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Title: Fluorescence decay kinetics of wild type and D2-H117N mutant photosystem II reaction centers isolated from Chlamydomonas reinhardtii

Abstract

The authors compare the chlorophyll fluorescence decay kinetics of the wild type and the D2-H117N mutant photosystem II reaction centers isolated from Chlamydomonas reinhardtii. The histidine residue located at site 117 on the D2 polypeptide of photosystem II is a proposed binding site for one of two peripheral accessory chlorophylls located in the reaction center complex. The peripheral accessory chlorophylls are thought to be coupled with the primary electron donor, P680, and thus involved in energy transfer with P680. The conservative replacement of the histidine residue with an asparagine residue allows the chlorophyll to remain bound to the reaction center. However, slight changes in the structural organization of the reaction center may exist that can affect the energy transfer kinetics. The authors show that the D2-H117N mutation causes a shift in the 20--30 ps lifetime component that has been associated with energy equilibration among coupled chlorophylls in the photosystem II reaction center.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Ohio State Univ., Columbus, OH (US)
Sponsoring Org.:
USDOE
OSTI Identifier:
20075910
Resource Type:
Journal Article
Journal Name:
Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical
Additional Journal Information:
Journal Volume: 104; Journal Issue: 19; Other Information: PBD: 18 May 2000; Journal ID: ISSN 1089-5647
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 14 SOLAR ENERGY; KINETICS; MUTANTS; FLUORESCENCE; PHOTOSYNTHETIC REACTION CENTERS; CHLAMYDOMONAS; HISTIDINE

Citation Formats

Johnston, H.G., Want, J., Ruffle, S.V., Sayre, R.T., and Gustafson, T.L. Fluorescence decay kinetics of wild type and D2-H117N mutant photosystem II reaction centers isolated from Chlamydomonas reinhardtii. United States: N. p., 2000. Web. doi:10.1021/jp993556l.
Johnston, H.G., Want, J., Ruffle, S.V., Sayre, R.T., & Gustafson, T.L. Fluorescence decay kinetics of wild type and D2-H117N mutant photosystem II reaction centers isolated from Chlamydomonas reinhardtii. United States. doi:10.1021/jp993556l.
Johnston, H.G., Want, J., Ruffle, S.V., Sayre, R.T., and Gustafson, T.L. Thu . "Fluorescence decay kinetics of wild type and D2-H117N mutant photosystem II reaction centers isolated from Chlamydomonas reinhardtii". United States. doi:10.1021/jp993556l.
@article{osti_20075910,
title = {Fluorescence decay kinetics of wild type and D2-H117N mutant photosystem II reaction centers isolated from Chlamydomonas reinhardtii},
author = {Johnston, H.G. and Want, J. and Ruffle, S.V. and Sayre, R.T. and Gustafson, T.L.},
abstractNote = {The authors compare the chlorophyll fluorescence decay kinetics of the wild type and the D2-H117N mutant photosystem II reaction centers isolated from Chlamydomonas reinhardtii. The histidine residue located at site 117 on the D2 polypeptide of photosystem II is a proposed binding site for one of two peripheral accessory chlorophylls located in the reaction center complex. The peripheral accessory chlorophylls are thought to be coupled with the primary electron donor, P680, and thus involved in energy transfer with P680. The conservative replacement of the histidine residue with an asparagine residue allows the chlorophyll to remain bound to the reaction center. However, slight changes in the structural organization of the reaction center may exist that can affect the energy transfer kinetics. The authors show that the D2-H117N mutation causes a shift in the 20--30 ps lifetime component that has been associated with energy equilibration among coupled chlorophylls in the photosystem II reaction center.},
doi = {10.1021/jp993556l},
journal = {Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical},
issn = {1089-5647},
number = 19,
volume = 104,
place = {United States},
year = {2000},
month = {5}
}