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Titolo:
Theoretical study of the role of low-barrier hydrogen bonds in enzyme catalysis: a model of proton transfer in serine protease
Autore:
Kim, Y; Ahn, KH;
Indirizzi:
Kyung Hee Univ, Dept Chem, Yongin City 449701, Kyunggi Do, South Korea Kyung Hee Univ Yongin City Kyunggi Do South Korea 449701 Do, South Korea
Titolo Testata:
THEORETICAL CHEMISTRY ACCOUNTS
fascicolo: 3, volume: 106, anno: 2001,
pagine: 171 - 177
SICI:
1432-881X(200107)106:3<171:TSOTRO>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR MAGNETIC-RESONANCE; GAS-PHASE; CHYMOTRYPSIN; STATE; COMPLEXES; TRIAD; HISTIDINE; ALPHA; ACTIVATION; MECHANISM;
Keywords:
low-barrier hydrogen bond; enzyme catalysis; serine protease; catalytic dyad; environmental effect;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Kim, Y Kyung Hee Univ, Dept Chem, Yongin City 449701, Kyunggi Do, South Korea Kyung Hee Univ Yongin City Kyunggi Do South Korea 449701 uth Korea
Citazione:
Y. Kim e K.H. Ahn, "Theoretical study of the role of low-barrier hydrogen bonds in enzyme catalysis: a model of proton transfer in serine protease", THEOR CH AC, 106(3), 2001, pp. 171-177

Abstract

A model of low-barrier hydrogen bonds (LBHBs) in enzymes has been studied by ab initio quantum mechanical calculations including the self-consistent reaction field solvent model. The hydrogen-bond strengths and the deprotonation energies for the hydrogen-bonded and non-hydrogen-bonded cis-urocanic acid were calculated at the HF/6-31 + G(d,p) level at various dielectric constants. The same calculations were performed for the alpha,beta -dihydrourocanic acid to model the catalytic dyad of serine protease. The deprotonation energy of N-epsilon2 in alpha,beta -dihydrourocanic acid is increased byformation of LBHBs and depends very much on the dielectric constant. This study suggests that the formation of LBHBs;increases the basicity of the dyad, and the polarity change near the reaction center in the active site could help the proton abstraction from Ser 195 and the donation to the leavinggroup. Both the LBHBs and the environment can play crucial roles in the enzyme catalysis.

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Documento generato il 29/03/20 alle ore 12:17:28