Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt, Germany.
Metallomics. 2013 Apr;5(4):302-17. doi: 10.1039/c2mt20225e.
Sulfate-reducing bacteria and archaea are important players in the biogeochemical sulfur cycle. ATP sulfurylase, adenosine 5'-phosphosulfate reductase and dissimilatory sulfite reductase are the key enzymes in the energy conserving process of SO4(2-) → H2S reduction. This review summarizes recent advances in our understanding of the activation of sulfate to adenosine 5'-phosphosulfate, the following reductive cleavage to SO3(2-) and AMP, and the final six-electron reduction of SO3(2-) to H2S in the hyperthermophilic archaeon Archaeoglobus fulgidus. Structure based mechanisms will be discussed for these three enzymes which host unique metal centers at their catalytic sites.
硫酸盐还原菌和古菌是生物地球化学硫循环中的重要参与者。三磷酸腺苷硫酸化酶、腺苷 5′-磷酸硫酸还原酶和异化亚硫酸盐还原酶是 SO4(2-)→H2S 还原过程中能量守恒的关键酶。本文综述了我们对硫酸盐激活为腺苷 5′-磷酸硫酸盐、随后还原裂解为 SO3(2-)和 AMP 以及超嗜热古菌嗜热菌最终六电子还原 SO3(2-)为 H2S 过程的最新理解。将讨论这些三种酶的基于结构的机制，这些酶在其催化位点上具有独特的金属中心。
