DOE/SC0007014-Final

Miller, Susan M.¹ 

[1] Univ. of California, San Francisco, CA (United States)

关键词: Hg toxicity;    Hg-protein adducts;    mass spectrometry;    Hg isotopes;   

DOI  :  10.2172/1192070
RP-ID  :  DOE/SC0007014--Final
PID  :  OSTI ID: 1192070
Others  :  Other: ER65195,

学科分类：生物科学（综合）

美国|英语

来源: SciTech Connect

【 摘 要 】

Hg is a wide-spread contaminant in the environment and is toxic in all of its various forms. Organomercurials (RHg+) and mercuric ion (Hg2+) directly inactivate proteins by binding to their cysteine or selenocysteine residues. In our previous collaborative project involving the Summers, Miller and Lipton laboratories, we developed a high-throughput, mass spectrometry-based global proteomics approach using the 7 stable isotopes of Hg to identify proteins from phenylmercury-exposed E. coli cells that form stable PhHg-adducts. The two overall objectives of this subsequent collaborative project were (1) to expand our novel organomercury-proteomics capability for use with inorganic ionic (HgX2) exposure and (2) to use this new capability to identify Hg-protein adducts in methylating and non-methylating Desulfovibrio exposed to inorganic ionic HgX2 and test whether those identified uniquely in methylating bacteria are involved in the methylation pathway. The specific objectives and accomplishments of the Miller lab in this project included: Development of algorithms for analysis of the Hg-proteomic mass spectrometry data to identify and quantify Hg-adducted peptides and other trends in the data.