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Titolo:
What evidences were elucidated about photoreactive nitrile hydratase?
Autore:
Endo, I; Odaka, M;
Indirizzi:
RIKEN, Inst Phys & Chem Res, Biochem Syst Lab, Wako, Saitama 3510198, Japan RIKEN Wako Saitama Japan 3510198 m Syst Lab, Wako, Saitama 3510198, Japan
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 1-3, volume: 10, anno: 2000,
pagine: 81 - 86
SICI:
1381-1177(20000904)10:1-3<81:WEWEAP>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHODOCOCCUS SP N-771; NONHEME IRON CENTER; ESCHERICHIA-COLI; POSTTRANSLATIONAL MODIFICATION; NUCLEOTIDE-SEQUENCE; RHODOCHROUS J1; OXIDE; CLONING; ENZYME; EXPRESSION;
Keywords:
nitrile hydratase; non-heme iron; post-translational modification; claw setting; hydration water molecule;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Endo, I RIKEN, Inst Phys & Chem Res, Biochem Syst Lab, Wako, Saitama 3510198, Japan RIKEN Wako Saitama Japan 3510198 ab, Wako, Saitama 3510198, Japan
Citazione:
I. Endo e M. Odaka, "What evidences were elucidated about photoreactive nitrile hydratase?", J MOL CAT B, 10(1-3), 2000, pp. 81-86

Abstract

Characteristic features of a photoreactive nitrile hydratase (NHase) from Rhodococcus sp. N-771 were introduced. We have found a new biological function of nitric oxide (NO) that controls the photoreactivity of NHase by association with thr: non-heme iron active center and photoinduced dissociationfrom it. We have elucidated the crystal structure of NHase in the nitrosylated state at 1.7 Angstrom resolution. A unique structure of the photoreactive catalytic center of the enzyme was revealed; the center consists of thenon-heme iron atom coordinated with the sulfur atoms from three cysteine residues (alpha Cys109, alpha Cys112 and alpha Cys114) and two amide nitrogen atoms in the main chain of alpha Ser113 and alpha Cys114. Two out of the three cysteine residues are post-translationally modified into cysteine sulfinic (alpha Cys112-SO2H) and -sulfenic (alpha Cys114-SOH) acids. The two oxygen atoms of alpha Cys112-SO2H and alpha Cys114-SOH form a unique structure, Claw setting, together with the oxygen atom, form alpha Ser113. We havealso studied the roles of the hydration water molecules in the enzyme. Thehydration water molecules stabilize the catalytic center and the tertiary and quaternary structures of the enzyme. The detailed hydration structure around the active center is also discussed. (C) 2000 Elsevier Science B.V. All rights reserved. (C) 2000 Elsevier Science B.V. All rights reserved.

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Documento generato il 29/11/20 alle ore 16:17:21