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Differential Reduction of CO 2 by Molybdenum and Vanadium Nitrogenases
Author(s) -
Rebelein Johannes G.,
Hu Yilin,
Ribbe Markus W.
Publication year - 2014
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.201406863
Subject(s) - nitrogenase , vanadium , molybdenum , catalysis , chemistry , enzyme , inorganic chemistry , biochemistry , nitrogen fixation , organic chemistry , nitrogen
The molybdenum and vanadium nitrogenases are two homologous enzymes with distinct structural and catalytic features. Previously, it was demonstrated that the V nitrogenase was nearly 700 times more active than its Mo counterpart in reducing CO to hydrocarbons. Herein, a similar discrepancy between the two nitrogenases in the reduction of CO 2 is reported, with the V nitrogenase being capable of reducing CO 2 to CO, CD 4 , C 2 D 4 , and C 2 D 6 , and its Mo counterpart only capable of reducing CO 2 to CO. Furthermore, it is shown that the V nitrogenase may direct the formation of CD 4 in part via CO 2 ‐derived CO, but that it does not catalyze the formation of C 2 D 4 and C 2 D 6 along this route. The exciting observation of a V nitrogenase‐catalyzed CC coupling with CO 2 as the origin of the building blocks adds another interesting reaction to the catalytic repertoire of this unique enzyme system. The differential activities of the V and Mo nitrogenases in CO 2 reduction provide an important framework for systematic investigations of this reaction in the future.