The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering

This short review summarizes our current knowledge about the functional relevance of protein dynamics in photosynthetic reaction centers. In the case of Photosystem II membrane fragments, elastic and quasielastic neutron scattering experiments reveal a dynamical transition at about 240 K correspondi...

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Main Author: Pieper Jörg
Format: Article
Language:English
Published: EDP Sciences 2015-01-01
Series:EPJ Web of Conferences
Online Access:http://dx.doi.org/10.1051/epjconf/20158302013
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author Pieper Jörg
author_facet Pieper Jörg
author_sort Pieper Jörg
collection DOAJ
description This short review summarizes our current knowledge about the functional relevance of protein dynamics in photosynthetic reaction centers. In the case of Photosystem II membrane fragments, elastic and quasielastic neutron scattering experiments reveal a dynamical transition at about 240 K corresponding to the activation of picosecond molecular motions. Likewise, a “freezing” of molecular dynamics is observed upon dehydration. Intriguingly, these effects correlate with the pronounced temperature- and hydration-dependence of specific electron transfer steps in Photosystem II indicating that molecular dynamics is an indispensable prerequisite for its function. Thus, electron transfer in Photosystem II appears to be a prototypical example for a dynamics-function correlation. Finally, the laser-neutron pump-probe technique is shown to permit in-situ monitoring of molecular dynamics in specific functional states of a protein in real time.
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spelling doaj.art-397aee3281874cbd80d0a47b5c80e8272022-12-21T23:18:35ZengEDP SciencesEPJ Web of Conferences2100-014X2015-01-01830201310.1051/epjconf/20158302013epjconf-Qens-Wins2014_02013The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scatteringPieper JörgThis short review summarizes our current knowledge about the functional relevance of protein dynamics in photosynthetic reaction centers. In the case of Photosystem II membrane fragments, elastic and quasielastic neutron scattering experiments reveal a dynamical transition at about 240 K corresponding to the activation of picosecond molecular motions. Likewise, a “freezing” of molecular dynamics is observed upon dehydration. Intriguingly, these effects correlate with the pronounced temperature- and hydration-dependence of specific electron transfer steps in Photosystem II indicating that molecular dynamics is an indispensable prerequisite for its function. Thus, electron transfer in Photosystem II appears to be a prototypical example for a dynamics-function correlation. Finally, the laser-neutron pump-probe technique is shown to permit in-situ monitoring of molecular dynamics in specific functional states of a protein in real time.http://dx.doi.org/10.1051/epjconf/20158302013
spellingShingle Pieper Jörg
The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering
EPJ Web of Conferences
title The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering
title_full The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering
title_fullStr The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering
title_full_unstemmed The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering
title_short The functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering
title_sort functional role of protein dynamics in photosynthetic reaction centers investigated by elastic and quasielastic neutron scattering
url http://dx.doi.org/10.1051/epjconf/20158302013
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