Short Hydrogen Bond between Redox-Active Tyrosine YZand D1-His190 in the Photosystem II Crystal Structure

Biochemistry ◽  
2011 ◽  
Vol 50 (45) ◽  
pp. 9836-9844 ◽  
Author(s):  
Keisuke Saito ◽  
Jian-Ren Shen ◽  
Toyokazu Ishida ◽  
Hiroshi Ishikita
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bond ◽  
Photosystem Ii ◽  
Redox Active ◽  
Short Hydrogen Bond

Electronic spectra, ESR and crystal structure of tetrahedral halocuprates(II). The existence of cations (2tbpo·H+) with a very short hydrogen bond

1983 ◽  
Vol 72 ◽  
pp. 127-131 ◽  
Author(s):  
Antonio Carlos Massabni ◽  
Otaciro Rangel Nascimento ◽  
Regina Helena De Almeida Santos ◽  
Regina Helena Porto Francisco ◽  
Johannes Rüdiger Lechat
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bond ◽  
Electronic Spectra ◽  
Short Hydrogen Bond

Pivotal role of the redox-active tyrosine in driving the water splitting catalyzed by photosystem II

2020 ◽  
Vol 22 (1) ◽  
pp. 273-285 ◽  
Author(s):  
Shin Nakamura ◽  
Matteo Capone ◽  
Daniele Narzi ◽  
Leonardo Guidoni
Keyword(s):  
Hydrogen Bond ◽  
Photosystem Ii ◽  
Water Splitting ◽  
Oxidation State ◽  
Water Oxidation ◽  
Oxidation Catalysis ◽  
Pivotal Role ◽  
Redox Active ◽  
Water Oxidation Catalysis

TyrZ oxidation state triggers hydrogen bond modification in the water oxidation catalysis.

scholarly journals Energetics of the Proton Transfer Pathway for Tyrosine D in Photosystem II

2016 ◽  
Vol 69 (9) ◽  
pp. 991 ◽  
Author(s):  
Keisuke Saito ◽  
Naoki Sakashita ◽  
Hiroshi Ishikita
Keyword(s):  
Hydrogen Bond ◽  
Photosystem Ii ◽  
Proton Transfer ◽  
Electrostatic Interactions ◽  
Water Molecules ◽  
Hydrogen Bond Network ◽  
Redox States ◽  
Redox Active ◽  
Bond Network ◽  
Tyrosine D

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.

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