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Bioelectrochemistry ; 70(1): 33-8, 2007 Jan.
Article in English | MEDLINE | ID: mdl-16730478

ABSTRACT

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.


Subject(s)
Photosystem II Protein Complex/chemistry , Photosystem II Protein Complex/metabolism , Dimerization , Spectrum Analysis , Spinacia oleracea/chemistry , Temperature , Water/chemistry
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