๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Recovery of photoinactivated photosystem II in leaves: retardation due to restricted mobility of photosystem II in the thylakoid membrane

โœ Scribed by Riichi Oguchi; Husen Jia; James Barber; Wah Soon Chow

Publisher
Springer
Year
2008
Tongue
English
Weight
783 KB
Volume
98
Category
Article
ISSN
0166-8595

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

NMR paramagnetic relaxation enhancements
NMR paramagnetic relaxation enhancements due to manganese in the S0and S2states of Photosystem II-enriched membrane fragments and in the detergent-solubilized Photosystem II complex
โœ Jean-Marc Bovet; Eun-Jung Park; Robert R. Sharp ๐Ÿ“‚ Article ๐Ÿ“… 1993 ๐Ÿ› Springer ๐ŸŒ English โš– 793 KB

The NMR paramagnetic relaxation enhancement (NMR-PRE) produced in the solvent proton resonance by manganese in the S o and S 2 states of the oxygen evolving center (OEC) has been recorded for three Photosystem II (PS II)-enriched preparations: (1) PS II-enriched thylakoid membrane fragments (TMF-2 p

Inhibitors of photosystem II and the top
Inhibitors of photosystem II and the topology of the herbicide and QBbinding polypeptide in the thylakoid membrane
โœ A. Trebst; W. Draber ๐Ÿ“‚ Article ๐Ÿ“… 1986 ๐Ÿ› Springer ๐ŸŒ English โš– 712 KB

The folding through the thylakoid membrane of the D-I herbicide binding polypeptide and of the homologous D-2 subunit of photosystem II is predicted from comparison of amino acid sequences and hydropathy index plots with the folding of the subunits L and M of a bacterial photosystem. As the function

Characterization of damage to the D1 pro
Characterization of damage to the D1 protein of photosystem II under photoinhibitory illumination in non-phosphorylated and phosphorylated thylakoid membranes
โœ N. Mizusawa; N. Yamamoto; M. Miyao ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 818 KB

Thylakoid membranes retaining a high capacity to phosphorylate the D 1 protein of photosystem II but free from contamination by exogenous proteases have been prepared. Almost all the DI protein in this preparation is unphosphorylated, but it is almost completely phosphorylated by illumination in the