The flavinyl transferase ApbE of Pseudomonas stutzeri matures the NosR protein required for nitrous oxide reduction

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• 作者：Lin Zhang^a ; Christian Trncik^a ; Susana L.A. Andrade^a ; ^b ; Oliver Einsle^a ; ^b ; ^{einsle@biochemie.uni-freiburg.de}
• 关键词：Bacterial denitrification ; Nitrous oxide reductase ; Flavin binding protein ; ApbE/NosX family protein ; X-ray crystallography
• 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1858
• 期：2
• 页码：95-102
• 全文大小：2075 K
• 卷排序：1858

文摘

The membrane protein NosR, required for assembly and function of nitrous oxide reductase, is covalently flavinylated. Pseudomonas stutzeri lacks a flavinyl transferase (NosX) gene in the nos operon. NosR can be functionally flavinylated by the single flavinyl transferase present in the genome, the AbpE protein. A three-dimensional structure of apo-ApbE is presented.