The role of TyrD in the electron transfer kinetics in Photosystem II.
Redox-active tyrosine (Tyr) D is indirectly involved in controlling the primary electron transfer in PSII. The presence of the oxidized TyrD renders P680+ more oxidizing by localizing the charge more on PD1 and thus facilitates trapping of the excitation energy in PSII. We also conclude that the mechanism of the primary charge separation and stabilization is altered upon QA reduction.
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, 45470 Mülheim a.d. Ruhr, Germany.
Malwina
M
Szczepaniak
Miwa
M
Sugiura
Alfred R
AR
Holzwarth
D002734:Chlorophyll / Q000737:chemistry; D000077194:Chlorophyll A; D000458:Cyanobacteria / Q000378:metabolism*; D004579:Electron Transport; D005453:Fluorescence; D007700:Kinetics; D008958:Models, Molecular; D050505:Mutant Proteins / Q000737:chemistry; D010084:Oxidation-Reduction; D045332:Photosystem II Protein Complex / Q000737:chemistry*; D013816:Thermodynamics; D013997:Time Factors; D014443:Tyrosine / Q000378:metabolism*
D050505:Mutant Proteins; D045332:Photosystem II Protein Complex; D002734:Chlorophyll; D014443:Tyrosine; D000077194:Chlorophyll A