ArticleJournal of the American Chemical Society2017
Reversible Protonated Resting State of the Nitrogenase Active Site.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Deserts, Rivers, Pools, and Billabongs: Water Features of the Nitrogenase Proteins, and their Functions.Chembiochem : a European journal of chemical biology · 2025Review
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra.Nature communications · 2024Article
- Evaluating Diazene to NChemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Nitrogenase beyond the Resting State: A Structural Perspective.Molecules (Basel, Switzerland) · 2023Review
- Understanding the Electronic Structure Basis for NInorganic chemistry · 2023Article
- Structures of the nitrogenase complex prepared under catalytic turnover conditions.Science (New York, N.Y.) · 2022Article
- Selenium Valence-to-Core X-ray Emission Spectroscopy and Kβ HERFD X-ray Absorption Spectroscopy as Complementary Probes of Chemical and Electronic Structure.Inorganic chemistry · 2022Article
- Statistical analysis of PRSC advances · 2022Article
- The EChemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Structural Enzymology of Nitrogenase Enzymes.Chemical reviews · 2020Review
- Article
- Molybdenum imidazole citrate and bipyridine homocitrate in different oxidation states - balance between coordinated α-hydroxy and α-alkoxy groups.RSC advances · 2018Article
- Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for NProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State EInorganic chemistry · 2018Article
- An S =Journal of the American Chemical Society · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
Protonated states of the nitrogenase active site are mechanistically significant since substrate reduction is invariably accompanied by proton uptake. We report the low pH characterization by X-ray crystallography and EPR spectroscopy of the nitrogenase molybdenum iron (MoFe) proteins from two phylogenetically distinct nitrogenases (Azotobacter vinelandii, Av, and Clostridium pasteurianum, Cp) at pHs between 4.5 and 8. X-ray data at pHs of 4.5-6 reveal the repositioning of side chains along one side of the FeMo-cofactor, and the corresponding EPR data shows a new S = 3/2 spin system with spectral features similar to a state previously observed during catalytic turnover. The structural changes suggest that FeMo-cofactor belt sulfurs S3A or S5A are potential protonation sites. Notably, the observed structural and electronic low pH changes are correlated and reversible. The detailed structural rearrangements differ between the two MoFe proteins, which may reflect differences in potential protonation sites at the active site among nitrogenase species. These observations emphasize the benefits of investigating multiple nitrogenase species. Our experimental data suggest that reversible protonation of the resting state is likely occurring, and we term this state "E
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.