Abstract
The enzyme nitrogenase catalyzes the biological nitrogen fixation where N-2 is reduced to NH3. Density functional calculations are presented of the bonding and hydrogenation of N-2 on a MoFe6S9 complex constructed to model aspects of the active site of nitrogenase. N-2 is found to bind end on to one of the Fe atoms. A complete energy diagram for the addition of hydrogen to the MoFe6S9 complex with and without N-2 is given, and a mechanism for ammonia synthesis is proposed on this basis.
Original language | English |
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Journal | Physical Review Letters |
Volume | 82 |
Issue number | 20 |
Pages (from-to) | 4054-4057 |
ISSN | 0031-9007 |
DOIs | |
Publication status | Published - 1999 |
Bibliographical note
Copyright (1999) by the American Physical Society.Keywords
- SURFACE
- P-CLUSTER
- FEMO-COFACTOR
- CATALYSIS
- PROTEIN
- PASTEURIANUM
- AZOTOBACTER-VINELANDII
- DINITROGEN
- AMMONIA-SYNTHESIS
- PSEUDOPOTENTIALS