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RESONANCE‐ENHANCED CARS SPECTROSCOPY OF BILIPROTEINS. INFLUENCE OF AGGREGATION and LINKER PROTEINS ON CHROMOPHORE STRUCTURE IN ALLOPHYCOCYANIN (Mastigocladus laminosus)
Author(s) -
Schneider S.,
Prenzel C.J.,
Brehm G.,
Gottschalk L.,
Zhao K.H.,
Scheer H.
Publication year - 1995
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1995.tb09146.x
Subject(s) - trimer , linker , chromophore , allophycocyanin , monomer , phycocyanin , chemistry , photochemistry , crystallography , resonance raman spectroscopy , raman spectroscopy , stereochemistry , dimer , organic chemistry , cyanobacteria , polymer , physics , biology , computer science , bacteria , optics , genetics , operating system
— Resonance‐enhanced coherent anti‐Stokes Raman spectra (CARS) are reported for monomers and for trimers with and without linker proteins of allophycocyanin isolated from Mastigocladus laminosus. The CARS spectrum of the monomer is independent of the presence of linker proteins and is very similar to that of phycocyanin monomers indicating that the equivalent chromophores exhibit like structures in both biliproteins. Large differences are, however, observed between the spectra of phycocyanin trimers and those of allophycocyanin trimers with or without linker proteins (L c 8,9 ). The observed differences between monomer and trimer spectra are consistent with a change of the α‐chromophore‐protein arrangement upon aggregation without linker. If linker proteins are present in the trimer, then additional geometry changes of the β‐chromophores are induced; these could relate to a transition from the 15Z‐ anti to 15Z‐ syn conformation.