Proton shuttle in green fluorescent protein studied by dynamic simulations.

Abstract:

:As a direct simulation of a multistep proton transfer reaction involving protein residues, the proton relay shuttle between A and I forms of green fluorescent protein (GFP) is simulated in atomic detail by using a special molecular dynamics simulation technique. Electronic excitation of neutral chromophore in wild-type GFP is generally followed by excited-state proton transfer to a nearby glutamic acid residue via a water molecule and a serine residue. Here we show that the second and third transfer steps occur ultrafast on time scales of several tens of femtoseconds. Proton back-shuttle in the ground state is slower and occurs in a different sequence of events. The simulations provide atomic models of various intermediates and yield realistic rate constants for proton transfer events. In particular, we argue that the I form observed spectroscopically under equilibrium conditions may differ from the I form observed as a fast intermediate by an anti to syn rotation of the carboxyl proton of neutral Glu-222.

authors

Lill MA,Helms V

doi

10.1073/pnas.052520799

keywords:

subject

Has Abstract

pub_date

2002-03-05 00:00:00

pages

2778-81

issue

5

eissn

0027-8424

issn

1091-6490

pii

99/5/2778

journal_volume

99

pub_type

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