Circular dichroism of the photoreceptor pigment oxyblepharismin.
Circular dichroism (CD) was used to study the structure of oxyblepharismin (OxyBP), the photoreceptor chromophore for the photophobic response of the blue form of Blepharisma japonicum. Both the chromophore associated to its native protein and the free chromophore in ethanol solution were investigated. CD spectra in the far-UV range indicate that OxyBP induces a slight increase in the alpha-helix content of the protein matrix. CD spectra in the near-UV and visible region of the spectrum show that OxyBP adopts a chiral conformation with a preferential geometry not only when associated to its protein matrix, but also when isolated and dissolved in ethanol. This experimental result is related to the existence of a high-energy interconversion barrier between two enantiomeric structures of the molecule and discussed on the basis of an asymmetric biosynthesis of its precursor, blepharismin.
Pieroni
Osvaldo
O
Istituto di Biofisica CNR-Sezione di Pisa, 56124 Pisa, Italy. osvaldo.pieroni@pi.ibf.cnr.it
Plaza
Pascal
P
Mahet
Mathilde
M
Angelini
Nicola
N
Checcucci
Giovanni
G
Malatesta
Manuela
M
Martin
Monique M
MM
Lenci
Francesco
F
D000818:Animals; D016798:Ciliophora / Q000737:chemistry; D002942:Circular Dichroism; D015394:Molecular Structure; D010569:Perylene / Q000031:analogs & derivatives* / Q000737:chemistry / Q000145:classification; D010786:Photoreceptor Cells / Q000737:chemistry*; D020283:Photoreceptors, Microbial / Q000737:chemistry / Q000145:classification; D010860:Pigments, Biological / Q000737:chemistry / Q000145:classification; D011485:Protein Binding; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet
D020283:Photoreceptors, Microbial; D010860:Pigments, Biological; D015800:Protozoan Proteins; C505951:oxyblepharismin; D010569:Perylene