Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement

Thomas Spatzal, Julia Schlesier, Eva-Maria Burger, Daniel Sippel, Limei Zhang, Susana L.A. Andrade, Douglas C. Rees and Oliver Einsle ()
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Thomas Spatzal: Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
Julia Schlesier: Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
Eva-Maria Burger: Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
Daniel Sippel: Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
Limei Zhang: California Institute of Technology
Susana L.A. Andrade: Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
Douglas C. Rees: Howard Hughes Medical Institute, California Institute of Technology
Oliver Einsle: Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg

Nature Communications, 2016, vol. 7, issue 1, 1-7

Abstract: Abstract The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the largest known metal cluster and catalyses the 6-electron reduction of dinitrogen to ammonium in biological nitrogen fixation. Only recently its atomic structure was clarified, while its reactivity and electronic structure remain under debate. Here we show that for its resting S=3/2 state the common iron oxidation state assignments must be reconsidered. By a spatially resolved refinement of the anomalous scattering contributions of the 7 Fe atoms of FeMoco, we conclude that three irons (Fe1/3/7) are more reduced than the other four (Fe2/4/5/6). Our data are in agreement with the recently revised oxidation state assignment for the molybdenum ion, providing the first spatially resolved picture of the resting-state electron distribution within FeMoco. This might provide the long-sought experimental basis for a generally accepted theoretical description of the cluster that is in line with available spectroscopic and functional data.

Date: 2016
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DOI: 10.1038/ncomms10902

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