Biogenesis of the Bacterial Respiratory CuA, Cu-S Enzyme Nitrous Oxide Reductase

作者：Walter G. Zumft · 发表于：Microbial Physiology · 年份：2005 · DOI：10.1159/000091562 · 被引用次数：53 · 研究领域：Metalloenzymes and iron-sulfur proteins、Trace Elements in Health、Metal-Catalyzed Oxygenation Mechanisms

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.