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Tuning of the H‐Transfer Coordinate in Primitive versus Well‐Evolved Enzymes
Author(s) -
Yahashiri Atsushi,
Howell Elizabeth E.,
Kohen Am
Publication year - 2008
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200800067
Subject(s) - dihydrofolate reductase , acceptor , chemistry , enzyme , reaction coordinate , transfer (computing) , ideal (ethics) , stereochemistry , physics , computer science , computational chemistry , biochemistry , philosophy , quantum mechanics , epistemology , parallel computing
Born to tunnel? The nature of H‐transfer in reactions catalyzed by the primitive R67 dihydrofolate reductase is compared to that in the well‐evolved chromosomal enzyme (cDHFR). In contrast to cDHFR, R67 has a poorly optimized reaction coordinate and a non‐ideal donor–acceptor distance for H‐tunneling.