Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 377-377 |
| Journal | Biochimica et Biophysica Acta. B, Bioenergetics |
| Volume | 1847 |
| Issue number | 3 |
| DOIs |
|
| Publication status | Published - 2015 |
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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 journal › Comment/Letter to the editor › Academic
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 -