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. 2008 Aug 22;283(34):22890–22894. doi: 10.1074/jbc.C800124200

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Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 4. — Structural and kinetic intermediates along the human Srx reaction coordinate. A, the moiety (purple), Cys sulfinic acid 52 (Csd52), poised for an inline attack of the γ-phosphate of ATP, based on the ATP·Mg²⁺·Srx (blue) and Srx-S–S_P-PrxI crystal structures (Protein Data Bank numbers 3CYI and 2RII) (11, 22). The resulting phosphorylated intermediate (not shown) can be readily hydrolyzed. B, model of the thiosulfinate intermediate between Srx and Prx. C, the crystallographically determined Prx-S_P–S-Srx disulfide-bonded complex (Protein Data Bank number 2RII). This complex could form through several steps involving reactions between the sulfenic acid form of Prx and Srx.

Inline graphic — Structural and kinetic intermediates along the human Srx reaction coordinate. A, the moiety (purple), Cys sulfinic acid 52 (Csd52), poised for an inline attack of the γ-phosphate of ATP, based on the ATP·Mg²⁺·Srx (blue) and Srx-S–S_P-PrxI crystal structures (Protein Data Bank numbers 3CYI and 2RII) (11, 22). The resulting phosphorylated intermediate (not shown) can be readily hydrolyzed. B, model of the thiosulfinate intermediate between Srx and Prx. C, the crystallographically determined Prx-S_P–S-Srx disulfide-bonded complex (Protein Data Bank number 2RII). This complex could form through several steps involving reactions between the sulfenic acid form of Prx and Srx.