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We describe the one\u2010pot total synthesis of human thiosulfate:glutathione sulfurtransferase (TSTD1). WT\u2010TSTD1 was synthesized in a C\u2010to\u2010N synthetic approach involving multiple NCL reactions, Cu\n                    <jats:sup>II<\/jats:sup>\n                    \u2010mediated deprotection of selenazolidine (Sez), and chemoselective deselenization. The seleno\u2010analog Se\u2010TSTD1, in which the active site Cys is replaced with selenocysteine, was also synthesized with a kinetically controlled ligation with an N\u2010to\u2010C synthetic approach. The catalytic activity of the two proteins indicated that Se\u2010TSTD1 possessed only four\u2010fold lower activity than WT\u2010TSTD1, thus suggesting that selenoproteins can have physiologically comparable sulfutransferase activity to their cysteine counterparts.\n                  <\/jats:p>","DOI":"10.1002\/anie.201909484","type":"journal-article","created":{"date-parts":[[2019,8,13]],"date-time":"2019-08-13T11:33:15Z","timestamp":1565695995000},"page":"14610-14614","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Copper\u2010Mediated Selenazolidine Deprotection Enables One\u2010Pot Chemical Synthesis of Challenging Proteins"],"prefix":"10.1002","volume":"58","author":[{"given":"Zhenguang","family":"Zhao","sequence":"first","affiliation":[{"name":"Institute of Chemistry The Hebrew University of Jerusalem  Edmond J. 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