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Título: | 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 |
Autor: | Pueyo, José Javier CSIC ORCID ; Alfonso Lozano, Miguel CSIC ORCID ; Andrés Plou, Carmen; Picorel Castaño, Rafael CSIC ORCID | Palabras clave: | Oxygen evolution 33-kDa protein Photosystem II Heat inactivation Manganese stabilizing protein |
Fecha de publicación: | abr-2002 | Editor: | Elsevier | Citación: | Pueyo 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) | Resumen: | Photosynthetic 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. | Descripción: | 7 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. | Versión del editor: | http://dx.doi.org/10.1016/S0005-2728(02)00208-6 | URI: | http://hdl.handle.net/10261/99574 | DOI: | 10.1016/S0005-2728(02)00208-6 | Identificadores: | doi: 10.1016/S0005-2728(02)00208-6 issn: 0005-2728 |
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