Probing mode and site of substrate water binding to the oxygen-evolving complex in the S2 state of photosystem II by 17O-HYSCORE spectroscopy.
In the oxygen-evolving complex (OEC) of photosystem II (PSII) molecular oxygen is formed from two substrate water molecules that are ligated to a mu-oxo bridged cluster containing four Mn ions and one Ca ion (Mn4OxCa cluster; Ox symbolizes the unknown number of mu-oxo bridges; x >or= 5). There is a long-standing enigma as to when, where, and how the two substrate water molecules bind to the Mn4OxCa cluster during the cyclic water-splitting reaction, which involves five distinct redox intermediates (Si-states; i = 0,...,4). To address this question we employed hyperfine sublevel correlation (HYSCORE) spectroscopy on H217O-enriched PSII samples poised in the paramagnetic S2 state. This approach allowed us to resolve the magnetic interaction between one solvent exchangeable 17O that is directly ligated to one or more Mn ions of the Mn4OxCa cluster in the S2 state of PSII. Direct coordination of 17O to Mn is supported by the strong (A approximately 10 MHz) hyperfine coupling. Because these are properties expected from a substrate water molecule, this spectroscopic signature holds the potential for gaining long-sought information about the binding mode and site of one of the two substrate water molecules in the S2 state of PSII.
Su
Ji-Hu
JH
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
Lubitz
Wolfgang
W
Messinger
Johannes
J
D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D008345:Manganese / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D045332:Photosystem II Protein Complex / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D045332:Photosystem II Protein Complex; D014867:Water; D008345:Manganese; D010100:Oxygen