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- Title
Spectroscopic Characterization of an Eight‐Iron Nitrogenase Cofactor Precursor that Lacks the "9<sup>th</sup> Sulfur".
- Authors
Jasniewski, Andrew J.; Wilcoxen, Jarett; Tanifuji, Kazuki; Hedman, Britt; Hodgson, Keith O.; Britt, R. David; Hu, Yilin; Ribbe, Markus W.
- Abstract
Nitrogenases catalyze the reduction of N2 to NH4+ at its cofactor site. Designated the M‐cluster, this [MoFe7S9C(R‐homocitrate)] cofactor is synthesized via the transformation of a [Fe4S4] cluster pair into an [Fe8S9C] 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 [Fe8S8C] 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.
- Subjects
COFACTORS (Biochemistry); NITROGENASES; ELECTRON spin echoes; MOLYBDENUM; SULFUR; X-ray absorption
- Publication
Angewandte Chemie, 2019, Vol 131, Issue 41, p14845
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201907593