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Title

Increased tolerance to thermal inactivation of oxygen evolution in spinach Photosystem II membranes by substitution of the extrinsic 33-kDa protein by its homologue from a thermophilic cyanobacterium

AuthorsPueyo, José Javier ; Alfonso Lozano, Miguel ; Andrés Plou, Carmen; Picorel Castaño, Rafael
KeywordsOxygen evolution
33-kDa protein
Photosystem II
Heat inactivation
Manganese stabilizing protein
Issue DateApr-2002
PublisherElsevier
CitationPueyo JJ, Alfonso M, Andres C, Picorel R. Increased tolerance to thermal inactivation of oxygen evolution in spinach Photosystem II membranes by substitution of the extrinsic 33-kDa protein by its homologue from a thermophilic cyanobacterium. Biochimica et Biophysica Acta - Bioenergetics 1554 (1-2): 29-35 (2002)
AbstractPhotosynthetic oxygen evolution is an extremely heat-sensitive process and incubation of spinach Photosystem II (PSII) membranes at 40 °C for only several minutes leads to its complete inactivation. Substitution experiments of the spinach 33-kDa manganese stabilizing protein by a homologue protein, isolated either from the thermophilic cyanobacterium Phormidium laminosum, or from Escherichia coli as a recombinant thermophilic cyanobacterial protein, showed a significant increase in tolerance to heat inactivation of the oxygen-evolving activity. The results allow us to suggest that thermal inactivation of oxygen evolution in higher plant PSII membranes is due to dissociation of the 33-kDa protein as a consequence of temperature-induced conformational changes, and stabilization can be provided by substitution by a thermostable homologue whose secondary structure and binding to PSII remain unaltered at moderately high temperatures.
Description7 Págs., 5 Figs. This article is published under an Elsevier user license, it is protected by copyright and may be used for non-commercial purposes.
Publisher version (URL)http://dx.doi.org/10.1016/S0005-2728(02)00208-6
URIhttp://hdl.handle.net/10261/99574
DOI10.1016/S0005-2728(02)00208-6
Identifiersdoi: 10.1016/S0005-2728(02)00208-6
issn: 0005-2728
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