ReviewArchives of biochemistry and biophysics2021
Diversity of structures and functions of oxo-bridged non-heme diiron proteins.
Review in Archives of biochemistry and biophysics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Engineering membrane-bound alkane monooxygenase from Marinobacter sp. for increased activity in the selective ω-hy-droxylation of linear and branched aliphatic esters.Protein science : a publication of the Protein Society · 2026Article
- Unsymmetric bimetallic centres in metalloproteins and synthetic models.Nature reviews. Chemistry · 2026Review
- New molecular components of high and low affinity iron import systems in Drosophila.Nature communications · 2025Article
- A [FeFe] Hydrogenase-Rubrerythrin Chimeric Enzyme Functions to Couple HJournal of the American Chemical Society · 2025Article
- [Fe(µMolecules (Basel, Switzerland) · 2024Article
- Drosophila Evi5 is a critical regulator of intracellular iron transport via transferrin and ferritin interactions.Nature communications · 2024Article
- Mobilization of iron stored in bacterioferritin, a new target for perturbing iron homeostasis and developing antibacterial and antibiofilm molecules.Journal of inorganic biochemistry · 2023Review
- Iron Metabolism of the Skin: Recycling versus Release.Metabolites · 2023Review
- Repair of Iron Center Proteins-A Different Class of Hemerythrin-like Proteins.Molecules (Basel, Switzerland) · 2022Review
- An Abundant and Diverse New Family of Electron Bifurcating Enzymes With a Non-canonical Catalytic Mechanism.Frontiers in microbiology · 2022Article
- Genome-Scale Mutational Analysis of Cathode-OxidizingFrontiers in microbiology · 2022Article
- Iron-Containing Ureases.Coordination chemistry reviews · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Oxo-bridged diiron proteins are a distinct class of non-heme iron proteins. Their active sites are composed of two irons that are coordinated by amino acid side chains, and a bridging oxygen that interacts with each iron. These proteins are members of the ferritin superfamily and share the structural feature of a four α-helix bundle that provides the residues that coordinate the irons. The different proteins also display a wide range of structures and functions. A prototype of this family is hemerythrin, which functions as an oxygen transporter. Several other hemerythrin-like proteins have been described with a diversity of functions including oxygen and iron sensing, and catalytic activities. Rubrerythrins react with hydrogen peroxide and rubrerythrin-like proteins possess a rubredoxin domain, in addition to the oxo-bridged diiron center. Other redox enzymes with oxo-bridged irons include flavodiiron proteins that act as O
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