Groff, Dan, Thielges, Megan C, Cellitti, Susan, Schultz, Peter and Romesberg, Floyd E (2009) Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase. Angewandte Chemie (International ed. in English), 48 (19). pp. 3478-3481. ISSN 1521-3773

Abstract

State secrets: Site-specific deuteration and FTIR studies reveal that Tyr100 in dihydrofolate reductase plays an important role in catalysis, with a strong electrostatic coupling occurring between Tyr100 and the charge that develops in the hydride-transfer transition state (see picture, NADP(+) purple, Tyr100 green). However, relaying correlated motions that facilitate catalysis from distal sites of the protein to the hydride donor may also be involved.

Item Type:	Article
Related URLs:	http://www.ncbi.nlm.nih.gov/sites/entrez...
Additional Information:	archiving not allowed on institutional repository
Keywords:	deuterium; dihydrofolate reductase; nzyme catalysis; IR spectroscopy; noncovalent interactions
Related URLs:	http://www.ncbi.nlm.nih.gov/sites/entrez...
Date Deposited:	14 Dec 2009 13:49
Last Modified:	31 Jan 2013 00:57
URI:	https://oak.novartis.com/id/eprint/1207