Linked Life Data

15125669

Source:http://linkedlifedata.com/resource/pubmed/id/15125669

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2004-5-5
pubmed:abstractText
The proton-coupled electron transfer reaction catalyzed by soybean lipoxygenase-1 is studied with a multistate continuum theory that represents the transferring hydrogen nucleus as a quantum mechanical wave function. The inner-sphere reorganization energy of the iron cofactor is calculated with density functional theory, and the outer-sphere reorganization energy of the protein is calculated with the frequency-resolved cavity model for conformations obtained with docking simulations. Both classical and quantum mechanical treatments of the proton donor-acceptor vibrational motion are presented. The temperature dependence of the calculated rates and kinetic isotope effects is in agreement with the experimental data. The weak temperature dependence of the rates is due to the relatively small free energy barrier arising from a balance between the reorganization energy and the reaction free energy. The unusually high deuterium kinetic isotope effect of 81 is due to the small overlap of the reactant and product proton vibrational wave functions and the dominance of the lowest energy reactant and product vibronic states in the tunneling process. The temperature dependence of the kinetic isotope effect is strongly influenced by the proton donor-acceptor distance with the dominant contribution to the overall rate. This dominant proton donor-acceptor distance is significantly smaller than the equilibrium donor-acceptor distance and is determined by a balance between the larger coupling and the smaller Boltzmann probability as the distance decreases. Thus, the proton donor-acceptor vibrational motion plays a vital role in decreasing the dominant donor-acceptor distance relative to its equilibrium value to facilitate the proton-coupled electron transfer reaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5763-75
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Proton-coupled electron transfer in soybean lipoxygenase.
pubmed:affiliation
Department of Chemistry, 152 Davey Laboratory, Pennsylvania State University, University Park, Pennsylvania, 16802, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.