Details in the catalytic mechanism of mammalian thioredoxin reductase 1 revealed using point mutations and juglone-coupled enzyme activities
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- 作者：Jianqiang Xua ; b ; Qing Chengb ; Elias S.J. Arné ; rb ; Elias.Arner@ki.se" class="auth_mail" title="E-mail the corresponding author
- 关键词：Trx ; thioredoxin ; TrxR ; thioredoxin reductase ; TrxR1 ; thioredoxin reductase 1 ; Sec or U ; selenocysteine ; Cys or C ; cysteine ; Trp or W ; tryptophan ; Ser or S ; serine ; Asn or N ; asparagine ; Ala or A ; alanine ; Gly or G ; glycine ; juglone ; 5-hydroxy-1 ; 4-naphthoquinone ; DNCB ; 1-chloro-2 ; 4-dinitrobenzene ; DTNB ; 5 ; 5&prime ; -dithiobis (2-nitrobenzoic acid) ; DTT ; dithiothreitol ; FAD ; flavin adenine dinucleotide ; NADPH ; nicotinamide adenine dinucleotide phosphate ; reduced form ; SecTRAPs ; selenium-compromis
- 刊名：Free Radical Biology and Medicine
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：94
- 期：Complete
- 页码：110-120
- 全文大小：1523 K
文摘
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Sec-deficient forms of TrxR1 reduce juglone but not typical TrxR1 substrates.
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The Cys497 residue of TrxR1 is required for efficient redox cycling activity with juglone.
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Juglone arylates Cys497 and additional residues of TrxR1.
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The previously proposed guiding bar of the enzyme supports activity of juglone-arylated TrxR1.