2014/12/30 by Ragnar Björnsson, Frank Neese, Richard R. Schrock +2 · 1 citation
Energy · Chemical Engineering · #Metalloenzymes and iron-sulfur proteins #Electrocatalysts for Energy Conversion #Ammonia Synthesis and Nitrogen Reduction
paper · pdf · doi:10.1007/s00775-014-1230-6
openalex publication_date 2014/12/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Biological nitrogen fixation is enabled by molybdenum-dependent nitrogenase enzymes, which effect the reduction of dinitrogen to ammonia using an Fe7MoS9C active site, referred to as the iron molybdenum cofactor or FeMoco. In this mini-review, we summarize the current understanding of the molecular and electronic structure of FeMoco. The advances in our understanding of the active site structure are placed in context with the parallel evolution of synthetic model studies. The recent discovery of Mo(III) in the FeMoco active site is highlighted with an emphasis placed on the important role that model studies have played in this finding. In addition, the reactivities of synthetic models are discussed in terms of their relevance to the enzymatic system.