Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase.
basic_science · Level V
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- Record sourced from PubMed, PMID 18250329.
- Also identified by DOI 10.1073/pnas.0711659105 and PMC identifier 2538850.
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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 A, 100K; 0.80 A, 15K; 1.75 A, 293K), neutron Laue data (2.2 A, 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.
Medical subject headings
- Aldehyde Reductase
- Quantum Theory
- X-Ray Diffraction