Substantial Deletions in the DE Loop of the Photosystem II D1 Protein Do Not Prevent its Turnover or Cross-linking with the α-subunit of Cytochrome b559. A Study Using Synechocystis sp. PCC 6803 Mutants
暂无分享,去创建一个
J. Barber | E. Aro | D. Carbonera | P. Mulo | R. Barbato | P. Mäenpää | E. Bergo | Giorgio M. Gracometti
[1] E. Aro,et al. Stepwise photoinhibition of photosystem II. Studies with Synechocystis species PCC 6803 mutants with a modified D-E loop of the reaction center polypeptide D1. , 1998, Plant physiology.
[2] G. Friso,et al. Reduced turnover of the D1 polypeptide and photoactivation of electron transfer in novel herbicide resistant mutants of Synechocystis sp. PCC 6803. , 1997, European journal of biochemistry.
[3] M. Ikeuchi,et al. Selective and specific cleavage of the D1 and D2 proteins of Photosystem II by exposure to singlet oxygen: factors responsible for the susceptibility to cleavage of the proteins , 1996 .
[4] A. Trebst,et al. Cycloheximide retards high light driven D1 protein degradation in Chlamydomonas reinhardtii , 1996 .
[5] G. Giacometti,et al. Pigment-protein complexes from the photosynthetic membrane of the cyanobacterium Synechocystis sp. PCC 6803. , 1995, European journal of biochemistry.
[6] G. Friso,et al. Characterization of the Light-induced Cross-linking of the α-Subunit of Cytochrome b559 and the D1 Protein in Isolated Photosystem II Reaction Centers (*) , 1995, The Journal of Biological Chemistry.
[7] M. Ikeuchi,et al. Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: implications for the mechanism of degradation of the D1 protein under illumination. , 1995, Biochemistry.
[8] B. Diner,et al. Deletion of the PEST-like Region of Photosystem Two Modifies the QB-binding Pocket but Does Not Prevent Rapid Turnover of D1 (*) , 1995, The Journal of Biological Chemistry.
[9] C. Francke,et al. Destructive role of singlet oxygen during aerobic illumination of the Photosystem II core complex , 1994 .
[10] D. Carbonera,et al. A well resolved ODMR triplet minus singlet spectrum of P680 from PSII particles , 1994, FEBS letters.
[11] E. Aro,et al. Photoinhibition of Photosystem II. Inactivation, protein damage and turnover. , 1993, Biochimica et biophysica acta.
[12] P. Leeuwen,et al. Analysis of the optical absorbance spectra of D1-D2-cytochrome b-559 complexes by absorbance-detected magnetic resonance: Structural properties of P680 , 1992 .
[13] G. Friso,et al. Characterization of a 41 kDa photoinhibition adduct in isolated photosystem II reaction centres , 1992, FEBS letters.
[14] G. Friso,et al. Photoinduced degradation of the D1 protein in isolated thylakoids and various photosystem II particles after donor‐side inactivations Detection of a C‐terminal 16 kDa fragment , 1992, FEBS letters.
[15] I. Vass,et al. Reversible and irreversible intermediates during photoinhibition of photosystem II: stable reduced QA species promote chlorophyll triplet formation. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[16] J. Barber,et al. Too much of a good thing: light can be bad for photosynthesis. , 1992, Trends in biochemical sciences.
[17] J. Barber,et al. New evidence suggests that the initial photoinduced cleavage of the D1‐protein may not occur near the PEST sequence , 1991, FEBS letters.
[18] G. Peter,et al. Biochemical composition and organization of higher plant photosystem II light-harvesting pigment-proteins. , 1991, The Journal of biological chemistry.
[19] J. Barber,et al. Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[20] S. Styring,et al. Fast oxygen‐independent degradation of the DI reaction center protein in photosystem II , 1991, FEBS letters.
[21] E. Aro,et al. In vitro studies on light-induced inhibition of Photosystem II and D1-protein degradation at low temperatures , 1990 .
[22] B. Andersson,et al. Light‐induced D1‐protein degradation in isolated photosystem II core complexes , 1990, FEBS letters.
[23] J. Barber,et al. Determination of Catabolism of the Photosystem II D 1 Subunit by Structural Motifs in the Polypeptide Sequence , 1990, Zeitschrift fur Naturforschung. C, Journal of biosciences.
[24] M. Edelman,et al. Identification of a primary in vivo degradation product of the rapidly‐turning‐over 32 kd protein of photosystem II. , 1987, The EMBO journal.
[25] J. Barber,et al. Characterisation of a PS II reaction centre isolated from the chloroplasts of Pisum sativum , 1987 .
[26] A. Trebst. The Three-Dimensional Structure of the Herbicide Binding Niche on the Reaction Center Polypeptides of Photosystem II , 1987 .
[27] O. Nanba,et al. Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-559. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[28] S. Dunn,et al. Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on Western blots by monoclonal antibodies. , 1986, Analytical biochemistry.
[29] S. Theg,et al. Photoinactivation of chloroplasts already inhibited on the oxidizing side of Photosystem II , 1986 .
[30] I. Ohad,et al. Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[31] A. Hoff,et al. High-resolution optical absorption-difference spectra of the triplet state of the primary donor in isolated reaction centers of the photosynthetic bacteria Rhodopseudomonas sphaeroides R-26 and Rhodopseudomonas viridis measured with optically detected magnetic resonance at 1.2 K , 1982 .
[32] M. Edelman,et al. The rapidly metabolized 32,000-dalton polypeptide of the chloroplast is the "proteinaceous shield" regulating photosystem II electron transport and mediating diuron herbicide sensitivity. , 1981, Proceedings of the National Academy of Sciences of the United States of America.