Selenite Reduction by the Thioredoxin System: Kinetics and Identification of Protein-Bound Selenide | Zendy

Takashi Tamura | Zendy; Kumi Sato | Zendy; Kentaro KOMORI | Zendy; Takeshi Imai | Zendy; Mitsuhiko KUWAHARA | Zendy; Takahiro Okugochi | Zendy; Hisaaki Mihara | Zendy; Nobuyoshi Esaki | Zendy; Kenji Inagaki | Zendy

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Selenite Reduction by the Thioredoxin System: Kinetics and Identification of Protein-Bound Selenide

Author(s) -

Takashi Tamura,

Kumi Sato,

Kentaro KOMORI,

Takeshi Imai,

Mitsuhiko KUWAHARA,

Takahiro Okugochi,

Hisaaki Mihara,

Nobuyoshi Esaki,

Kenji Inagaki

Publication year - 2011

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.100847

Subject(s) - selenium , thioredoxin reductase , thioredoxin , chemistry , divalent , biochemistry , kinetics , substrate (aquarium) , reductase , enzyme , biology , organic chemistry , ecology , physics , quantum mechanics

Selenite (SeO(3)(2-)) assimilation into a bacterial selenoprotein depends on thioredoxin (trx) reductase in Esherichia coli, but the molecular mechanism has not been elucidated. The mineral-oil overlay method made it possible to carry out anaerobic enzyme assay, which demonstrated an initial lag-phase followed by time-dependent steady NADPH consumption with a positive cooperativity toward selenite and trx. SDS-PAGE/autoradiography using (75)Se-labeled selenite as substrate revealed the formation of trx-bound selenium in the reaction mixture. The protein-bound selenium has metabolic significance in being stabilized in the divalent state, and it also produced the selenopersulfide (-S-SeH) form by the catalysis of E. coli trx reductase (TrxB).

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