N 2 Binding to the FeMo‐Cofactor of Nitrogenase
Nitrogenase converts gaseous dinitrogen into biologically accessible ammonia. The binding of N 2 to a reduced and protonated form of the FeMo‐cofactor of nitrogenase including its central carbon ligand was investigated by means of density functional calculations. It was found the central ligand to s...
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| Published in: | Zeitschrift für anorganische und allgemeine Chemie (1950) Vol. 641; no. 1; pp. 118 - 122 |
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| Main Authors: | , |
| Format: | Journal Article |
| Language: | English |
| Published: |
01.01.2015
|
| ISSN: | 0044-2313, 1521-3749 |
| Online Access: | Get full text |
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| Summary: | Nitrogenase converts gaseous dinitrogen into biologically accessible ammonia. The binding of N
2
to a reduced and protonated form of the FeMo‐cofactor of nitrogenase including its central carbon ligand was investigated by means of density functional calculations. It was found the central ligand to stabilize the cluster. N
2
can associate to iron or molybdenum with iron being the preferred binding site. While
endo
and
exo
binding modes were investigated the
exo
modes are more stable. Implications on the mechanism of N
2
reduction are discussed. |
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| ISSN: | 0044-2313 1521-3749 |
| DOI: | 10.1002/zaac.201400114 |