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The Crystal Structure of an [Fe]‐Hydrogenase–Substrate Complex Reveals the Framework for H 2 Activation
Author(s) -
Hiromoto Takeshi,
Warkentin Eberhard,
Moll Johanna,
Ermler Ulrich,
Shima Seigo
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.200902695
Subject(s) - hydrogenase , substrate (aquarium) , binary number , computer science , basis (linear algebra) , resolution (logic) , crystallography , chemistry , information retrieval , biology , mathematics , catalysis , ecology , artificial intelligence , geometry , biochemistry , arithmetic
An open and closed case : The structure of a binary complex of C176A [Fe]‐hydrogenase with methylenetetrahydromethanopterin was solved at 2.15 Å resolution in an open conformation. A closed form of the complex was modeled on the basis of the experimentally determined structure. In this model, the iron‐site trans to the acyl carbon is located next to the C14a and therefore considered as H 2 binding site.