Fast oxygen‐independent degradation of the DI reaction center protein in photosystem II

[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.