Efforts Toward the Direct Experimental Characterization of Enzyme Microenvironments: Tyrosine100 in Dihydrofolate Reductase

✍ Scribed by Dan Groff; Megan C. Thielges; Susan Cellitti; Peter G. Schultz; Floyd E. Romesberg

• Book ID: 101566551
• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 309 KB
• Volume: 48
• Category: Article
• ISSN: 0044-8249
• DOI: 10.1002/anie.200806239

✦ Synopsis

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 occuring 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.magnified image