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

Willem Vermaas, Jeroen Charité, Gaozhong Shen

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39 Scopus citations


Two D2 mutants were created with a site-directed mutation near the presumable binding site of QA. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to QAand/or in binding of QA, had been replaced by Leu, PS II was undetectable in thylakoids.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 QA and Fe2+, 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 QA to the photosystem II reaction center complex is a prerequisite for stability of the photosystem II complex. Impairment of QA binding leads to rapid inactivation of photosystem II, which may be followed by a structural disintegration of the complex.

Original languageEnglish (US)
Pages (from-to)359-365
Number of pages7
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Issue number5
StatePublished - May 1990


  • Cyanobacteria
  • Photoinhibition
  • Photosynthesis
  • Plastoquinone
  • Site-Directed Mutagenesis

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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