scholarly journals Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements

2016 ◽  
Vol 56 (9-10) ◽  
pp. 841-851 ◽  
Author(s):  
Roman Davydov ◽  
Nimesh Khadka ◽  
Zhi-Yong Yang ◽  
Andrew J. Fielding ◽  
Dmitriy Lukoyanov ◽  
...  
Keyword(s):  
Proton Transfer ◽  
Conformational Changes ◽  
Mofe Protein ◽  
Femo Cofactor ◽  
Epr Measurements ◽  
Electron Proton Transfer

scholarly journals Comment on “Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase”

Science ◽  
2021 ◽  
Vol 371 (6530) ◽  
pp. eabe5481 ◽  
Author(s):  
John W. Peters ◽  
Oliver Einsle ◽  
Dennis R. Dean ◽  
Serena DeBeer ◽  
Brian M. Hoffman ◽  
...  
Keyword(s):  
Active Site ◽  
Biochemical Evidence ◽  
Mofe Protein ◽  
Femo Cofactor

Kang et al. (Reports, 19 June 2020, p. 1381) report a structure of the nitrogenase MoFe protein that is interpreted to indicate binding of N2 or an N2-derived species to the active-site FeMo cofactor. Independent refinement of the structure and consideration of biochemical evidence do not support this claim.

scholarly journals Base-enhanced catalytic water oxidation by a carboxylate–bipyridine Ru(II) complex

2015 ◽  
Vol 112 (16) ◽  
pp. 4935-4940 ◽  
Author(s):  
Na Song ◽  
Javier J. Concepcion ◽  
Robert A. Binstead ◽  
Jennifer A. Rudd ◽  
Aaron K. Vannucci ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Proton Transfer ◽  
Water Oxidation ◽  
Proton Acceptor ◽  
Half Time ◽  
X Ray ◽  
X Ray Crystallography ◽  
Buffer Base ◽  
Electron Proton Transfer ◽  
C Nmr

In aqueous solution above pH 2.4 with 4% (vol/vol) CH3CN, the complex [RuII(bda)(isoq)2] (bda is 2,2′-bipyridine-6,6′-dicarboxylate; isoq is isoquinoline) exists as the open-arm chelate, [RuII(CO2-bpy-CO2−)(isoq)2(NCCH3)], as shown by 1H and 13C-NMR, X-ray crystallography, and pH titrations. Rates of water oxidation with the open-arm chelate are remarkably enhanced by added proton acceptor bases, as measured by cyclic voltammetry (CV). In 1.0 M PO43–, the calculated half-time for water oxidation is ∼7 μs. The key to the rate accelerations with added bases is direct involvement of the buffer base in either atom–proton transfer (APT) or concerted electron–proton transfer (EPT) pathways.

scholarly journals Solvent-dependent transition from concerted electron–proton to proton transfer in photoinduced reactions between phenols and polypyridine Ru complexes with proton-accepting sites

2018 ◽  
Vol 47 (44) ◽  
pp. 15917-15928 ◽  
Author(s):  
Sergei V. Lymar ◽  
Mehmed Z. Ertem ◽  
Dmitry E. Polyansky
Keyword(s):  
Proton Transfer ◽  
Polar Solvent ◽  
Ru Complexes ◽  
Photoinduced Reactions ◽  
Electron Proton Transfer

Transition from photo-induced concerted electron–proton transfer to a proton transfer is enhanced in more polar solvent.

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.

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