Protein's electronic polarization contributes significantly to its catalytic function

Yun Xiang, Lili Duan, John Zhang

Research output: Contribution to journalArticle

Abstract

Ab initio quantum mechanicalmolecular mechanical method is combined with the polarized protein-specific charge to study the chemical reactions catalyzed by protein enzymes. Significant improvement in the accuracy and efficiency of free-energy simulation is demonstrated by calculating the free-energy profile of the primary proton transfer reaction in triosephosphate isomerase. Quantitative agreement with experimental results is achieved. Our simulation results indicate that electronic polarization makes important contribution to enzyme catalysis by lowering the energy barrier by as much as 3 kcalmol.

Original languageEnglish (US)
Article number205101
JournalJournal of Chemical Physics
Volume134
Issue number20
DOIs
StatePublished - May 28 2011

Fingerprint

Free energy
enzymes
free energy
Triose-Phosphate Isomerase
Polarization
proteins
Proton transfer
Energy barriers
polarization
Enzymes
Catalysis
electronics
catalysis
Protons
Chemical reactions
chemical reactions
Proteins
simulation
protons
profiles

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry
  • Medicine(all)

Cite this

Protein's electronic polarization contributes significantly to its catalytic function. / Xiang, Yun; Duan, Lili; Zhang, John.

In: Journal of Chemical Physics, Vol. 134, No. 20, 205101, 28.05.2011.

Research output: Contribution to journalArticle

@article{bdeaf8d86a89448c891069e4320078b0,
title = "Protein's electronic polarization contributes significantly to its catalytic function",
abstract = "Ab initio quantum mechanicalmolecular mechanical method is combined with the polarized protein-specific charge to study the chemical reactions catalyzed by protein enzymes. Significant improvement in the accuracy and efficiency of free-energy simulation is demonstrated by calculating the free-energy profile of the primary proton transfer reaction in triosephosphate isomerase. Quantitative agreement with experimental results is achieved. Our simulation results indicate that electronic polarization makes important contribution to enzyme catalysis by lowering the energy barrier by as much as 3 kcalmol.",
author = "Yun Xiang and Lili Duan and John Zhang",
year = "2011",
month = "5",
day = "28",
doi = "10.1063/1.3592987",
language = "English (US)",
volume = "134",
journal = "Journal of Chemical Physics",
issn = "0021-9606",
publisher = "American Institute of Physics Publising LLC",
number = "20",

}

TY - JOUR

T1 - Protein's electronic polarization contributes significantly to its catalytic function

AU - Xiang, Yun

AU - Duan, Lili

AU - Zhang, John

PY - 2011/5/28

Y1 - 2011/5/28

N2 - Ab initio quantum mechanicalmolecular mechanical method is combined with the polarized protein-specific charge to study the chemical reactions catalyzed by protein enzymes. Significant improvement in the accuracy and efficiency of free-energy simulation is demonstrated by calculating the free-energy profile of the primary proton transfer reaction in triosephosphate isomerase. Quantitative agreement with experimental results is achieved. Our simulation results indicate that electronic polarization makes important contribution to enzyme catalysis by lowering the energy barrier by as much as 3 kcalmol.

AB - Ab initio quantum mechanicalmolecular mechanical method is combined with the polarized protein-specific charge to study the chemical reactions catalyzed by protein enzymes. Significant improvement in the accuracy and efficiency of free-energy simulation is demonstrated by calculating the free-energy profile of the primary proton transfer reaction in triosephosphate isomerase. Quantitative agreement with experimental results is achieved. Our simulation results indicate that electronic polarization makes important contribution to enzyme catalysis by lowering the energy barrier by as much as 3 kcalmol.

UR - http://www.scopus.com/inward/record.url?scp=79958083942&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79958083942&partnerID=8YFLogxK

U2 - 10.1063/1.3592987

DO - 10.1063/1.3592987

M3 - Article

C2 - 21639481

AN - SCOPUS:79958083942

VL - 134

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

SN - 0021-9606

IS - 20

M1 - 205101

ER -