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FeMoco
FeMoco is the primary cofactor of nitrogenase. Nitrogenase is the enzyme that catalyzes the conversion of atmospheric N2 into ammonia (NH3), through the process known as nitrogen fixation. Containing iron and molybdenum, the cofactor is called FeMoco. Its stoichiometry is Fe7MoS9C. ==Structure == The FeMo cofactor is a cluster with composition Fe7MoS9C. This large cluster can be viewed as two subunits composed of one Fe4S3 cluster and one MoFe3S3 cluster. The two clusters are linked by three sulfide ligands. The unique Fe is anchored to the protein by a cysteine. It is also bound to three sulfides, resulting in tetrahedral molecular geometry. The additional six Fe centers in the cluster are each bonded to three sulfides. These six internal Fe centers define a trigonal prismatic arrangement around a central carbide center. The molybdenum is attached to three sulfides and is anchored to the protein by the imidazole group of a histidine residue. Also bound to Mo is a bidentate homocitrate cofactor, leading to octahedral geometry.〔G.J. Leigh. Ch. 5 Structure and Spectroscopic Properties of Metallo-sulfur Clusters ''Nitrogen Fixation at the Millenium.'' Elsevier Science B. V., Amsterdam, 2002. 209-210. ISBN 9780444509659.〕 Crystallographic analysis of the MoFe protein initially proposed the geometry of FeMoco, which was confirmed by extended X-ray absorption fine-structure (EXAFS) studies.〔Roat-Malone, R.M. Ch.6 MoFe Protein Structure. Bioinorganic Chemistry. John Wiley & Sons, Inc., Hoboken, New Jersey, 2002. 253-254. ISBN 9780471265337.〕 Distances for Fe-S, Fe-Fe and Fe-Mo distances were determined to be 2.32, 2.64, and 2.73 Å respectively3.
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