scholarly journals Role of Hydrogen Bonding in Photoinduced Electron–Proton Transfer from Phenols to a Polypyridine Ru Complex with a Proton-Accepting Ligand

2017 ◽  
Vol 8 (17) ◽  
pp. 4043-4048 ◽  
Author(s):  
Sergei V. Lymar ◽  
Mehmed Z. Ertem ◽  
Anna Lewandowska-Andralojc ◽  
Dmitry E. Polyansky
Keyword(s):  
Hydrogen Bonding ◽  
Proton Transfer ◽  
Ru Complex ◽  
Electron Proton Transfer

scholarly journals Hydrogen bonding between hydroxylic donors and MLCT-excited Ru(bpy)2(bpz)2+ complex: implications for photoinduced electron–proton transfer

2019 ◽  
Vol 55 (42) ◽  
pp. 5870-5873 ◽  
Author(s):  
Sergei V. Lymar ◽  
Gerald F. Manbeck ◽  
Dmitry E. Polyansky
Keyword(s):  
Free Energy ◽  
Hydrogen Bonding ◽  
Proton Transfer ◽  
Energy Correlation ◽  
Electron Proton Transfer

Rates of electron–proton transfer within the H-bonded exciplexes are evaluated using the free energy correlation with donor's H-bonding acidity.

scholarly journals Visualizing the protons in a metalloenzyme electron proton transfer pathway

2020 ◽  
Vol 117 (12) ◽  
pp. 6484-6490 ◽  
Author(s):  
Hanna Kwon ◽  
Jaswir Basran ◽  
Juliette M. Devos ◽  
Reynier Suardíaz ◽  
Marc W. van der Kamp ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Electron Transfer ◽  
Hydrogen Bonding ◽  
Proton Transfer ◽  
Proton Donor ◽  
Biological Processes ◽  
Proton Coupled Electron Transfer ◽  
Neutron Structure ◽  
Bona Fide ◽  
Electron Proton Transfer

In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-Å neutron crystal structure of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation.

The Role of Free Energy Change in Coupled Electron−Proton Transfer

2007 ◽  
Vol 129 (49) ◽  
pp. 15098-15099 ◽  
Author(s):  
Christine J. Fecenko ◽  
H. Holden Thorp ◽  
Thomas J. Meyer
Keyword(s):  
Free Energy ◽  
Proton Transfer ◽  
Free Energy Change ◽  
Energy Change ◽  
Electron Proton Transfer

Theoretical study of the role of hydrogen bonding and proton transfer in oxygen reduction by semiquinones

1997 ◽  
Vol 398-399 ◽  
pp. 445-449 ◽  
Author(s):  
Adam Liwo ◽  
Danuta Jeziorek ◽  
Dariusz Dyl ◽  
Tadeusz Ossowski ◽  
Lech Chmurzyński
Keyword(s):  
Hydrogen Bonding ◽  
Proton Transfer ◽  
Oxygen Reduction ◽  
Theoretical Study

scholarly journals Deciphering the incognito role of water in a light driven proton coupled electron transfer process

2018 ◽  
Vol 9 (4) ◽  
pp. 910-921 ◽  
Author(s):  
Senthil Kumar Thiyagarajan ◽  
Raghupathy Suresh ◽  
Vadivel Ramanan ◽  
Perumal Ramamurthy
Keyword(s):  
Electron Transfer ◽  
Proton Transfer ◽  
Transfer Process ◽  
Electron Transfer Process ◽  
Solvent Water ◽  
Proton Coupled Electron Transfer ◽  
Electron Proton Transfer ◽  
Role Of Solvent ◽  
Proton Transfer Process

The incognito role of solvent water as a proton transfer bridge in a multi-site electron proton transfer process was depicted.

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