Abstract
The oxygen-evolving complex (OEC) is a Mn4O5Ca cluster embedded in the Photosystem II (PSII) protein complex. As the site of water oxidation, the OEC is connected to the lumen by channels that conduct water, oxygen, and/or protons during the catalytic cycle. The hydrogen-bond networks found in these channels also serve to stabilize the oxidized intermediates, known as the S states. We review recent developments in characterizing these networks via protein mutations, molecular inhibitors, and computational modeling. On the basis of these results, we highlight regions of the PSII protein in which changes have indirect effects on the S1, S2, and S3 oxidation states of the OEC while still allowing photosynthetic activity.
| Original language | English |
|---|---|
| Pages (from-to) | 152?158 |
| Journal | Current Opinion in Chemical Biology |
| Volume | 25 |
| DOIs | |
| Publication status | Published - Apr 1 2015 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Analytical Chemistry
Cite this
Oxygen-evolving complex of Photosystem II : An analysis of second-shell residues and hydrogen-bonding networks. / Vogt, Leslie; Vinyard, David J.; Khan, Sahr; Brudvig, Gary W.
In: Current Opinion in Chemical Biology, Vol. 25, 01.04.2015, p. 152?158.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Oxygen-evolving complex of Photosystem II
T2 - An analysis of second-shell residues and hydrogen-bonding networks
AU - Vogt, Leslie
AU - Vinyard, David J.
AU - Khan, Sahr
AU - Brudvig, Gary W
PY - 2015/4/1
Y1 - 2015/4/1
N2 - The oxygen-evolving complex (OEC) is a Mn4O5Ca cluster embedded in the Photosystem II (PSII) protein complex. As the site of water oxidation, the OEC is connected to the lumen by channels that conduct water, oxygen, and/or protons during the catalytic cycle. The hydrogen-bond networks found in these channels also serve to stabilize the oxidized intermediates, known as the S states. We review recent developments in characterizing these networks via protein mutations, molecular inhibitors, and computational modeling. On the basis of these results, we highlight regions of the PSII protein in which changes have indirect effects on the S1, S2, and S3 oxidation states of the OEC while still allowing photosynthetic activity.
AB - The oxygen-evolving complex (OEC) is a Mn4O5Ca cluster embedded in the Photosystem II (PSII) protein complex. As the site of water oxidation, the OEC is connected to the lumen by channels that conduct water, oxygen, and/or protons during the catalytic cycle. The hydrogen-bond networks found in these channels also serve to stabilize the oxidized intermediates, known as the S states. We review recent developments in characterizing these networks via protein mutations, molecular inhibitors, and computational modeling. On the basis of these results, we highlight regions of the PSII protein in which changes have indirect effects on the S1, S2, and S3 oxidation states of the OEC while still allowing photosynthetic activity.
UR - http://www.scopus.com/inward/record.url?scp=84921533157&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84921533157&partnerID=8YFLogxK
U2 - 10.1016/j.cbpa.2014.12.040
DO - 10.1016/j.cbpa.2014.12.040
M3 - Article
VL - 25
SP - 152?158
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
SN - 1367-5931
ER -