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Titolo:
Proton transfer at carbon
Autore:
Richard, JP; Amyes, TL;
Indirizzi:
SUNY Buffalo, Dept Chem, Buffalo, NY 14260 USA SUNY Buffalo Buffalo NY USA 14260 ffalo, Dept Chem, Buffalo, NY 14260 USA
Titolo Testata:
CURRENT OPINION IN CHEMICAL BIOLOGY
fascicolo: 6, volume: 5, anno: 2001,
pagine: 626 - 633
SICI:
1367-5931(200112)5:6<626:PTAC>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID-BASE CATALYSIS; AQUEOUS-SOLUTION; MANDELATE RACEMASE; ACTIVE-SITE; GLUTAMATE RACEMASE; PSEUDOMONAS-PUTIDA; TRANSITION-STATE; ENZYME; ENOLASE; MECHANISM;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Richard, JP SUNY Buffalo, Dept Chem, Buffalo, NY 14260 USA SUNY Buffalo Buffalo NY USA 14260 Chem, Buffalo, NY 14260 USA
Citazione:
J.P. Richard e T.L. Amyes, "Proton transfer at carbon", CURR OP C B, 5(6), 2001, pp. 626-633

Abstract

The viability of living systems requires that C-H bonds of biological molecules be stable in water, but that there also be a mechanism for shorteningthe timescale for their heterolytic cleavage through enzymatic catalysis of a variety of catabolic and metabolic reactions. An understanding of the mechanism of enzymatic catalysis of proton transfer at carbon requires the integration of results of studies to determine the structure of the enzyme-substrate complex with model studies on the mechanism for the non-enzymatic reaction in water, and the effect of the local protein environment on the stability of the transition state for this reaction. A common theme is the importance of electrostatic interactions in providing stabilization of boundcarbanion intermediates of enzyme-catalyzed proton-transfer reactions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/04/20 alle ore 23:19:44