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PDBsum entry 6n4m
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Oxidoreductase
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PDB id
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6n4m
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References listed in PDB file
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Key reference
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Title
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Site-Specific oxidation state assignments of the iron atoms in the [4fe:4s]2+/1+/0 states of the nitrogenase fe-Protein.
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Authors
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B.B.Wenke,
T.Spatzal,
D.C.Rees.
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Ref.
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Angew Chem Int Ed Engl, 2019,
58,
3894-3897.
[DOI no: ]
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PubMed id
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Abstract
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The nitrogenase iron protein (Fe-protein) contains an unusual [4Fe:4S]
iron-sulphur cluster that is stable in three oxidation states: 2+, 1+, and 0.
Here, we use spatially resolved anomalous dispersion (SpReAD) refinement to
determine oxidation assignments for the individual irons for each state.
Additionally, we report the 1.13-Å resolution structure for the ADP bound
Fe-protein, the highest resolution Fe-protein structure presently determined. In
the dithionite-reduced [4Fe:4S]1+ state, our analysis identifies a
solvent exposed, delocalized Fe2.5+ pair and a buried Fe2+
pair. We propose that ATP binding by the Fe-protein promotes an internal redox
rearrangement such that the solvent-exposed Fe pair becomes reduced, thereby
facilitating electron transfer to the nitrogenase molybdenum iron-protein. In
the [4Fe:4S]0 and [4Fe:4S]2+ states, the SpReAD analysis
supports oxidation states assignments for all irons in these clusters of
Fe2+ and valence delocalized Fe2.5+ , respectively.
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