Pulsed EPR Studies of Doublet Signal and Singlet-like Signal in Oriented Ca2+-Depleted PS II Membranes:  Location of the Doublet Signal Center in PS II†

Biochemistry ◽  
2000 ◽  
Vol 39 (36) ◽  
pp. 11034-11040 ◽  
Author(s):  
Hiroyuki Mino ◽  
Asako Kawamori ◽  
Taka-aki Ono
Keyword(s):  
Ps Ii ◽  
1999 ◽  
Vol 39 (supplement) ◽  
pp. S82
Author(s):  
H. Mino ◽  
A. Kawamori ◽  
T. Ono
Keyword(s):  
Ps Ii ◽  

1982 ◽  
Vol 37 (3-4) ◽  
pp. 256-259 ◽  
Author(s):  
F. Schuler ◽  
P. Brandt ◽  
W. Wießner

Abstract An improved method for isolation of (photosystem II)-particles from Euglena gracilis, strain Z was established. PS II-particles isolated by ultrasonic treatment and following differential centrifugation show fluorescence emission and absorption spectra identical with in vivo properties of Euglena gracilis. These PS II-particles have only PS II-activity and contain CP a, the typical chlorophyll-protein-complex of PS II. No contamination of PS I-components are detectable.


2010 ◽  
Vol 98 (3) ◽  
pp. 232a
Author(s):  
You Zhou ◽  
Daniel J. Mayo ◽  
Robert M. McCarrick ◽  
Gary A. Lorigan
Keyword(s):  

1993 ◽  
Vol 48 (3-4) ◽  
pp. 163-167
Author(s):  
Koichi Yoneyama ◽  
Yoshihiro Nakajima ◽  
Masaru Ogasawara ◽  
Hitoshi Kuramochi ◽  
Makoto Konnai ◽  
...  

Abstract Through the studies on structure-activity relationships of 5-acyl-3-(1-aminoalkylidene)-4-hydroxy-2 H-pyran-2,6(3 H)-dione derivatives in photosystem II (PS II) inhibition, overall lipophilicity of the molecule was found to be a major determinant for the activity. In the substituted N -benzyl derivatives, not only the lipophilicity but also the electronic and steric characters of the substituents greatly affected the activity. Their mode of PS II inhibition seemed to be similar to that of DCMU , whereas pyran-enamine derivatives needed to be highly lipophilic to block the electron transport in thylakoid membranes, which in turn diminished the permeability through biomembranes.


1994 ◽  
Vol 105 (2) ◽  
pp. 113-119 ◽  
Author(s):  
A.V. Astashkin ◽  
Y. Kodera ◽  
A. Kawamori
Keyword(s):  

1993 ◽  
Vol 48 (3-4) ◽  
pp. 234-240 ◽  
Author(s):  
G. Renger ◽  
H. M. Gleiter ◽  
E. Haag ◽  
F. Reifarth

Studies on thermodynamics and kinetics of electron transfer from QA- to QB(QB-) were performed by monitoring laser flash induced changes of the relative fluorescence emission as a function of temperature (220 K < T < 310 K) in isolated thylakoids and PS II membrane fragments.In addition, effects of bivalent metal ions on PS II were investigated by measuring conventional fluorescence induction curves, oxygen evolution, manganese content and atrazine binding mostly in PS II membrane fragments. It was found: a) the normalized level of the fluorescence remaining 10 s after the actinic flash (Ft/F0) steeply increases at temperatures below -10 to - 20 °C, b) the fast phase of the transient fluorescence change becomes markedly retarded with decreasing temperatures, c) among different cations (Cu2+, Zn2+, Cd2+, Ni2+, Co2+) only Cu2+ exhibits marked effects in the concentration range below 100 μᴍ and d) Cu2+ decreases the normalized variable fluorescence, inhibits oxygen evolution and diminishes the affinity to atrazine binding without affecting the number of binding sites. The content of about four manganeses per functionally competent oxygen evolving complex is not changed by [Cu2+] < 70 μᴍ.Based on these findings it is concluded: i) a temperature dependent equilibrium between an inactive (I) and active (A) state of QA- reoxidation by QB(QB- ) is characterized by standard enthalpies ΔH° of 95 kJ mol-1 and 60 kJ mol-1 and standard entropies ΔS° of 370 kJ K-1 mol-1 and 240 kJ K-1 mol-1 in isolated thylakoids and PS II membrane fragments, respectively, ii) the activation energies of QA- reoxidation by plastoquinone bound to the QB site are about 30 kJ mol-1 (thylakoids) and 40 kJ mol-1 (PS II membrane fragments) in 220 K < T < 300 K, and iii) Cu2+ causes at least a two-fold effect on PS II by modifying the atrazine binding affinity at lower concentrations ( ~ 5 μᴍ) and interference with the redox active tyrosine Yz at slightly higher concentration ( ~ 10 μᴍ) leading to blockage of oxygen evolution.


2001 ◽  
Vol 153 (2) ◽  
pp. 178-185 ◽  
Author(s):  
Nikolai I. Avdievich ◽  
Gary J. Gerfen

Sign in / Sign up

Export Citation Format

Share Document