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Fischer–Tropsch Chemistry at Room Temperature?
Author(s) -
Gerlach Deidra L.,
Lehnert Nicolai
Publication year - 2011
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.201102979
Subject(s) - nitrogenase , fischer–tropsch process , catalysis , vanadium , chemistry , adenosine triphosphate , adenosine diphosphate , enzyme , biochemistry , inorganic chemistry , organic chemistry , biology , nitrogen fixation , platelet aggregation , platelet , nitrogen , immunology , selectivity
The unique catalytic activity of vanadium nitrogenase suggests a new direction for the direct production of biofuels from CO with either synthetic catalysts or nitrogenase‐containing bacteria. The reduction of CO by V nitrogenase to light hydrocarbons (see scheme) shows striking similarities to the established Fischer–Tropsch process; however, the enzyme does not use H 2 directly for this reaction. ADP=adenosine diphosphate, ATP= adenosine triphosphate.