ArticleJournal of the American Chemical Society2026
Structural Characterization of Four Redox States of the P-cluster in Molybdenum Nitrogenase via Electrochemical Control of Crystals.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
We report X-ray crystallographic structures of the Azotobacter vinelandii nitrogenase MoFe protein showing the 8Fe-7S electron-transfer P-cluster in four redox states. Using electrochemical poising of protein crystals, together with in crystallo EPR spectroscopic verification of the redox state, we obtain structures showing the P-cluster at PN, P1+, P2+, and P3+ levels. This provides a detailed structural characterization of P-cluster rearrangement between the catalytically relevant PN and P1+ levels and the first experimental confirmation that the S = 7/2 P3+ state is structurally similar to P2+. These studies pave the way for future understanding of the structure-function relationship in nitrogenase catalysis.
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