Microbial reduction of selenate and nitrate: common themes and variations.
Microbial reduction of selenate and nitrate: common themes and variations.
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微生物还原硒酸盐和硝酸盐：常见主题和变化。
DOI：
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发表时间：
2005
影响因子：
3.9
通讯作者：
C. Butler
中科院分区：
文献类型：
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作者：
Carys A. Watts;Helen Ridley;E. J. Dridge;James T. Leaver;A. Reilly;David J. Richardson;C. Butler
许多生物化学上不同的系统已被表征为含氧阴离子、硒酸盐（SeO（4）（2-））和硝酸盐（NO（3）（-））的微生物还原。两类依赖氘的硝酸还原酶催化硝酸盐（NO（3）（-））还原为亚硝酸盐（NO（2）（-））的还原反应。主要的呼吸硝酸还原酶（NAR）是膜锚定的，其活性位点面向细胞质区室。另一种酶（NAP）是水溶性的，位于周质中。近年来，我们对这些酶系统的理解显著增加。NAR和NAP的晶体结构现已得到解决，它们为这些呼吸复合物的结构，功能和进化提供了新的见解。相比之下，我们对微生物硒酸盐（SeO（4）（2-））还原和呼吸作用的理解处于早期阶段;然而，与硝酸还原酶系统的相似性正在出现。本文将考虑不同类型的硝酸盐和硒酸盐还原酶之间的一些共同主题和变化。
A number of biochemically distinct systems have been characterized for the microbial reduction of the oxyanions, selenate (SeO(4)(2-)) and nitrate (NO(3)(-)). Two classes of molybdenum-dependent nitrate reductase catalyse the respiratory-linked reduction of nitrate (NO(3)(-)) to nitrite (NO(2)(-)). The main respiratory nitrate reductase (NAR) is membrane-anchored, with its active site facing the cytoplasmic compartment. The other enzyme (NAP) is water-soluble and located in the periplasm. In recent years, our understanding of each of these enzyme systems has increased significantly. The crystal structures of both NAR and NAP have now been solved and they provide new insight into the structure, function and evolution of these respiratory complexes. In contrast, our understanding of microbial selenate (SeO(4)(2-)) reduction and respiration is at an early stage; however, similarities to the nitrate reductase systems are emerging. This review will consider some of the common themes and variations between the different classes of nitrate and selenate reductases.