TY - JOUR
T1 - Site-directed mutations of two histidine residues in the D2 protein inactivate and destabilize photosystem ii in the cyanobacterium synechocystis 6803
AU - Vermaas, Willem
AU - Williams, John G K
AU - Arntzen, Charles J.
PY - 1987/6/1
Y1 - 1987/6/1
N2 - Site-directed mutations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues of the photosystem II (PS II) D2 protein. In one mutant (tyr-197), the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did not show any low-temperature fluorescence attributable to PS II, but contained a PSII chlorophyll-protein, CP-47, in significant quantities. Another PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm, but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role of the his-197 and his-214 residues in the D2 protein, and are interpreted to support the hypothesis that the D2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous functions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with QA and Fe2+. In absence of a functional D2 protein, the PS II core complex appears to be destabilized as evidenced by loss of chlorophyll-proteins inthe mutants.
AB - Site-directed mutations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues of the photosystem II (PS II) D2 protein. In one mutant (tyr-197), the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did not show any low-temperature fluorescence attributable to PS II, but contained a PSII chlorophyll-protein, CP-47, in significant quantities. Another PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm, but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role of the his-197 and his-214 residues in the D2 protein, and are interpreted to support the hypothesis that the D2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous functions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with QA and Fe2+. In absence of a functional D2 protein, the PS II core complex appears to be destabilized as evidenced by loss of chlorophyll-proteins inthe mutants.
KW - Cyanobacteria
KW - Herbicide Binding
KW - Photosynthesis
KW - Photosystem II Proteins
KW - Site-Directed Mutagenesis
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U2 - 10.1515/znc-1987-0620
DO - 10.1515/znc-1987-0620
M3 - Article
AN - SCOPUS:84961487659
VL - 42
SP - 762
EP - 768
JO - Zeitschrift fur Naturforschung. Teil C: Biochemie, Biophysik, Biologie, Virologie
JF - Zeitschrift fur Naturforschung. Teil C: Biochemie, Biophysik, Biologie, Virologie
SN - 0939-5075
IS - 6
ER -