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TSPP exhibited a complex pattern of aggregation on varying the RM size and pH in the absence of the protein: at low <jats:italic>\u03c9<\/jats:italic><jats:sub>0<\/jats:sub> (the ratio of water concentration to AOT concentration, the emission of H\u2010aggregates prevails under acidic or neutral \u201cpH<jats:sub>ext<\/jats:sub>\u201d conditions. Upon formation of the water\u2010pool, J\u2010aggregates and monomeric diacid species dominate at low \u201cpH<jats:sub>ext<\/jats:sub>\u201d but only monomer is detected at neutral \u201cpH<jats:sub>ext<\/jats:sub>\u201d. The aggregation number increases with <jats:italic>\u03c9<\/jats:italic><jats:sub>0<\/jats:sub> and the presence of the protein does not seem to contribute to further growth of the aggregate. The presence of protein leads to H\u2010deaggregation but promotes J\u2010aggregation up to a certain protein\/porphyrin ratio above which, complexation with the monomer bound to a hydrophobic site of the protein prevails. The effective complex binding constants are smaller than in free aqueous solution; this indicates a weaker binding in these RM probably due to some conformational changes imposed by encapsulation. Only a weak quenching of TMpyP fluorescence is detected due to the presence of protein in contrast to the negative porphyrin.<\/jats:p>","DOI":"10.1002\/chem.200500047","type":"journal-article","created":{"date-parts":[[2005,10,26]],"date-time":"2005-10-26T03:46:34Z","timestamp":1130298394000},"page":"1046-1057","source":"Crossref","is-referenced-by-count":45,"title":["Spectroscopic Studies of Water\u2010Soluble Porphyrins with Protein Encapsulated in Bis(2\u2010ethylhexyl)sulfosuccinate (AOT) Reverse Micelles: Aggregation versus Complexation"],"prefix":"10.1002","volume":"12","author":[{"given":"Suzana M.","family":"Andrade","sequence":"first","affiliation":[]},{"given":"S\u00edlvia M. 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