6N4L
Dithionite-reduced ADP-bound form of the nitrogenase Fe-protein from A. vinelandii
Summary for 6N4L
| Entry DOI | 10.2210/pdb6n4l/pdb |
| Descriptor | Nitrogenase iron protein 1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | nitrogenase, iron sulfur cluster, adp, oxidoreductase |
| Biological source | Azotobacter vinelandii |
| Total number of polymer chains | 1 |
| Total formula weight | 32220.19 |
| Authors | Wenke, B.B.,Spatzal, T.,Rees, D.C. (deposition date: 2018-11-19, release date: 2019-02-13, Last modification date: 2023-10-11) |
| Primary citation | Wenke, B.B.,Spatzal, T.,Rees, D.C. Site-Specific Oxidation State Assignments of the Iron Atoms in the [4Fe:4S]2+/1+/0States of the Nitrogenase Fe-Protein. Angew. Chem. Int. Ed. Engl., 58:3894-3897, 2019 Cited by PubMed Abstract: 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] state, our analysis identifies a solvent exposed, delocalized Fe pair and a buried Fe 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] and [4Fe:4S] states, the SpReAD analysis supports oxidation states assignments for all irons in these clusters of Fe and valence delocalized Fe , respectively. PubMed: 30698901DOI: 10.1002/anie.201813966 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.13 Å) |
Structure validation
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