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A 30-kDa chlorophyll-a/b-binding protein was purified from photosystem II membrane fragments using Ca(2+)-chelating Sepharose 6B chromatography. The protein binds approximately four chlorophyll a molecules, one chlorophyll b molecule and carotenoids. Its 77-K fluorescence-emission spectrum exhibits a maximum at 680 +/- 1 nm. The protein has a high tendency to form a dimer in the presence of Ca2+.Ca2+ binding affects the low-temperature fluorescence-emission maximum, leading to a decrease in its intensity and a blue shift of 1 nm. Similar spectral changes were obtained in the presence of Mg2+, possibly indicating a common binding domain for both cations. We interpret these observations as cation-induced conformational changes of the protein, which were reversible upon subsequent incubation in EDTA. Evidence is presented for the involvement of carboxyl groups in the coordination sphere of the bivalent cations. The possible structural and functional role of the protein is discussed.
K D Irrgang, and
G Renger, and
J Vater
February 1986,
Plant physiology,
K D Irrgang, and
G Renger, and
J Vater
May 2005,
Microbes and infection,
K D Irrgang, and
G Renger, and
J Vater
August 1991,
Journal of immunological methods,
K D Irrgang, and
G Renger, and
J Vater
September 1965,
The Biochemical journal,
K D Irrgang, and
G Renger, and
J Vater
January 2004,
Methods in molecular biology (Clifton, N.J.),
K D Irrgang, and
G Renger, and
J Vater
June 1992,
Plant molecular biology,
K D Irrgang, and
G Renger, and
J Vater
June 1995,
Plant physiology,
K D Irrgang, and
G Renger, and
J Vater
July 1989,
Nucleic acids research,
K D Irrgang, and
G Renger, and
J Vater
February 1984,
The Journal of biological chemistry,
K D Irrgang, and
G Renger, and
J Vater
January 1989,
Journal of steroid biochemistry,
