Fast oxygen‐independent degradation of the DI reaction center protein in photosystem II
暂无分享,去创建一个
[1] S. Styring,et al. Photosystem II: Molecular Organization, Function, and Acclimation , 1991 .
[2] E. Aro,et al. In vitro studies on light-induced inhibition of Photosystem II and D1-protein degradation at low temperatures , 1990 .
[3] B. Andersson,et al. Light‐induced D1‐protein degradation in isolated photosystem II core complexes , 1990, FEBS letters.
[4] E. Aro,et al. Restoration of light induced photosystem II inhibition without de novo protein synthesis , 1990, FEBS letters.
[5] C. Jegerschöld,et al. Light-dependent degradation of the D1 protein in photosystem II is accelerated after inhibition of the water splitting reaction. , 1990, Biochemistry.
[6] S. Styring,et al. Changes in the organization of photosystem II following light-induced D1-protein degradation. , 1990 .
[7] J. Barber,et al. Spectral resolution of more than one chlorophyll electron donor in the isolated Photosystem II reaction centre complex , 1990 .
[8] G. Cheniae,et al. Kinetics of photoinhibition in hydroxylamine-extracted photosystem II membranes: relevance to photoactivation and sites of electron donation. , 1990, Biochemistry.
[9] M. Edelman,et al. Free Radical Scavengers Inhibit Light-Dependent Degradation of the 32 kDa Photosystem II Reaction Center Protein , 1990 .
[10] N. Adir,et al. Mechanism of photoinhibition in vivo. A reversible light-induced conformational change of reaction center II is related to an irreversible modification of the D1 protein. , 1990, The Journal of biological chemistry.
[11] S. Styring,et al. Strong light photoinhibition of electrontransport in Photosystem II. Impairment of the function of the first quinone acceptor, QA , 1990 .
[12] A. Rutherford,et al. The influence of the quinone-iron electron acceptor complex on the reaction centre photochemistry of Photosystem II , 1989 .
[13] M. Edelman,et al. Separate photosensitizers mediate degradation of the 32-kDa photosystem II reaction center protein in the visible and UV spectral regions. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[14] A. Rutherford. Photosystem II, the water-splitting enzyme. , 1989, Trends in biochemical sciences.
[15] D. Klug,et al. Resolution of a long lived fluorescence component from D1/D2/ cytochrome b‐559 reaction centres , 1989 .
[16] M. Edelman,et al. Dynamics of the photosystem II reaction center , 1989, Cell.
[17] G. Brudvig,et al. Cytochrome b-559 may function to protect photosystem II from photoinhibition. , 1988, Biochemistry.
[18] S. Styring,et al. Photosystem II disorganization and manganese release after photoinhibition of isolated spinach thylakoid membranes , 1988 .
[19] D. Kirilovsky,et al. Reversible and irreversible photoinhibition in herbicide-resistant mutants of Synechocystis 6714 , 1988 .
[20] K. Satoh,et al. Primary radical pair in the Photosystem II reaction centre , 1987 .
[21] 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.
[22] F. Callahan,et al. Studies on the Photoactivation of the Water-Oxidizing Enzyme: II. Characterization of Weak Light Photoinhibition of PSII and Its Light-Induced Recovery. , 1986, Plant physiology.
[23] A. Trebst. The Topology of the Plastoquinone and Herbicide Binding Peptides of Photosystem II in the Thylakoid Membrane , 1986 .
[24] A. Trebst,et al. On the role of the QB protein of PS II in photoinhibition , 1986 .
[25] I. Ohad,et al. Light‐dependent degradation of the QB‐protein in isolated pea thylakoids , 1985, The EMBO journal.
[26] 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.
[27] M. Edelman,et al. Regulation of protein metabolism: Coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membranes. , 1984, Proceedings of the National Academy of Sciences of the United States of America.