A V-Nitrogenase Variant Containing a Citrate-Substituted Cofactor.

Nitrogenases catalyze the ambient reduction of N and CO at its cofactor site. Herein we present a biochemical and spectroscopic characterization of an Azotobacter vinelandii V nitrogenase variant expressing a citrate-substituted cofactor. Designated VnfDGK , the catalytic component of this V nitrogenase variant has an αβ (δ) subunit composition and carries an 8Fe P* cluster and a citrate-substituted V cluster analogue in the αβ dimer, as well as a 4Fe cluster in the "orphaned" β-subunit.

Electrochemical Characterization of Isolated Nitrogenase Cofactors from Azotobacter vinelandii.

The nitrogenase cofactors are structurally and functionally unique in biological chemistry. Despite a substantial amount of spectroscopic characterization of protein-bound and isolated nitrogenase cofactors, electrochemical characterization of these cofactors and their related species is far from complete. Herein we present voltammetric studies of three isolated nitrogenase cofactor species: the iron-molybdenum cofactor (M-cluster), iron-vanadium cofactor (V-cluster), and a homologue to the iron-iron cofactor (L-cluster).