Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 6(105), p. 1844-1848, 2008

DOI: 10.1073/pnas.0711659105

Links

Tools

Export citation

Search in Google Scholar

Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase

Journal article published in 2008 by Matthew P. Blakeley, Federico Ruiz ORCID, Raul Cachau, Isabelle Hazemann, Flora Meilleur ORCID, Andre Mitschler, Stephan Ginell, Pavel Afonine, Oscar N. Ventura, Alexandra Cousido-Siah, Michael Haertlein, Andrzej Joachimiak, Dean Myles, Alberto Podjarny
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Red circle
Preprint: archiving forbidden
Green circle
Postprint: archiving allowed
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

We present results of combined studies of the enzyme human aldose reductase (h-AR, 36 kDa) using single-crystal x-ray data (0.66 Å, 100K; 0.80 Å, 15K; 1.75 Å, 293K), neutron Laue data (2.2 Å, 293K), and quantum mechanical modeling. These complementary techniques unveil the internal organization and mobility of the hydrogen bond network that defines the properties of the catalytic engine, explaining how this promiscuous enzyme overcomes the simultaneous requirements of efficiency and promiscuity offering a general mechanistic view for this class of enzymes.