@article{Dubas2016,
title = {Unified Model of Nanosecond Charge Recombination in Closed Reaction Centers from Rhodobacter sphaeroides : Role of Protein Polarization Dynamics},
author = {Katarzyna Dubas and M Baranowski and A Podhorodecki and M R Jones and Krzysztof Gibasiewicz},
url = {http://pubs.acs.org/doi/10.1021/acs.jpcb.6b01459},
doi = {10.1021/acs.jpcb.6b01459},
issn = {1520-6106},
year = {2016},
date = {2016-06-01},
journal = {The Journal of Physical Chemistry B},
volume = {120},
number = {22},
pages = {4890--4896},
publisher = {American Chemical Society},
abstract = {Ongoing questions surround the influence of protein dynamics on rapid processes such as biological electron transfer. Such questions are particularly addressable in light-activated systems. In Rhodobacter sphaeroides reaction centers, charge recombination or back electron transfer from the reduced bacteriopheophytin, HA–, to the oxidized dimeric bacteriochlorophyll, P+, may be monitored by both transient absorption spectroscopy and transient fluorescence spectroscopy. Signals measured with both these techniques decay in a similar three-exponential fashion with lifetimes of ∼0.6–0.7, ∼2–4, and ∼10–20 ns, revealing the complex character of this electron transfer reaction. In this study a single kinetic model was developed to connect lifetime and amplitude data from both techniques. The model took into account the possibility that electron transfer from HA– to P+ may occur with transient formation of the state P+BA–. As a result it was possible to model the impact of nanosecond protein relaxation on the free...},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
