Mutagenesis of the Symmetry Related H117 Residue in the Photosystem II D2 Protein of Chlamydomonas: Implications for Energy Transfer from ... View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1998

AUTHORS

Stuart Ruffle , Ronald Hutchison , Richard T. Sayre

ABSTRACT

Similar to the quinone-type, bacterial photosynthetic reaction center (BRC), the photosystem II (PSII) reaction center complex contains four-five polypeptides. These polypeptides include: the D1, D2, cytochrome b559 polypeptides, plus a small polypeptide, psbI known from its gene product [1–5]. Two of the polypeptides (D1 and D2) have substantial sequence and topological similarity to the L and M subunits of the BRC [2, 4, 5]. Regions of the L and M and D1 and D2 proteins which are most highly conserved are the non-heme Fe and the chlorophyll special pair (ChlSP)ligands and adjacent residues. Similar to the BRC the PII complex has two quinones (QA and QB) per reaction center complex, but in contrast to the BRC has 6 chlorophylls per 2 pheophytins [6] (Figure 1). Two of the chlorophylls make up the chlorophyll special pair, two chlorophyll monomers participate in electron transfer between the Chlsp and pheophytin, and an additional pair of accessory chlorophylls is thought to be located at the margins of the reaction center complex [6–8]. It has been proposed that the accessory chlorophylls function as antennae or are involved in an electron transfer cycle around PSII (including cytochrome b559) which protects PSU from photoinhibitory protein degradation [7–9]. More... »

PAGES

1013-1016

References to SciGraph publications

Book

TITLE

Photosynthesis: Mechanisms and Effects

ISBN

978-0-7923-5547-2
978-94-011-3953-3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-3953-3_240

DOI

http://dx.doi.org/10.1007/978-94-011-3953-3_240

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1090933114


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