Unknown

Dataset Information

0

Site-Specific Oxidation State Assignments of the Iron Atoms in the [4Fe:4S]2+/1+/0 States of the Nitrogenase Fe-Protein.

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]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.

SUBMITTER: Wenke BB 

PROVIDER: S-EPMC6519357 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Site-Specific Oxidation State Assignments of the Iron Atoms in the [4Fe:4S]<sup>2+/1+/0</sup> States of the Nitrogenase Fe-Protein.

Wenke Belinda B BB   Spatzal Thomas T   Rees Douglas C DC  

Angewandte Chemie (International ed. in English) 20190214 12

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]<sup>1+</sup> st  ...[more]

Similar Datasets

Unknown Characterization of [4Fe-4S] cluster vibrations and structure in nitrogenase Fe protein at three oxidation levels via combined NRVS, EXAFS, and DFT analyses.
| S-EPMC3644515 | biostudies-literature
Unknown Highly Loaded Independent Pt<sup>0</sup> Atoms on Graphdiyne for pH-General Methanol Oxidation Reaction.
| S-EPMC9165484 | biostudies-literature
Unknown Mass spectrometric detection of iron nitrosyls, sulfide oxidation and mycothiolation during nitrosylation of the NO sensor [4Fe-4S] NsrR.
| S-EPMC5994877 | biostudies-literature
Unknown Quick and Spontaneous Transformation between [3Fe-4S] and [4Fe-4S] Iron-Sulfur Clusters in the tRNA-Thiolation Enzyme TtuA.
| S-EPMC9821441 | biostudies-literature
Unknown Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA.
| S-EPMC6748827 | biostudies-literature
Unknown Generation of <sup>34</sup>S-substituted protein-bound [4Fe-4S] clusters using <sup>34</sup>S-L-cysteine.
| S-EPMC7200944 | biostudies-literature
Unknown Connecting the geometric and electronic structures of the nitrogenase iron-molybdenum cofactor through site-selective <sup>57</sup>Fe labelling.
| S-EPMC10710871 | biostudies-literature
Unknown Advanced Oxidation Processes Coupled to Nanofiltration Membranes with Catalytic Fe<sup>0</sup> Nanoparticles in Symmetric and Asymmetric Polyelectrolyte Multilayers.
| S-EPMC10141899 | biostudies-literature
Unknown Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.
| S-EPMC8251694 | biostudies-literature
Unknown Evidence that phosphorylation of iron regulatory protein 1 at Serine 138 destabilizes the [4Fe-4S] cluster in cytosolic aconitase by enhancing 4Fe-3Fe cycling.
| S-EPMC2675999 | biostudies-literature