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Two D2 mutants were created with a site-directed mutation near the presumable binding site of Q A . In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to Q A  and/or in binding of Q A, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photoheterotroph. In another mutant the Gly-215 residue, located next to the His residue that is proposed to bind Q A  and Fe 2+ , was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction centers on a chlorophyll basis. We propose that proper binding of Q A  to the photosystem II reaction center complex is a prerequisite for stability of the photosystem II complex. Impairment of Q a binding leads to rapid inactivation of photosystem II, which may be followed by a structural disintegration of the complex.

Q a Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II