Zumft Walter G
Institute of Applied Biosciences, Division of Molecular Microbiology, University of Karlsruhe, Karlsruhe, Germany.
J Mol Microbiol Biotechnol. 2005;10(2-4):154-66. doi: 10.1159/000091562.
Nitrous oxide reductase (NosZ, EC 1.7.99.6) is the terminal oxidoreductase of a respiratory electron transfer chain that transforms nitrous oxide to dinitrogen. The enzyme carries six Cu atoms. Two are arranged in the mixed-valent binuclear CuA site, and four make up the mu4-sulfide-bridged Cu cluster, CuZ. The biogenesis of a catalytically active NosZ requires auxiliary functions for metal center assembly in the periplasm. Both Tat and Sec pathways share the task to transport the various Nos proteins to their functional sites. Biogenesis of NosZ requires an ABC transporter complex and the periplasmic Cu chaperone NosL. Sustaining whole-cell NosZ function depends on the periplasmic, FAD-containing protein NosX, and the membrane-bound iron-sulfur flavoprotein NosR. Most components with a biogenetic function are now amenable to structural studies.
一氧化二氮还原酶（NosZ，EC 1.7.99.6）是呼吸电子传递链的末端氧化还原酶，可将一氧化二氮转化为氮气。该酶含有六个铜原子。两个铜原子排列在混合价双核CuA位点，另外四个构成μ4-硫化物桥联的铜簇CuZ。具有催化活性的NosZ的生物合成需要周质中金属中心组装的辅助功能。Tat和Sec途径共同承担将各种Nos蛋白转运到其功能位点的任务。NosZ的生物合成需要ABC转运蛋白复合物和周质铜伴侣NosL。维持全细胞NosZ功能依赖于周质中含FAD的蛋白NosX和膜结合的铁硫黄素蛋白NosR。现在，大多数具有生物发生功能的成分都适合进行结构研究。
