Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase.
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ABSTRACT:
SUBMITTER: Groff D
PROVIDER: S-EPMC3166254 | biostudies-literature | 2009
REPOSITORIES: biostudies-literature
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Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase.
Groff Dan D Thielges Megan C MC Cellitti Susan S Schultz Peter G PG Romesberg Floyd E FE
Angewandte Chemie (International ed. in English) 20090101 19
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. ...[more]
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