Composition and function of cytochrome b559 in reaction centers of photosystem II of green plants

1994 ◽  
Vol 26 (6) ◽  
pp. 619-626 ◽  
Author(s):  
Vladimir A. Shuvalov
Keyword(s):  
Photosystem Ii ◽  
Reaction Centers ◽  
Cytochrome B559 ◽  
Green Plants ◽  
And Function

Energy Transfer and Trapping in Isolated Photosystem II Reaction Centers of Green Plants at Low Temperature. A Study by Spectral Hole Burning

1996 ◽  
Vol 100 (27) ◽  
pp. 11488-11495 ◽  
Author(s):  
M. L. Groot ◽  
J. P. Dekker ◽  
R. van Grondelle ◽  
F. T. H. den Hartog ◽  
S. Völker
Keyword(s):  
Energy Transfer ◽  
Low Temperature ◽  
Photosystem Ii ◽  
Reaction Centers ◽  
Hole Burning ◽  
Spectral Hole Burning ◽  
Green Plants ◽  
Spectral Hole

Light stress provokes plastic and elastic modifications in structure and function of photosystem II in camellia leaves

1997 ◽  
Vol 101 (2) ◽  
pp. 265-277 ◽  
Author(s):  
Gert H. J. Kruger ◽  
Merope Tsimilli-Michael ◽  
Reto J. Strasser
Keyword(s):  
Photosystem Ii ◽  
Light Stress ◽  
Structure And Function ◽  
And Function

Mechanism of photoinduced electron transfer in photosystem II reaction centers

BIOPHYSICS ◽  
2007 ◽  
Vol 52 (1) ◽  
pp. 40-45 ◽  
Author(s):  
I. B. Klenina ◽  
W. O. Feikema ◽  
P. Gast ◽  
M. G. Zvereva ◽  
I. I. Proskuryakov
Keyword(s):  
Electron Transfer ◽  
Photosystem Ii ◽  
Photoinduced Electron Transfer ◽  
Reaction Centers

scholarly journals Mass spectrometry-based cross-linking study shows that the Psb28 protein binds to cytochrome b559 in Photosystem II

2017 ◽  
Vol 114 (9) ◽  
pp. 2224-2229 ◽  
Author(s):  
Daniel A. Weisz ◽  
Haijun Liu ◽  
Hao Zhang ◽  
Sundarapandian Thangapandian ◽  
Emad Tajkhorshid ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Photosystem Ii ◽  
Protein Interactions ◽  
Protein Complexes ◽  
Protein Docking ◽  
Cross Linking ◽  
Protein Protein Interactions ◽  
Cytochrome B559 ◽  
Reaction Center Complex ◽  
Assembly Intermediate

Photosystem II (PSII), a large pigment protein complex, undergoes rapid turnover under natural conditions. During assembly of PSII, oxidative damage to vulnerable assembly intermediate complexes must be prevented. Psb28, the only cytoplasmic extrinsic protein in PSII, protects the RC47 assembly intermediate of PSII and assists its efficient conversion into functional PSII. Its role is particularly important under stress conditions when PSII damage occurs frequently. Psb28 is not found, however, in any PSII crystal structure, and its structural location has remained unknown. In this study, we used chemical cross-linking combined with mass spectrometry to capture the transient interaction of Psb28 with PSII. We detected three cross-links between Psb28 and the α- and β-subunits of cytochrome b559, an essential component of the PSII reaction-center complex. These distance restraints enable us to position Psb28 on the cytosolic surface of PSII directly above cytochrome b559, in close proximity to the QB site. Protein–protein docking results also support Psb28 binding in this region. Determination of the Psb28 binding site and other biochemical evidence allow us to propose a mechanism by which Psb28 exerts its protective effect on the RC47 intermediate. This study also shows that isotope-encoded cross-linking with the “mass tags” selection criteria allows confident identification of more cross-linked peptides in PSII than has been previously reported. This approach thus holds promise to identify other transient protein–protein interactions in membrane protein complexes.

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