ArticleJournal of the American Chemical Society2016
Tyrosine-Coordinated P-Cluster in G. diazotrophicus Nitrogenase: Evidence for the Importance of O-Based Ligands in Conformationally Gated Electron Transfer.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 45 citations in OpenAlex.
- Molecular basis of NNature communications · 2026Article
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Iron-sulfur clusters: the road to room temperature.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Nitrogenase beyond the Resting State: A Structural Perspective.Molecules (Basel, Switzerland) · 2023Review
- Facile and dynamic cleavage of every iron-sulfide bond in cuboidal iron-sulfur clusters.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Quantum Mechanical Calculations of Redox Potentials of the Metal Clusters in Nitrogenase.Molecules (Basel, Switzerland) · 2022Article
- Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster.Journal of the American Chemical Society · 2022Article
- A conformational role for NifW in the maturation of molybdenum nitrogenase P-cluster.Chemical science · 2022Article
- Statistical analysis of PRSC advances · 2022Article
- Crystallographic snapshots of a BNature · 2022Article
- Molecular Basis of Multiple Mitochondrial Dysfunctions Syndrome 2 Caused by CYS59TYR BOLA3 Mutation.International journal of molecular sciences · 2021Article
- Shallow Distance Dependence for Proton-Coupled Tyrosine Oxidation in Oligoproline Peptides.Journal of the American Chemical Society · 2020Article
- Reduction of Substrates by Nitrogenases.Chemical reviews · 2020Review
- The Spectroscopy of Nitrogenases.Chemical reviews · 2020Review
- Structural Enzymology of Nitrogenase Enzymes.Chemical reviews · 2020Review
- Electron Transfer in Nitrogenase.Chemical reviews · 2020Review
- Structural evidence for a dynamic metallocofactor during NScience (New York, N.Y.) · 2020Article
- Double-Cubane [8Fe9S] Clusters: A Novel Nitrogenase-Related Cofactor in Biology.Chembiochem : a European journal of chemical biology · 2020Review
- Article
- Electronic landscape of the P-cluster of nitrogenase as revealed through many-electron quantum wavefunction simulations.Nature chemistry · 2019Article
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5 authors at 2 institutions in 1 country.
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Abstract
The P-cluster is a unique iron-sulfur center that likely functions as a dynamic electron (e(-)) relay site between the Fe-protein and the catalytic FeMo-cofactor in nitrogenase. The P-cluster has been shown to undergo large conformational changes upon 2-e(-) oxidation which entail the coordination of two of the Fe centers to a Ser side chain and a backbone amide N, respectively. Yet, how and if this 2-e(-) oxidized state (P(OX)) is involved in catalysis by nitrogenase is not well established. Here, we present the crystal structures of reduced and oxidized MoFe-protein (MoFeP) from Gluconacetobacter diazotrophicus (Gd), which natively possesses an Ala residue in the position of the Ser ligand to the P-cluster. While reduced Gd-MoFeP is structurally identical to previously characterized counterparts around the FeMo-cofactor, oxidized Gd-MoFeP features an unusual Tyr coordination to its P-cluster along with ligation by a backbone amide nitrogen. EPR analysis of the oxidized Gd-MoFeP P-cluster confirmed that it is a 2-e(-) oxidized, integer-spin species. Importantly, we have found that the sequence positions corresponding to the Ser and Tyr ligands are almost completely covariant among Group I nitrogenases. These findings strongly support the possibility that the P(OX) state is functionally relevant in nitrogenase catalysis and that a hard, O-based anionic ligand serves to stabilize this state in a switchable fashion.
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