TY - JOUR
T1 - The mechanism of proton transfer between adjacent sites on the molecular surface
AU - Gutman, Menachem
AU - Nachliel, Esther
AU - Friedman, Ran
N1 - Funding Information:
The authors are grateful to Professor Steve Scheiner, from Utah State University, for his assistance and advice. The authors are grateful to their colleagues from the Laser Laboratory for Fast Reactions in Biology for their cooperation and for providing us with their results. The research in the Laser Laboratory for Fast Reactions in Biology is supported by the following research grants: The Israeli Science Foundation (472/01–2), and the Center of Complexity Sciences (GR2004-032). R. F. would like to acknowledge the Colton Foundation for a Colton Fellowship.
PY - 2006/8
Y1 - 2006/8
N2 - The surface of a protein, or a membrane, is spotted with a multitude of proton binding sites, some of which are only few Å apart. When a proton is released from one site, it propagates through the water by a random walk under the bias of the local electrostatic potential determined by the distribution of the charges on the protein. Eventually, the released protons are dispersed in the bulk, but during the first few nanoseconds after the dissociation, the protons can be trapped by encounter with nearby acceptor sites. While the study of this reaction on the surface of a protein suffers from experimental and theoretical difficulties, it can be investigated with simple model compounds like derivatives of fluorescein. In the present study, we evaluate the mechanism of proton transfer reactions that proceed, preferentially, inside the Coulomb cage of the dye molecules. Kinetic analysis of the measured dynamics reveals the role of the dimension of the Coulomb cage on the efficiency of the reaction and how the ordering of the water molecules by the dye affects the kinetic isotope effect.
AB - The surface of a protein, or a membrane, is spotted with a multitude of proton binding sites, some of which are only few Å apart. When a proton is released from one site, it propagates through the water by a random walk under the bias of the local electrostatic potential determined by the distribution of the charges on the protein. Eventually, the released protons are dispersed in the bulk, but during the first few nanoseconds after the dissociation, the protons can be trapped by encounter with nearby acceptor sites. While the study of this reaction on the surface of a protein suffers from experimental and theoretical difficulties, it can be investigated with simple model compounds like derivatives of fluorescein. In the present study, we evaluate the mechanism of proton transfer reactions that proceed, preferentially, inside the Coulomb cage of the dye molecules. Kinetic analysis of the measured dynamics reveals the role of the dimension of the Coulomb cage on the efficiency of the reaction and how the ordering of the water molecules by the dye affects the kinetic isotope effect.
KW - Coloumb cage
KW - Flourescein
KW - Intra-molecular proton transfer
KW - Kinetic isotope effect
KW - Laser induced proton pulse
KW - Molecular dynamics
KW - Molecular surface
KW - Proton Transfer
UR - http://www.scopus.com/inward/record.url?scp=33748899467&partnerID=8YFLogxK
U2 - 10.1016/j.bbabio.2006.01.012
DO - 10.1016/j.bbabio.2006.01.012
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C2 - 16581015
AN - SCOPUS:33748899467
SN - 0005-2728
VL - 1757
SP - 931
EP - 941
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 8
ER -