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

AuthorsPueyo, José Javier ; Alfonso Lozano, Miguel ; Andrés, Carmen; Picorel Castaño, Rafael
KeywordsPhotosystem II
Heat inactivation
33-kDa protein
Manganese stabilizing protein
Oxygen evolution
Issue Date2002
CitationBiochimica et Biophysica Acta 1554: 29-35 (2002)
AbstractPhotosynthetic oxygen evolution is an extremely heat-sensitive process and incubation of spinach Photosystem II (PSII) membranes at 40ºC for only several minutes leads to its complete inactivation. Substitution experiments of the spinach 33-kDa manganese stabili<ing 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 oxigen-evolving activity. The results allow us to suggest that thermalinactivation 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 sustitution by a thermostable homologue whose secondary structure and binding to PSII remain ulatered at moderately hight temperature.
Description7 pages, figures, and tables statistics.
Appears in Collections:(IRN) Artículos
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