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Catalytic Mechanism of the Metal‐Free Hydrogenase from Methanogenic Archaea: Reversed Stereospecificity of the Catalytic and Noncatalytic Reaction
Author(s) -
Geierstanger Bernhard H.,
Prasch Thomas,
Griesinger Christian,
Hartmann Gudrun,
Buurman Gerrit,
Thauer Rolf K.
Publication year - 1998
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/(sici)1521-3773(19981217)37:23<3300::aid-anie3300>3.0.co;2-a
Subject(s) - exergonic reaction , chemistry , stereospecificity , catalysis , hydrogenase , archaea , enzyme , reaction mechanism , stereochemistry , photochemistry , organic chemistry , biochemistry , gene
By activation of the hydrogen acceptor , the metal‐free hydrogenase from methanogenic archaea catalyzes the reduction of methenyl tetrahydromethanopterin with H 2 . According to NMR spectroscopic analysis of the conformation of the hydrogen acceptor in solution and of the stereospecificity of the catalyzed and noncatalyzed reaction, in the enzyme‐catalyzed reaction the hydrogenation product is formed in a constraint conformation which relaxes upon dissociation from the enzyme. This exergonic conformational change could help to avoid product inhibition of the enzyme.