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

08:00 EDT 14th August 2019 | BioPortfolio

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

Nitrogenase catalyzes the reduction of N2 to NH₄+ at its cofactor site. Designated the M-cluster, this [MoFe₇S₉C(R-homocitrate)] cofactor is synthesized via transformation of a [Fe₄S₄] cluster pair into an [Fe₈S₉C] precursor (designated the L-cluster) prior to insertion of Mo and homocitrate. Here we report the characterization of an eight-iron cofactor precursor (designated the L*-cluster), which is proposed to have a composition of [Fe₈S₈C] and lack the "9th sulfur" in the belt region of the L-cluster. Our X-ray absorption and electron spin echo envelope modulation analyses strongly suggest that the L*-cluster represents a structural homolog 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 nitrogenase.

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This article was published in the following journal.

Name: Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
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