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Chromophore composition of the phycobiliprotein Cr-PC577 from the cryptophyte Hemiselmis pacifica.
Overkamp, Kristina E; Langklotz, Sina; Aras, Marco; Helling, Stefan; Marcus, Katrin; Bandow, Julia E; Hoef-Emden, Kerstin; Frankenberg-Dinkel, Nicole.
Affiliation
  • Overkamp KE; Physiology of Microorganisms, Faculty for Biology and Biotechnology, Ruhr University Bochum, Universitätsstraße 150, 44780, Bochum, Germany.
Photosynth Res ; 122(3): 293-304, 2014 Dec.
Article in En | MEDLINE | ID: mdl-25134685
ABSTRACT
The cryptophyte phycocyanin Cr-PC577 from Hemiselmis pacifica is a close relative of Cr-PC612 found in Hemiselmis virescens and Hemiselmis tepida. The two biliproteins differ in that Cr-PC577 lacks the major peak at around 612 nm in the absorption spectrum. Cr-PC577 was thus purified and characterized with respect to its bilin chromophore composition. Like other cryptophyte phycobiliproteins, Cr-PC577 is an (αß)(α'ß) heterodimer with phycocyanobilin (PCB) bound to the α-subunits. While one chromophore of the ß-subunit is also PCB, mass spectrometry identified an additional chromophore with a mass of 585 Da at position ß-Cys-158. This mass can be attributed to either a dihydrobiliverdin (DHBV), mesobiliverdin (MBV), or bilin584 chromophore. The doubly linked bilin at position ß-Cys-50 and ß-Cys-61 could not be identified unequivocally but shares spectral features with DHBV. We found that Cr-PC577 possesses a novel chromophore composition with at least two different chromophores bound to the ß-subunit. Overall, our data contribute to a better understanding of cryptophyte phycobiliproteins and furthermore raise the question on the biosynthetic pathway of cryptophyte chromophores.
Subject(s)

Full text: 1 Database: MEDLINE Main subject: Cryptophyta / Phycobiliproteins Language: En Year: 2014 Type: Article

Full text: 1 Database: MEDLINE Main subject: Cryptophyta / Phycobiliproteins Language: En Year: 2014 Type: Article