Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes

Rahul Banerjee, Vivek Srinivas, Hugo Lebrette

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations


Ferritin-like proteins share a common fold, a four α-helix bundle core, often coordinating a pair of metal ions. Although conserved, the ferritin fold permits a diverse set of reactions, and is central in a multitude of macromolecular enzyme complexes. Here, we emphasize this diversity through three members of the ferritin-like superfamily: the soluble methane monooxygenase, the class I ribonucleotide reductase and the aldehyde deformylating oxygenase. They all rely on dinuclear metal cofactors to catalyze different challenging oxygen-dependent reactions through the formation of multi-protein complexes. Recent studies using cryo-electron microscopy, serial femtosecond crystallography at an X-ray free electron laser source, or single-crystal X-ray diffraction, have reported the structures of the active protein complexes, and revealed unprecedented insights into the molecular mechanisms of these three enzymes.

Original languageEnglish (US)
Title of host publicationSubcellular Biochemistry
PublisherSpringer Science and Business Media B.V.
Number of pages45
StatePublished - 2022

Publication series

NameSub-cellular biochemistry
PublisherPlenum Publishers
ISSN (Print)0306-0225

Bibliographical note

Publisher Copyright:
© 2022, The Author(s), under exclusive license to Springer Nature Switzerland AG.


  • Aldehyde deformylating oxygenase
  • Cryo-electron microscopy
  • Ferritin-like superfamily
  • Methane monooxygenase
  • Ribonucleotide reductase
  • Serial femtosecond crystallography
  • X-ray crystallography
  • X-ray free electron laser
  • Ribonucleotide Reductases/chemistry
  • Ferritins/metabolism
  • Crystallography, X-Ray
  • Ions/metabolism
  • Oxygen/metabolism
  • Aldehydes
  • Cryoelectron Microscopy
  • Oxygenases/chemistry
  • Multienzyme Complexes/metabolism

PubMed: MeSH publication types

  • Journal Article


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