Journal
BIOELECTROCHEMISTRY
Volume 70, Issue 1, Pages 33-38Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2006.03.020
Keywords
Photosystem II; fluorescence quenching; protein aggregation; dynamic light scattering
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In this work the effect of temperature and n-dodecyl-beta-D-maltoside (DM) on PSII complexes organization was investigated. An aggregation process of PSII monomers and dimers was documented at different temperatures and low DM concentration by steady-state fluorescence, absorption, circular dichroism, Rayleigh and dynamic light-scattering experiments. Measures of oxygen evolution enabled us to estimate the change in photoactivity of PSII during the aggregation. This process was found to be extensively reversed by increasing DM concentration as proved by means of steady-state fluorescence and dynamic light-scattering experiments. (c) 2006 Elsevier B.V. All rights reserved.
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