期刊
CATALYSTS
卷 10, 期 11, 页码 -出版社
MDPI
DOI: 10.3390/catal10111317
关键词
nitrogenase; biomimetic; FeMoco; NifB-co; carbide; biogenesis
资金
- National Science Foundation [NSF CHE-1808311]
- Robert A. Welch Foundation [F-1822]
The family of nitrogenase enzymes catalyzes the reduction of atmospheric dinitrogen (N-2) to ammonia under remarkably benign conditions of temperature, pressure, and pH. Therefore, the development of synthetic complexes or materials that can similarly perform this reaction is of critical interest. The primary obstacle for obtaining realistic synthetic models of the active site iron-sulfur-carbide cluster (e.g., FeMoco) is the incorporation of a truly inorganic carbide. This review summarizes the present state of knowledge regarding biological and chemical (synthetic) incorporation of carbide into iron-sulfur clusters. This includes the Nif cluster of proteins and associated biochemistry involved in the endogenous biogenesis of FeMoco. We focus on the chemical (synthetic) incorporation portion of our own efforts to incorporate and modify C-1 units in iron/sulfur clusters. We also highlight recent contributions from other research groups in the area toward C-1 and/or inorganic carbide insertion.
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