Summary
The results from an investigation of the molecular composition of photosynthetic membrane-protein complexes using radiation inactivation techniques are discussed. Evidence has been obtained to indicate that water oxidation in PS2 needs more polypeptides than is required for reaction centre function. Reaction centre chlorophyll inactivation has unusual characteristics in PS1 and the bacterial reaction centre giving a small target size and in PS2 indicates the involvement of stronger protein binding to electron carriers than found in the other reaction centres. in the cytochrome b6f complex a result explained by binding of the inhibitor DBMIB to the cytochrome b 6 protein is supported by examination of the amino acid sequence for quinone binding sites. A possible quinone binding site on a PS1 65–70 kDa polypeptide can also be postulated.
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© 1987 Martinus Nijhoff Publishers, Dordrecht
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Nugent, J.H.A. (1987). The Molecular Size of Photosynthetic Membrane Protein Complexes. In: Biggins, J. (eds) Progress in Photosynthesis Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-3535-8_2
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DOI: https://doi.org/10.1007/978-94-009-3535-8_2
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-8080-4
Online ISBN: 978-94-009-3535-8
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