Electron transfer in photosystem II at cryogenic temperatures

Biochemistry ◽  
1985 ◽  
Vol 24 (27) ◽  
pp. 8114-8120 ◽  
Author(s):  
Julio C. De Paula ◽  
Jennifer B. Innes ◽  
Gary W. Brudvig
2008 ◽  
Vol 1777 (9) ◽  
pp. 1109-1115 ◽  
Author(s):  
Han Bao ◽  
Chunxi Zhang ◽  
Keisuke Kawakami ◽  
Yanan Ren ◽  
Jian-Ren Shen ◽  
...  

BIOPHYSICS ◽  
2007 ◽  
Vol 52 (1) ◽  
pp. 40-45 ◽  
Author(s):  
I. B. Klenina ◽  
W. O. Feikema ◽  
P. Gast ◽  
M. G. Zvereva ◽  
I. I. Proskuryakov

Biochemistry ◽  
1990 ◽  
Vol 29 (38) ◽  
pp. 8977-8985 ◽  
Author(s):  
Carolyn A. Buser ◽  
Lynmarie K. Thompson ◽  
Bruce A. Diner ◽  
Gary W. Brudvig

2007 ◽  
Vol 111 (43) ◽  
pp. 12599-12604 ◽  
Author(s):  
David L. Jenson ◽  
Amaris Evans ◽  
Bridgette A. Barry

Author(s):  
Jörg Pieper ◽  
Leonid Rusevich ◽  
Thomas Hauß ◽  
Gernot Renger

AbstractThe effect of dehydration on the lamellar spacing of photosystem II (PS II) membrane fragments from spinach has been investigated using neutron membrane diffraction at room temperature. The diffraction data reveal a major peak at a scattering vector Q of 0.049 Å−1 at a relative humidity (r.h.) of 90% corresponding to a repeat distance D of about 129 Å. Upon dehydration to 44% r.h., this peak shifts to about 0.060 Å−1 corresponding to a distance of 104.7±2.5 Å. Within experimental error, the latter repeat distance remains almost the same at hydration levels below 44% r.h. indicating that most of the hydration water is removed. This result is consistent with the earlier finding that hydration-induced conformational protein motions in PS II membrane fragments are observed above 44% r.h. and correlated with the onset electron transfer in PS II (Pieper et al. 2008, Eur. Biophys. J. 37: 657–663).


2021 ◽  
pp. 3-38
Author(s):  
Jian-Ren Shen ◽  
Yoshiki Nakajima ◽  
Fusamichi Akita ◽  
Michihiro Suga

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