Reconstitution of the peridinin-chlorophyll a protein (PCP): evidence for functional flexibility in chlorophyll binding.
Photosynth Res
; 86(1-2): 229-40, 2005 Nov.
Article
em En
| MEDLINE
| ID: mdl-16172941
ABSTRACT
The coding regions for the N-domain, and full length peridinin-chlorophyll a apoprotein (full length PCP), were expressed in Escherichia coli. The apoproteins formed inclusion bodies from which the peptides could be released by hot buffer. Both the above constructs were reconstituted by addition of a total pigment extract from native PCP. After purification by ion exchange chromatography, the absorbance, fluorescence excitation and CD spectra resembled those of the native PCP. Energy transfer from peridinin to Chl a was restored and a specific fluorescence activity calculated which was approximately 86% of that of native PCP. Size exclusion analysis and CD spectra showed that the N-domain PCP dimerized on reconstitution. Chl a could be replaced by Chl b, 3-acetyl Chl a, Chl d and Bchl using the N-domain apo protein. The specific fluorescence activity was the same for constructs with Chl a, 3-acetyl Chl a, and Chl d but significantly reduced for those made with Chl b. Reconstitutions with mixtures of chlorophylls were also made with eg Chl b and Chl d and energy transfer from the higher energy Qy band to the lower was demonstrated.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Carotenoides
/
Proteínas de Protozoários
/
Clorofila
Idioma:
En
Revista:
Photosynth Res
Assunto da revista:
METABOLISMO
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Austrália