http://www.cnr.it/ontology/cnr/individuo/prodotto/ID22641
A spectroscopic study of the wavelength-dependent photoisomerizations of bilirubins bound to human serum albumin (Articolo in rivista)
- Type
- Label
- A spectroscopic study of the wavelength-dependent photoisomerizations of bilirubins bound to human serum albumin (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1088/1464-4258/7/12/006 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Marina Mazzoni; Giovanni Agati; Riccardo Pratesi; Maurizio Persico (literal)
- Pagina inizio
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- http://dx.doi.org/ (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Fisica Applicata 'Nello Carrara' del Consiglio Nazionale delle Ricerche,
Via Madonna del Piano, I-50019 Sesto Fiorentino, Italy.
Dipartimento di Fisica, Università di Firenze, via G Sansone 1, I-50019 Sesto Fiorentino,
Italy.
Dipartimento di Chimica e Chimica Industriale, Università di Pisa, via Risorgimento 35,
I-56126 Pisa, Italy. (literal)
- Titolo
- A spectroscopic study of the wavelength-dependent photoisomerizations of bilirubins bound to human serum albumin (literal)
- Abstract
- The wavelength-dependent photoisomerizations of the asymmetric bilirubin
BR-IX? and of the symmetric bilirubin-III? (BR-III) and
mesobilirubin-XIII? (MBR-XIII) bound to human serum albumin (HSA) in
aqueous solution were analysed with the help of an exciton coupling model.
The modelling was based on the absorption and circular dichroism (CD)
spectra (bisignate Cotton effect). Time-dependent density functional theory
(TD-DFT) of the free BR-IX molecule suggested the presence of two main
bands of exciton coupling character in the blue region of the spectrum, and
other weaker bands of charge transfer character at longer wavelengths.
These peculiarities were taken into account to fit the photoisomerization
quantum yields in the blue-green region as functions of the wavelength,
obtaining the bandshape of the exciton coupling bands from the experimental
CD spectra. The other excitons were extracted from the decomposition of
the band resulting from the difference between the absorption spectrum and
the sum (normalized-to-absorption) of the two CD excitons. We expressed
photoisomerization quantum yields in terms of the sum of the contributions
to photon absorption deriving from all the exciton states normalized to total
absorption. For all the reversible photoprocesses of bilirubins and for the
irreversible one of BR-IX? in HSA (i.e. lumirubin formation), we give
reliable mean values of the individual state excitation probabilities and
photoisomerization efficiencies in the pigment-protein complex. (literal)
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