Spectroscopic Characterization of an Eight-Iron Nitrogenase Cofactor Precursor that Lacks the "9th Sulfur".

ABSTRACT: Nitrogenases catalyze the reduction of N2 to NH4 + at its cofactor site. Designated the M-cluster, this [MoFe7 S9 C(R-homocitrate)] cofactor is synthesized via the transformation of a [Fe4 S4 ] cluster pair into an [Fe8 S9 C] precursor (designated the L-cluster) prior to insertion of Mo and homocitrate. We report the characterization of an eight-iron cofactor precursor (designated the L*-cluster), which is proposed to have the composition [Fe8 S8 C] and lack the "9th sulfur" in the belt region of the L-cluster. Our X-ray absorption and electron spin echo envelope modulation (ESEEM) analyses strongly suggest that the L*-cluster represents a structural homologue to the l-cluster except for the missing belt sulfur. The absence of a belt sulfur from the L*-cluster may prove beneficial for labeling the catalytically important belt region, which could in turn facilitate investigations into the reaction mechanism of nitrogenases.

SUBMITTER: Jasniewski AJ 

PROVIDER: S-EPMC6764854 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature