15 research outputs found
A hydrogen-atom abstraction model for the function of Y-Z in photosynthetic oxygen evolution
Recent magnetic-resonance work on Y-Z suggests that this species exhibits considerable motional flexibility in its functional site and that its phenol oxygen is not involved in a well-ordered hydrogen-bond interaction (Tang et al., submitted; Tommos et al., in press). Both of these observations are inconsistent with a simple electron-transfer function for this radical in photosynthetic water oxidation. By considering the roles of catalytically active amino acid radicals in other enzymes and recent data on the water-oxidation process in Photosystem II, we rationalize these observations by suggesting that Y-Z functions to abstract hydrogen atoms from aquo- and hydroxy-bound manganese ions in the (Mn)(4) cluster on each S-state transition. The hydrogen-atom abstraction process may occur either by sequential or concerted kinetic pathways. Within this model, the (Mn)(4)/Y-Z center forms a single catalytic center that comprises the Oxygen Evolving Complex in Photosystem II
Manganese and tyrosyl radical function in photosynthetic oxygen evolution
Photosystem II catalyzes the photosynthetic oxidation of
water to O 2. The structural and functional basis for this
remarkable process is emerging. The catalytic site contains
a tetramanganese cluster, calcium, chloride and a redox-active
tyrosine organized so as to promote electroneutral hydrogen
atom abstraction from manganese-bound substrate water
by the tyrosyl radical. Recent work is assessed within the
framework of this model for the water oxidizing process