PMID- 19090684
OWN - NLM
STAT- MEDLINE
DCOM- 20090511
LR  - 20211020
IS  - 1520-6106 (Print)
IS  - 1520-5207 (Linking)
VI  - 113
IP  - 11
DP  - 2009 Mar 19
TI  - Photodynamics in complex environments: ab initio multiple spawning quantum 
      mechanical/molecular mechanical dynamics.
PG  - 3280-91
LID - 10.1021/jp8073464 [doi]
AB  - Our picture of reactions on electronically excited states has evolved 
      considerably in recent years, due to advances in our understanding of points of 
      degeneracy between different electronic states, termed "conical intersections" 
      (CIs). CIs serve as funnels for population transfer between different electronic 
      states, and play a central role in ultrafast photochemistry. Because most 
      practical photochemistry occurs in solution and protein environments, it is 
      important to understand the role complex environments play in directing 
      excited-state dynamics generally, as well as specific environmental effects on CI 
      geometries and energies. In order to model such effects, we employ the full 
      multiple spawning (FMS) method for multistate quantum dynamics, together with 
      hybrid quantum mechanical/molecular mechanical (QM/MM) potential energy surfaces 
      using both semiempirical and ab initio QM methods. In this article, we present an 
      overview of these methods, and a comparison of the excited-state dynamics of 
      several biological chromophores in solvent and protein environments. Aqueous 
      solvation increases the rate of quenching to the ground state for both the 
      photoactive yellow protein (PYP) and green fluorescent protein (GFP) 
      chromophores, apparently by energetic stabilization of their respective CIs. In 
      contrast, solvation in methanol retards the quenching process of the retinal 
      protonated Schiff base (RPSB), the rhodopsin chromophore. Protein environments 
      serve to direct the excited-state dynamics, leading to higher quantum yields and 
      enhanced reaction selectivity.
FAU - Virshup, Aaron M
AU  - Virshup AM
AD  - Department of Chemistry, Center for Biophysics and Computational Biology, 
      University of Illinois, Urbana, Illinois 61801, USA.
FAU - Punwong, Chutintorn
AU  - Punwong C
FAU - Pogorelov, Taras V
AU  - Pogorelov TV
FAU - Lindquist, Beth A
AU  - Lindquist BA
FAU - Ko, Chaehyuk
AU  - Ko C
FAU - Martinez, Todd J
AU  - Martinez TJ
LA  - eng
GR  - T32 GM008276/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - J Phys Chem B
JT  - The journal of physical chemistry. B
JID - 101157530
RN  - 0 (4-hydroxybenzylidene-1,2-dimethylimidazolinone)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Imidazolines)
RN  - 0 (Photoreceptors, Microbial)
RN  - 0 (Proteins)
RN  - 0 (Schiff Bases)
RN  - 0 (Solvents)
RN  - 0 (photoactive yellow protein, Bacteria)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - 9009-81-8 (Rhodopsin)
SB  - IM
MH  - Algorithms
MH  - Bacterial Proteins/chemistry
MH  - Electrochemistry
MH  - Electrons
MH  - Energy Transfer
MH  - Green Fluorescent Proteins/chemistry
MH  - Imidazolines/chemistry
MH  - Models, Molecular
MH  - Molecular Conformation
MH  - *Photochemistry
MH  - Photoreceptors, Microbial/chemistry
MH  - Proteins/*chemistry
MH  - *Quantum Theory
MH  - Rhodopsin/chemistry
MH  - Schiff Bases/chemistry
MH  - Solvents
MH  - Stereoisomerism
EDAT- 2008/12/19 09:00
MHDA- 2009/05/12 09:00
CRDT- 2008/12/19 09:00
PHST- 2008/12/19 09:00 [entrez]
PHST- 2008/12/19 09:00 [pubmed]
PHST- 2009/05/12 09:00 [medline]
AID - 10.1021/jp8073464 [pii]
AID - 10.1021/jp8073464 [doi]
PST - ppublish
SO  - J Phys Chem B. 2009 Mar 19;113(11):3280-91. doi: 10.1021/jp8073464.