Arsenic methylation by an arsenite S-adenosylmethionine methyltransferase from Spirulina platensis

被引:28
作者
Guo, Yuqing [1 ,2 ]
Xue, Ximei [2 ]
Yan, Yu [2 ]
Zhu, Yongguan [2 ,3 ]
Yang, Guidi [1 ]
Ye, Jun [2 ]
机构
[1] Fujian Agr & Forestry Univ, Fujian Prov Key Lab Agroecol Proc & Safety Monito, Coll Life Sci, Fuzhou 350002, Peoples R China
[2] Chinese Acad Sci, Inst Urban Environm, Key Lab Urban Environm & Hlth, Xiamen 361021, Peoples R China
[3] Chinese Acad Sci, Res Ctr Ecoenvironm Sci, State Key Lab Urban & Reg Ecol, Beijing 100085, Peoples R China
来源
JOURNAL OF ENVIRONMENTAL SCIENCES | 2016年 / 49卷
基金
中国国家自然科学基金;
关键词
Spirulina platensis; Arsenic; Methylation; Methyltransferase; VOLATILIZATION; IDENTIFICATION; BIOTRANSFORMATION; BIOMETHYLATION; SPECIATION; ENVIRONMENT; MECHANISM; TOXICITY; RESIDUES; REMOVAL;
D O I
10.1016/j.jes.2016.06.013
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
Arsenic-contaminated water is a serious hazard for human health. Plankton plays a critical role in the fate and toxicity of arsenic in water by accumulation and biotransformation. Spirulina platensis (S. platensis), a typical plankton, is often used as a supplement or feed for pharmacy and aquiculture, and may introduce arsenic into the food chain, resulting in a risk to human health. However, there are few studies about how S. platensis biotransforms arsenic. In this study, we investigated arsenic biotransformation by S. platensis. When exposed to arsenite (As(III)), S. platensis accumulated arsenic up to 4.1 mg/kg dry weight. After exposure to As(III), arsenate (As(V)) was the predominant species making up 64% to 86% of the total arsenic. Monomethylarsenate (MMA(V)) and dimethylarsenate (DMA(V)) were also detected. An arsenite S-adenosylmethionine methyltransferase from S. platensis (SpArsM) was identified and characterized. SpArsM showed low identity with other reported ArsM enzymes. The Escherichia coli AW3110 bearing SparsM gene resulted in As(III) methylation and conferring resistance to As(III). The in vitro assay showed that SpArsM exhibited As(III) methylation activity. DMA(V) and a small amount of MMA(V) were detected in the reaction system within 0.5 hr. A truncated SpArsM derivative lacking the last 34 residues still had the ability to methylate As(III). The three single mutants of SpArsM (C59S, C186S, and C238S) abolished the capability of As(III) methylation, suggesting the three cysteine residues are involved in catalysis. We propose that SpArsM is responsible for As methylation and detoxification of As(III) and may contribute to As biogeochemistry. (C) 2016 The Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences. Published by Elsevier B.V.
引用
收藏
页码:162 / 168
页数:7
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