期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 40, 页码 15898-15903出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1310153110
关键词
nitrogenase; nitrogen fixation; Fe-N-2 complexes; small molecule activation; ammonia production
资金
- National Institutes of Health [GM 070757)]
- Gordon and Betty Moore Foundation
- National Science Foundation graduate fellowship
We report here a series of four-and five-coordinate Fe model complexes that feature an axial tri(silyl) methyl ligand positioned trans to a substrate-binding site. This arrangement is used to crudely model a single-belt Fe site of the FeMo-cofactor that might bind N-2 at a position trans to the interstitial C atom. Reduction of a trigonal pyramidal Fe(I) complex leads to uptake of N-2 and subsequent functionalization furnishes an open-shell Fe-diazenido complex. A related series of five-coordinate Fe-CO complexes stable across three redox states is also described. Spectroscopic, crystallographic, and Density Functional Theory (DFT) studies of these complexes suggest that a decrease in the covalency of the Fe-C-alkyl interaction occurs upon reduction and substrate binding. This leads to unusually long Fe-C-alkyl bond distances that reflect an ionic Fe-C bond. The data presented are contextualized in support of a hypothesis wherein modulation of a belt Fe-C interaction in the FeMo-cofactor facilitates substrate binding and reduction.
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