In this section
@article{Salna:2016:10.1038/nchem.2527,
author = {Salna, B and Benabbas, A and Sage, JT and van, Thor J and Champion, PM},
doi = {10.1038/nchem.2527},
journal = {Nature Chemistry},
pages = {874--880},
title = {Wide-dynamic-range kinetic investigations of deep proton tunnelling in proteins},
url = {http://dx.doi.org/10.1038/nchem.2527},
volume = {8},
year = {2016}
}
TY - JOUR
AB - Directional proton transport along ‘wires’ that feed biochemical reactions in proteins is poorly understood. Amino-acid residues with high pKa are seldom considered as active transport elements in such wires because of their large classical barrier for proton dissociation. Here, we use the light-triggered proton wire of the green fluorescent protein to study its ground-electronic-state proton-transport kinetics, revealing a large temperature-dependent kinetic isotope effect. We show that ‘deep’ proton tunnelling between hydrogen-bonded oxygen atoms with a typical donor–acceptor distance of 2.7–2.8Å fully accounts for the rates at all temperatures, including the unexpectedly large value (2.5 × 109s−1) found at room temperature. The rate-limiting step in green fluorescent protein is assigned to tunnelling of the ionization-resistant serine hydroxyl proton. This suggests how high-pKa residues within a proton wire can act as a ‘tunnel diode’ to kinetically trap protons and control the direction of proton flow.
AU - Salna,B
AU - Benabbas,A
AU - Sage,JT
AU - van,Thor J
AU - Champion,PM
DO - 10.1038/nchem.2527
EP - 880
PY - 2016///
SN - 1755-4330
SP - 874
TI - Wide-dynamic-range kinetic investigations of deep proton tunnelling in proteins
T2 - Nature Chemistry
UR - http://dx.doi.org/10.1038/nchem.2527
VL - 8
ER -
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