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Solvent‐Slaved Protein Motions Accompany Proton but Not Hydride Tunneling in Light‐Activated Protochlorophyllide Oxidoreductase
Author(s) -
Heyes Derren J.,
Sakuma Michiyo,
Scrutton Nigel S.
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200900086
Subject(s) - protochlorophyllide , hydride , chemistry , oxidoreductase , photochemistry , solvent , proton , quantum tunnelling , enzyme , physics , organic chemistry , hydrogen , condensed matter physics , quantum mechanics
H + but not H − : The reduction reaction of protochlorophyllide catalyzed by protochlorophyllide oxidoreductase features solvent‐slaved motions that control the proton‐ but not the hydride‐tunneling mechanism. These motions imply a long‐range dynamic network from the solvent to the enzyme active site that facilitate proton transfer (see picture, left). Motions for hydride transfer are more localized and are not slaved by the solvent (see picture, right).