ArticleNature communications2020
An evolutionary path to altered cofactor specificity in a metalloenzyme.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Relative bioavailability of dietary iron sources in growing Japanese quail: Multi-endpoint dose-response and Random Forest analyses.Poultry science · 2026Article
- A Zur-dependent regulatory RNA involved in maintaining zinc homeostasis in Staphylococcus aureus.Nucleic acids research · 2026Article
- An engineered biofactory for efficient production of diverse recombinant superoxide dismutase isozymes loaded with specific metal ions for biochemical characterization.bioRxiv : the preprint server for biology · 2026Article
- A closely related pair of superoxide dismutase isozymes from Staphylococcus aureus show distinct stabilities and proton-exchange dynamics.The Journal of biological chemistry · 2026Article
- The Factors Governing Metal Dependence of an Emergent Superfamily of Bimetallic Oxygenases.Journal of the American Chemical Society · 2026Article
- Distribution of Toxic and Essential Elements in Autopsy Organs of Subjects Living in South-Eastern Poland.International journal of molecular sciences · 2026Article
- An enzyme's metal preference evolves through redox modulation driven by the cofactor's secondary coordination sphere.Molecular biology and evolution · 2026Article
- Serine Mutation on Amicyanin Reveals Functional and Structural Roles of Asn47 and Asn54 in the Cu-Binding Ligand Containing Loop.Journal of microbiology and biotechnology · 2025Article
- Interpretable prediction of zinc ion location in proteins with ZincSight.Protein science : a publication of the Protein Society · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Rational Design of a Flavoenzyme for Aerobic Nicotine Catabolism.bioRxiv : the preprint server for biology · 2024Article
- Unveiling the Catalytic Mechanism of a Processive Metalloaminopeptidase.Biochemistry · 2023Article
- A Review of the Current State of Magnetic Force Microscopy to Unravel the Magnetic Properties of Nanomaterials Applied in Biological Systems and Future Directions for Quantum Technologies.Nanomaterials (Basel, Switzerland) · 2023Review
- An ancient metalloenzyme evolves through metal preference modulation.Nature ecology & evolution · 2023Article
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- Characterization of ancestral Fe/Mn superoxide dismutases indicates their cambialistic origin.Protein science : a publication of the Protein Society · 2022Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- The structure-function relationships and physiological roles of MnSOD mutants.Bioscience reports · 2022Review
- Old dogs, new tricks: New insights into the iron/manganese superoxide dismutase family.Journal of inorganic biochemistry · 2022Article
- The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3.Scientific reports · 2022Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
Abstract
Almost half of all enzymes utilize a metal cofactor. However, the features that dictate the metal utilized by metalloenzymes are poorly understood, limiting our ability to manipulate these enzymes for industrial and health-associated applications. The ubiquitous iron/manganese superoxide dismutase (SOD) family exemplifies this deficit, as the specific metal used by any family member cannot be predicted. Biochemical, structural and paramagnetic analysis of two evolutionarily related SODs with different metal specificity produced by the pathogenic bacterium Staphylococcus aureus identifies two positions that control metal specificity. These residues make no direct contacts with the metal-coordinating ligands but control the metal's redox properties, demonstrating that subtle architectural changes can dramatically alter metal utilization. Introducing these mutations into S. aureus alters the ability of the bacterium to resist superoxide stress when metal starved by the host, revealing that small changes in metal-dependent activity can drive the evolution of metalloenzymes with new cofactor specificity.
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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.