Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase.
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.
Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Dan
D
Groff
Megan C
MC
Thielges
Susan
S
Cellitti
Peter G
PG
Schultz
Floyd E
FE
Romesberg
D002384:Catalysis; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared; D055672:Static Electricity; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry* / Q000235:genetics; D014443:Tyrosine / Q000737:chemistry* / Q000235:genetics
D014443:Tyrosine; D013762:Tetrahydrofolate Dehydrogenase