Replacement of Tyrosine D with Phenylalanine Affects the Normal Proton Transfer Pathways for the Reduction of P680+in Oxygen-Evolving Photosystem II Particles fromChlamydomonas

Biochemistry ◽  
2002 ◽  
Vol 41 (52) ◽  
pp. 15754-15761 ◽  
Author(s):  
C. Jeans ◽  
M. J. Schilstra ◽  
N. Ray ◽  
S. Husain ◽  
J. Minagawa ◽  
...  

FEBS Letters ◽  
1983 ◽  
Vol 156 (1) ◽  
pp. 185-188 ◽  
Author(s):  
Jenny D. Clement-Metral ◽  
Elisabeth Gantt




Biochemistry ◽  
1991 ◽  
Vol 30 (5) ◽  
pp. 1335-1341 ◽  
Author(s):  
Victoria J. DeRose ◽  
Vittal K. Yachandra ◽  
Ann E. McDermott ◽  
R. David Britt ◽  
Kenneth Sauer ◽  
...  


2021 ◽  
Vol 1862 (1) ◽  
pp. 148329
Author(s):  
Hiroshi Kuroda ◽  
Keisuke Kawashima ◽  
Kazuyo Ueda ◽  
Takuya Ikeda ◽  
Keisuke Saito ◽  
...  


2016 ◽  
Vol 69 (9) ◽  
pp. 991 ◽  
Author(s):  
Keisuke Saito ◽  
Naoki Sakashita ◽  
Hiroshi Ishikita

The proton transfer pathway for redox active tyrosine D (TyrD) in photosystem II is a hydrogen-bond network that involves D2-Arg180 and a series of water molecules. Using quantum mechanical/molecular mechanical calculations, the detailed properties of the energetics and structural geometries were investigated. The potential-energy profile of all hydrogen bonds along the proton transfer pathway indicates that the overall proton transfer from TyrD is energetically downhill. D2-Arg180 plays a key role in the proton transfer pathway, providing a driving force for proton transfer, maintaining the hydrogen-bond network structure, stabilising P680•+, and thus deprotonating TyrD-OH to TyrD-O•. A hydrophobic environment near TyrD enhances the electrostatic interactions between TyrD and redox active groups, e.g. P680 and the catalytic Mn4CaO5 cluster: the redox states of those groups are linked with the protonation state of TyrD, i.e. release of the proton from TyrD. Thus, the proton transfer pathway from TyrD may ultimately contribute to the conversion of S0 into S1 in the dark in order to stabilise the Mn4CaO5 cluster when the photocycle is interrupted in S0.



Sign in / Sign up

Export Citation Format

Share Document