Control of selectivity in allylic alcohol oxidation on gold surfaces: the role of oxygen adatoms and hydroxyl species

2015 ◽  
Vol 17 (6) ◽  
pp. 4730-4738 ◽  
Author(s):  
Gregory M. Mullen ◽  
Liang Zhang ◽  
Edward J. Evans ◽  
Ting Yan ◽  
Graeme Henkelman ◽  
...  

Gold catalysts display high activity and good selectivity for partial oxidation of a number of alcohol species.

2015 ◽  
Vol 17 (14) ◽  
pp. 9569-9569
Author(s):  
Gregory M. Mullen ◽  
Liang Zhang ◽  
Edward J. Evans ◽  
Ting Yan ◽  
Graeme Henkelman ◽  
...  

Correction for ‘Control of selectivity in allylic alcohol oxidation on gold surfaces: the role of oxygen adatoms and hydroxyl species’ by Gregory M. Mullen et al., Phys. Chem. Chem. Phys., 2015, 17, 4730–4738.


1996 ◽  
Vol 159 (2) ◽  
pp. 418-426 ◽  
Author(s):  
Dezheng Wang ◽  
Olivier Dewaele ◽  
Ann M.De Groote ◽  
Gilbert F. Froment

2017 ◽  
Vol 121 (29) ◽  
pp. 15711-15718 ◽  
Author(s):  
Yang Liu ◽  
Wangping Xu ◽  
Yueyue Shan ◽  
Hu Xu

2018 ◽  
Author(s):  
Jamie A. Macpherson ◽  
Alina Theisen ◽  
Laura Masino ◽  
Louise Fets ◽  
Paul C. Driscoll ◽  
...  

ABSTRACTAllosteric regulation is central to the role of the glycolytic enzyme pyruvate kinase M2 (PKM2) in cellular metabolism. Multiple activating and inhibitory allosteric ligands regulate PKM2 activity by controlling the equilibrium between high activity tetramers and low activity dimers and monomers. However, it remains elusive how allosteric inputs upon simultaneous binding of different ligands are integrated to regulate PKM2 activity. Here, we show that, in the presence of the allosteric inhibitor L-phenylalanine (Phe), the activator fructose 1,6-bisphosphate (FBP) can induce PKM2 tetramerisation, but fails to maximally increase enzymatic activity. Guided by a new computational framework we developed to identify residues that mediate FBP-induced allostery, we generated two PKM2 mutants, A327S and C358A, in which activation by FBP remains intact but cannot be attenuated by Phe. Our findings demonstrate a role for residues involved in FBP-induced allostery in enabling the integration of allosteric input from Phe and reveal a mechanism that underlies the co-ordinate regulation of PKM2 activity by multiple allosteric ligands.


2016 ◽  
Vol 344 ◽  
pp. 778-783 ◽  
Author(s):  
Lu-Cun Wang ◽  
Michelle L. Personick ◽  
Stavros Karakalos ◽  
Rebecca Fushimi ◽  
Cynthia M. Friend ◽  
...  

2010 ◽  
Vol 269 (1) ◽  
pp. 26-32 ◽  
Author(s):  
Yassine Azizi ◽  
Corinne Petit ◽  
Véronique Pitchon
Keyword(s):  

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