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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 38 (1993), S. 279-296 
    ISSN: 1573-5079
    Keywords: electrochromic changes ; oxygen-evolving complex ; Photosystem II ; proton release ; protolytic reactions ; Tyrosine Z
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Old and very recent experiments on the extent and the rate of proton release during the four reaction steps of photosynthetic water oxidation are reviewed. Proton release is discussed in terms of three main sources, namely the chemical production upon electron abstraction from water, protolytic reactions of Mn-ligands (e.g. oxo-bridges), and electrostatic response of neighboring amino acids. The extent of proton release differs between the four oxidation steps and greatly varies as a function of pH both, but differently, in thylakoids and PS II-membranes. Contrastingly, it is about constant in PS II-core particles. In any preparation, and on most if not all reaction steps, a large portion of proton transfer can occur very rapidly (〈20 μs) and before the oxidation of the Mn-cluster by Yz + is completed. By these electrostatically driven reactions the catalytic center accumulates bases. An additional slow phase is observed during the oxygen evolving step, S3⇒S4→S0. Depending on pH, this phase consists of a release or an uptake of protons which accounts for the balance between the number of preformed bases and the four chemically produced protons. These data are compatible with the hypothesis of concerted electron/proton-transfer to overcome the kinetic and energetic constraints of water oxidation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 51 (1997), S. 27-42 
    ISSN: 1573-5079
    Keywords: Photosystem I ; Photosystem II ; photosynthetic reaction center ; bacteriorhodopsin ; evolution ; UV-protection ; t Rhodopseudomonasviridis ; t Heliobacillus mobilis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sequence alignments between membrane-spanning segments of pheophytin-quinone-type photosynthetic reaction centers, FeS-type photosynthetic reaction centers, core chlorophyll-proteins of PS II, chlorophyll t a/t b-containing antenna proteins of plants and light-harvesting complexes of purple bacteria led us to postulate a large common ancestral pigment-carrying protein with more than 10 membrane spans. Its original function as a UV-protector of the primordial cell is discussed. It is conceivable that a purely dissipative photochemistry started still in the context of the UV-protection. We suggest that mutations causing the t loss of certain porphyrin-type pigments led to the acquisition of redox cofactors and paved the way for a gradual transition from dissipative to productive photochemistry.
    Type of Medium: Electronic Resource
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