TY - JOUR
T1 - Molecular structure, localization and function of biliproteins in the chlorophyll a/d containing oxygenic photosynthetic prokaryote Acaryochloris marina
AU - Hu, Qiang
AU - Marquardt, Jürgen
AU - Iwasaki, Ikuko
AU - Miyashita, Hideaki
AU - Kurano, Norihide
AU - Mörschel, Erhard
AU - Miyachi, Shigetoh
N1 - Funding Information:
We thank Prof. R.F. Troxler (Dept. of Biochemistry, Boston University School of Medicine, Boston, MA) for a kind gift of PBP antibodies. This work was performed partially as a part of the Industrial Science and Technology Frontier Program supported by New Energy and Industrial Technology Development Organization, Japan. The financial support from the Deutsche Forschungsgemeinschaft is also gratefully acknowledged.
PY - 1999/8/4
Y1 - 1999/8/4
N2 - We investigated the localization, structure and function of the biliproteins of the oxygenic photosynthetic prokaryote Acaryochloris marina, the sole organism known to date that contains chlorophyll d as the predominant photosynthetic pigment. The biliproteins were isolated by means of sucrose gradient centrifugation, ion exchange and gel filtration chromatography. Up to six biliprotein subunits in a molecular mass range of 15.5-18.4 kDa were found that cross-reacted with antibodies raised against phycocyanin or allophycocyanin from a red alga. N-Terminal sequences of the α- and β-subunits of phycocyanin showed high homogeneity to those of cyanobacteria and red algae, but not to those of cryptomonads. As shown by electron microscopy, the native biliprotein aggregates are organized as rod-shaped structures and located on the cytoplasmic side of the thylakoid membranes predominantly in unstacked thylakoid regions. Biochemical and spectroscopic analysis revealed that they consist of four hexameric units, some of which are composed of phycocyanin alone, others of phycocyanin together with allophycocyanin. Spectroscopic analysis of isolated photosynthetic reaction center complexes demonstrated that the biliproteins are physically attached to the photosystem II complexes, transferring light energy to the photosystem II reaction center chlorophyll d with high efficiency. Copyright (C) 1999 Elsevier Science B.V.
AB - We investigated the localization, structure and function of the biliproteins of the oxygenic photosynthetic prokaryote Acaryochloris marina, the sole organism known to date that contains chlorophyll d as the predominant photosynthetic pigment. The biliproteins were isolated by means of sucrose gradient centrifugation, ion exchange and gel filtration chromatography. Up to six biliprotein subunits in a molecular mass range of 15.5-18.4 kDa were found that cross-reacted with antibodies raised against phycocyanin or allophycocyanin from a red alga. N-Terminal sequences of the α- and β-subunits of phycocyanin showed high homogeneity to those of cyanobacteria and red algae, but not to those of cryptomonads. As shown by electron microscopy, the native biliprotein aggregates are organized as rod-shaped structures and located on the cytoplasmic side of the thylakoid membranes predominantly in unstacked thylakoid regions. Biochemical and spectroscopic analysis revealed that they consist of four hexameric units, some of which are composed of phycocyanin alone, others of phycocyanin together with allophycocyanin. Spectroscopic analysis of isolated photosynthetic reaction center complexes demonstrated that the biliproteins are physically attached to the photosystem II complexes, transferring light energy to the photosystem II reaction center chlorophyll d with high efficiency. Copyright (C) 1999 Elsevier Science B.V.
KW - Acaryochloris marina
KW - Chlorophyll d
KW - Energy transfer
KW - Photosystem II-biliprotein complex
KW - Phycobiliprotein
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U2 - 10.1016/S0005-2728(99)00067-5
DO - 10.1016/S0005-2728(99)00067-5
M3 - Article
C2 - 10482787
AN - SCOPUS:0032788352
SN - 0005-2728
VL - 1412
SP - 250
EP - 261
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 3
ER -