Structural mechanism for bacterial oxidation of oceanic trimethylamine into trimethylamine N-oxide
Chun-Yang Li, Xiu-Lan Chen, Dian Zhang, Peng Wang, Qi Sheng, Ming Peng, Bin-Bin Xie, Qi-Long Qin, Ping-Yi Li, Xi-Ying Zhang, Hai-Nan Su, Xiao-Yan Song, Mei Shi, Bai-Cheng Zhou, Lu-Ying Xun, Yin Chen and Yu-Zhong Zhang
Version of Record online: 10 JAN 2017 | DOI: 10.1111/mmi.13605
Trimethylamine (TMA) and trimethylamine N-oxide (TMAO) are widespread in the ocean. TMA monooxygenase (Tmm), a bacterial flavin-containing monooxygenase (FMO), is responsible for converting marine TMA to TMAO. In this study, we elucidated the catalytic mechanism of TMA oxidation by a marine bacterial Tmm. The catalytic process of Tmm consists of a reductive half-reaction and an oxidative half-reaction. Our findings first demonstrate that NADP+ undergoes a conformational change in the oxidative half-reaction of FMOs.