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.
Groff
Dan
D
Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Thielges
Megan C
MC
Cellitti
Susan
S
Schultz
Peter G
PG
Romesberg
Floyd E
FE
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