Structural analysis of haemin demetallation by L-chain apoferritins.
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Summary
It is concluded that L-chain ferritins are capable of binding and demetallating haemin, generating in the process N-ethylprotoporphyrin IX both in vivo and in vitro.
- Type
- article
- Published
- 2012-07-01
- Cited by
- 31
- References
- 54
- OpenAlex
- https://openalex.org/W1975552457
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:9254932
Keywords
Chemistry, Porphyrin, Cofactor, Mutant, Recombinant DNA
References
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- Disruption of hepatic heme biosynthesis after interaction of xenobiotics with cytochrome P‐450
- FERRITIN I. PHYSICAL AND CHEMICAL PROPERTIES OF HORSE SPLEEN FERRITIN
- Mass spectrometry studies of demetallation of haemin by recombinant horse L chain apoferritin and its mutant (E 53,56,57,60 Q)
- Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution.
- Amino acid sequence of horse spleen apoferritin
- Iron mobilization from ferritin by chelating agents.
- Crystal structure of bullfrog M ferritin at 2.8 Å resolution: analysis of subunit interactions and the binuclear metal center
- Optical and EPR spectroscopic studies of demetallation of hemin by L-chain apoferritins.
- Unpaarigkeit und Radikalketten im Reaktionsmechanismus organischer und enzymatischer Vorgänge
- Fluorescence analysis of the labile iron pool of mammalian cells.
- Structural basis for high‐affinity volatile anesthetic binding in a natural 4‐helix bundle protein
- Evidence of new cadmium binding sites in recombinant horse L‐chain ferritin by anomalous Fourier difference map calculation
- High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites.
- Structural description of the active sites of mouse L-chain ferritin at 1.2 Å resolution
- Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.
- Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
- The CCP4 suite: programs for protein crystallography.
Cited by
- Fe2+ Substrate Transport through Ferritin Protein Cage Ion Channels Influences Enzyme Activity and Biomineralization
- The importance of eukaryotic ferritins in iron handling and cytoprotection.
- Unity in the biochemistry of the iron-storage proteins ferritin and bacterioferritin.
- Apoferritin applications in nanomedicine.
- Cisplatin encapsulation within a ferritin nanocage: a high-resolution crystallographic study.
- Exploring the Nature of the Nanocavity and Channels in Apoferritin and Apoferritin–Sodium Dodecyl Sulfate Complex Using an Enhanced Antenna Effect through the Encapsulation of EuIII–Tetracycline
- Chemistry at the protein–mineral interface in L-ferritin assists the assembly of a functional (μ3-oxo)Tris[(μ2-peroxo)] triiron(III) cluster
- Unsaturated Long-Chain Fatty Acids Are Preferred Ferritin Ligands That Enhance Iron Biomineralization.
- Medium throughput cage state stability screen of conditions for the generation of gold nanoparticles encapsulated within a mini-ferritin.
- Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods
- Processing Apoferritin with the Appion Pipeline
- RELION-3: new tools for automated high-resolution cryo-EM structure determination
- New tools for automated high-resolution cryo-EM structure determination in RELION-3
- Photochemistry of ferritin decorated with plasmonic gold nanoparticles
- Multifunctional graphene supports for electron cryomicroscopy
- Solvent flows, conformation changes and lattice reordering in a cold protein crystal.
- Controlling protein nanocage assembly with hydrostatic pressure
- Ferritin Nanocage: A Versatile Nanocarrier Utilized in the Field of Food, Nutrition, and Medicine
- Devitrification reduces beam-induced movement in cryo-EM
- Protein nanoparticles in molecular, cellular, and tissue imaging.
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