Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP

Minako Kondo; Ismael A. Heisler; Deborah Stoner-Ma; Peter J. Tonge; Stephen R. Meech

doi:10.1021/ja907690g

Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP

Minako Kondo
, Ismael A. Heisler
, Deborah Stoner-Ma
, Peter J. Tonge
, Stephen R. Meech

Chemistry

University of East Anglia
Stony Brook University

Research output: Contribution to journal › Article › peer-review

40 Scopus citations

Abstract

(Chemical Equation Presented) Ultrafast proton transfer dynamics on a short H-bond in a protein were studied through the time-resolved fluorescence of the S65T/H148D green fluorescent protein (GFP) mutant. In response to the change in chromophore pK_a upon excitation, the donor-proton-acceptor structure evolves on a sub-100 fs time scale, followed by picosecond time scale vibrational cooling and host structure reorganization.

Original language	English
Pages (from-to)	1452-1453
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	132
Issue number	5
DOIs	https://doi.org/10.1021/ja907690g
State	Published - Feb 10 2010

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title = "Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP",

abstract = "(Chemical Equation Presented) Ultrafast proton transfer dynamics on a short H-bond in a protein were studied through the time-resolved fluorescence of the S65T/H148D green fluorescent protein (GFP) mutant. In response to the change in chromophore pKa upon excitation, the donor-proton-acceptor structure evolves on a sub-100 fs time scale, followed by picosecond time scale vibrational cooling and host structure reorganization.",

author = "Minako Kondo and Heisler, \{Ismael A.\} and Deborah Stoner-Ma and Tonge, \{Peter J.\} and Meech, \{Stephen R.\}",

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T2 - S65T/H148D GFP

AU - Kondo, Minako

AU - Heisler, Ismael A.

AU - Stoner-Ma, Deborah

AU - Tonge, Peter J.

AU - Meech, Stephen R.

PY - 2010/2/10

Y1 - 2010/2/10

N2 - (Chemical Equation Presented) Ultrafast proton transfer dynamics on a short H-bond in a protein were studied through the time-resolved fluorescence of the S65T/H148D green fluorescent protein (GFP) mutant. In response to the change in chromophore pKa upon excitation, the donor-proton-acceptor structure evolves on a sub-100 fs time scale, followed by picosecond time scale vibrational cooling and host structure reorganization.

AB - (Chemical Equation Presented) Ultrafast proton transfer dynamics on a short H-bond in a protein were studied through the time-resolved fluorescence of the S65T/H148D green fluorescent protein (GFP) mutant. In response to the change in chromophore pKa upon excitation, the donor-proton-acceptor structure evolves on a sub-100 fs time scale, followed by picosecond time scale vibrational cooling and host structure reorganization.

UR - https://www.scopus.com/pages/publications/76149115551

U2 - 10.1021/ja907690g

DO - 10.1021/ja907690g

M3 - Article

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AN - SCOPUS:76149115551

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JO - Journal of the American Chemical Society

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ER -

Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP

Abstract

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