Corrigendum to “Fluorescence kinetics of PSII crystals containing Ca2+ or Sr2+ in the oxygen evolving complex [Biochim. Biophys. Acta Bioenerg. 1837 (2014) 264–269]

B.F. van Oort, J. Kargul, K. Maghlaouic, J. Barber, H. van Amerongen

Research output: Contribution to journalComment/Letter to the editorAcademic

Abstract

Photosystem II (PSII) is the pigment–protein complex which converts sunlight energy into chemical energy by catalysing the process of light-driven oxidation of water into reducing equivalents in the form of protons and electrons. Three-dimensional structures from x-ray crystallography have been used extensively to model these processes. However, the crystal structures are not necessarily identical to those of the solubilised complexes. Here we compared picosecond fluorescence of solubilised and crystallised PSII core particles isolated from the thermophilic cyanobacterium Thermosynechococcus elongatus. The fluorescence of the crystals is sensitive to the presence of artificial electron acceptors (K3Fe(CN)3) and electron transport inhibitors (DCMU). In PSII with reaction centres in the open state, the picosecond fluorescence of PSII crystals and solubilised PSII is indistinguishable. Additionally we compared picosecond fluorescence of native PSIIwith PSII inwhich Ca2 in the oxygen evolving complex (OEC) is biosynthetically replaced by Sr2+. With the Sr2+ replaced OEC the average fluorescence decay slows down slightly (81 ps to 85 ps), and reaction centres are less readily closed, indicating that both energy transfer/trapping and electron transfer are affected by the replacement.
Original languageEnglish
Pages (from-to)377-377
JournalBiochimica et Biophysica Acta. B, Bioenergetics
Volume1847
Issue number3
DOIs
Publication statusPublished - 2015

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Photosystem II Protein Complex
Fluorescence
Oxygen
Crystals
Kinetics
Electrons
Diuron
Crystallography
Sunlight
Energy Transfer
Cyanobacteria
Electron Transport
Energy transfer
corrigendum
Protons
Crystal structure
X-Rays
Light
X rays
Oxidation

Cite this

@article{3299fbdb5fce4c9d8a7222e326f16b52,
title = "Corrigendum to “Fluorescence kinetics of PSII crystals containing Ca2+ or Sr2+ in the oxygen evolving complex [Biochim. Biophys. Acta Bioenerg. 1837 (2014) 264–269]",
abstract = "Photosystem II (PSII) is the pigment–protein complex which converts sunlight energy into chemical energy by catalysing the process of light-driven oxidation of water into reducing equivalents in the form of protons and electrons. Three-dimensional structures from x-ray crystallography have been used extensively to model these processes. However, the crystal structures are not necessarily identical to those of the solubilised complexes. Here we compared picosecond fluorescence of solubilised and crystallised PSII core particles isolated from the thermophilic cyanobacterium Thermosynechococcus elongatus. The fluorescence of the crystals is sensitive to the presence of artificial electron acceptors (K3Fe(CN)3) and electron transport inhibitors (DCMU). In PSII with reaction centres in the open state, the picosecond fluorescence of PSII crystals and solubilised PSII is indistinguishable. Additionally we compared picosecond fluorescence of native PSIIwith PSII inwhich Ca2 in the oxygen evolving complex (OEC) is biosynthetically replaced by Sr2+. With the Sr2+ replaced OEC the average fluorescence decay slows down slightly (81 ps to 85 ps), and reaction centres are less readily closed, indicating that both energy transfer/trapping and electron transfer are affected by the replacement.",
author = "{van Oort}, B.F. and J. Kargul and K. Maghlaouic and J. Barber and {van Amerongen}, H.",
year = "2015",
doi = "10.1016/j.bbabio.2014.11.007",
language = "English",
volume = "1847",
pages = "377--377",
journal = "Biochimica et Biophysica Acta. B, Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "3",

}

Corrigendum to “Fluorescence kinetics of PSII crystals containing Ca2+ or Sr2+ in the oxygen evolving complex [Biochim. Biophys. Acta Bioenerg. 1837 (2014) 264–269]. / van Oort, B.F.; Kargul, J.; Maghlaouic, K.; Barber, J.; van Amerongen, H.

In: Biochimica et Biophysica Acta. B, Bioenergetics, Vol. 1847, No. 3, 2015, p. 377-377.

Research output: Contribution to journalComment/Letter to the editorAcademic

TY - JOUR

T1 - Corrigendum to “Fluorescence kinetics of PSII crystals containing Ca2+ or Sr2+ in the oxygen evolving complex [Biochim. Biophys. Acta Bioenerg. 1837 (2014) 264–269]

AU - van Oort, B.F.

AU - Kargul, J.

AU - Maghlaouic, K.

AU - Barber, J.

AU - van Amerongen, H.

PY - 2015

Y1 - 2015

N2 - Photosystem II (PSII) is the pigment–protein complex which converts sunlight energy into chemical energy by catalysing the process of light-driven oxidation of water into reducing equivalents in the form of protons and electrons. Three-dimensional structures from x-ray crystallography have been used extensively to model these processes. However, the crystal structures are not necessarily identical to those of the solubilised complexes. Here we compared picosecond fluorescence of solubilised and crystallised PSII core particles isolated from the thermophilic cyanobacterium Thermosynechococcus elongatus. The fluorescence of the crystals is sensitive to the presence of artificial electron acceptors (K3Fe(CN)3) and electron transport inhibitors (DCMU). In PSII with reaction centres in the open state, the picosecond fluorescence of PSII crystals and solubilised PSII is indistinguishable. Additionally we compared picosecond fluorescence of native PSIIwith PSII inwhich Ca2 in the oxygen evolving complex (OEC) is biosynthetically replaced by Sr2+. With the Sr2+ replaced OEC the average fluorescence decay slows down slightly (81 ps to 85 ps), and reaction centres are less readily closed, indicating that both energy transfer/trapping and electron transfer are affected by the replacement.

AB - Photosystem II (PSII) is the pigment–protein complex which converts sunlight energy into chemical energy by catalysing the process of light-driven oxidation of water into reducing equivalents in the form of protons and electrons. Three-dimensional structures from x-ray crystallography have been used extensively to model these processes. However, the crystal structures are not necessarily identical to those of the solubilised complexes. Here we compared picosecond fluorescence of solubilised and crystallised PSII core particles isolated from the thermophilic cyanobacterium Thermosynechococcus elongatus. The fluorescence of the crystals is sensitive to the presence of artificial electron acceptors (K3Fe(CN)3) and electron transport inhibitors (DCMU). In PSII with reaction centres in the open state, the picosecond fluorescence of PSII crystals and solubilised PSII is indistinguishable. Additionally we compared picosecond fluorescence of native PSIIwith PSII inwhich Ca2 in the oxygen evolving complex (OEC) is biosynthetically replaced by Sr2+. With the Sr2+ replaced OEC the average fluorescence decay slows down slightly (81 ps to 85 ps), and reaction centres are less readily closed, indicating that both energy transfer/trapping and electron transfer are affected by the replacement.

U2 - 10.1016/j.bbabio.2014.11.007

DO - 10.1016/j.bbabio.2014.11.007

M3 - Comment/Letter to the editor

VL - 1847

SP - 377

EP - 377

JO - Biochimica et Biophysica Acta. B, Bioenergetics

JF - Biochimica et Biophysica Acta. B, Bioenergetics

SN - 0005-2728

IS - 3

ER -