7.9±0.25 S²⁻. The photochemically reduced enzyme had a multiline EPR spectrum resulting from two interacting [4Fe–4S] centers. The properties of the different APS reductases were remarkably similar, although the enzyme is involved in different metabolic pathways and was isolated from phylogenetically far separated organisms. A structural model is proposed, with FAD bound to the α-subunit, and two [4Fe–4S] centers located in close proximity on the β-subunit.

【 授权许可】

Unknown