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Titolo:
An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase
Autore:
Endo, I; Odaka, M; Yohda, M;
Indirizzi:
Inst Phys & Chem Res, Biochem Syst Lab, Wako, Saitama 3510198, Japan Inst Phys & Chem Res Wako Saitama Japan 3510198 o, Saitama 3510198, Japan
Titolo Testata:
TRENDS IN BIOTECHNOLOGY
fascicolo: 6, volume: 17, anno: 1999,
pagine: 244 - 249
SICI:
0167-7799(199906)17:6<244:AECBLT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHODOCOCCUS SP N-771; NONHEME IRON CENTER; BINDING ACTIVITY INVITRO; SULFENIC ACID; TRANSCRIPTIONAL REGULATOR; NUCLEOTIDE-SEQUENCE; BREVIBACTERIUM SP; CYSTEINE RESIDUE; REDOX REGULATION; ALPHA-SUBUNIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Endo, I Inst Phys & Chem Res, Biochem Syst Lab, Wako, Saitama 3510198, Japan Inst Phys & Chem Res Wako Saitama Japan 3510198 ma 3510198, Japan
Citazione:
I. Endo et al., "An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase", TRENDS BIOT, 17(6), 1999, pp. 244-249

Abstract

Extensive studies have revealed the molecular mechanism of the photoreactivity of nitrile hydratase from Rhodococcus sp, N-771. In the inactive enzyme, nitric oxide is bound to the non-heme ferric iron at the catalytic center, stabilized by a claw like structure formed by two post-translationally modified cysteines and a serine. The inactive nitrile hydratase is activatedby the photoinduced release of the nitric oxide. This result might providea means of designing novel photoreactive chemical compounds or proteins that would be applicable to biochips and light-controlled metabolic systems.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 10:44:30