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Fig. 5 Overall structure of PSII dimer from Thermosynechococcus vulcanus at a resolution of
1.9Å. View from the direction perpendicular to the membrane normal. a Overall structure. The
protein subunits are coloured individually in the right hand monomer and in light grey in the left-
hand monomer, and the cofactors are coloured in the left-hand monomer and in light grey in the
right-hand monomer. Orange balls represent water molecules. b Arrangement of water molecules
in the PSII dimer. The protein subunits are coloured in light grey and all other cofactors are omit-
ted. The central broken lines are the noncrystallographic two-fold axes relating the two mono-
mers. Data source Umena et al. ( 2011 )
(one of which is in the Mn 4 Ca cluster), three Cl ions (two of which are near
the Mn 4 CaO 5 cluster), one bicarbonate ion and more than 15 detergents (Fig. 5 )
(Krauß 2003 ; Nilsson Lill 2011 ; Umena et al. 2011 ; Zouni et al. 2001 ; Kamiya and
Shen 2003 ; Ferreira et al. 2004 ; Loll et al. 2005 ; Murray et al. 2008 ; Kawakami
et al. 2009 ; Guskov et al. 2009 ; Biesiadka et al. 2004 ). PSII reaction center or pri-
mary donor P680 in PSII is an approximately C 2 -symmetric structure formed by
polypeptides (D1 and D2) and six chlorin cofactors: four chlorophyll a and two
pheophytin a (Pheo D1 and Pheo D2 ) (Fig. 5 ) (Nilsson Lill 2011 ; Umena et al. 2011 ).
Each PSII monomer consists of more than 1,300 water molecules, yielding a total
of 2,795 water molecules in the dimer (Umena et al. 2011 ). The water molecules
are organized into two layers located on the surfaces of the stromal and lumenal
sides, respectively, with the latter having more water molecules than the former
(Umena et al. 2011 ). A few water molecules are detected within the membrane
region, most of them serving as ligands to chlorophylls (Umena et al. 2011 ).
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