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000276225 1001_ $$0P:(DE-HGF)0$$aMichalczyk, Ryszard$$b0
000276225 245__ $$aJoint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer
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000276225 520__ $$aProton transfer is a fundamental mechanism at the core of many enzyme-catalyzed reactions. It is also exquisitely sensitive to a number of factors, including pH, electrostatics, proper active-site geometry, and chemistry. Carbonic anhydrase has evolved a fast and efficient way to conduct protons through a combination of hydrophilic amino acid side chains that coordinate a highly ordered H-bonded water network. This study uses a powerful approach, combining NMR solution studies with neutron protein crystallography, to determine the effect of pH and divalent cations on key residues involved in proton transfer in human carbonic anhydrase. The results have broad implications for our understanding of proton transfer and how subtle changes in ionization and H-bonding interactions can modulate enzyme catalysis.
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000276225 7001_ $$0P:(DE-HGF)0$$aUnkefer, Clifford J.$$b1
000276225 7001_ $$0P:(DE-HGF)0$$aBacik, John-Paul$$b2
000276225 7001_ $$0P:(DE-Juel1)138266$$aSchrader, Tobias E.$$b3$$ufzj
000276225 7001_ $$0P:(DE-HGF)0$$aOstermann, Andreas$$b4
000276225 7001_ $$0P:(DE-HGF)0$$aKovalevsky, Andrey Y.$$b5
000276225 7001_ $$0P:(DE-HGF)0$$aMcKenna, Robert$$b6
000276225 7001_ $$0P:(DE-HGF)0$$aFisher, Suzanne Zoë$$b7$$eCorresponding author
000276225 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.1502255112$$gVol. 112, no. 18, p. 5673 - 5678$$n18$$p5673 - 5678$$tProceedings of the National Academy of Sciences of the United States of America$$v112$$x1091-6490$$y2015
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