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Cited by 51Porphyrin Metabolism and DisordersMetalloenzymes and iron-sulfur proteinsEnzyme Structure and Function

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Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization

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Romão, Célia V., Ladakis, Dimitrios, Lobo, Susana A. L., Carrondo, Maria A., Brindley, Amanda A., Deery, Evelyne, Matias, Pedro M., Pickersgill, Richard W., Saraiva, Lígia M., Warren, Martin J.·2011·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1014298108PMC PMC3017170
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Abstract

The class II chelatases associated with heme, siroheme, and cobalamin biosynthesis are structurally related enzymes that insert a specific metal ion (Fe 2+ or Co 2+ ) into the center of a modified tetrapyrrole (protoporphyrin or sirohydrochlorin). The structures of two related class II enzymes, CbiX S from Archaeoglobus fulgidus and CbiK from Salmonella enterica , that are responsible for the insertion of cobalt along the cobalamin biosynthesis pathway are presented in complex with their metallated product. A further structure of a CbiK from Desulfovibrio vulgaris Hildenborough reveals how cobalt is bound at the active site. The crystal structures show that the binding of sirohydrochlorin is distinctly different to porphyrin binding in the protoporphyrin ferrochelatases and provide a molecular overview of the mechanism of chelation. The structures also give insights into the evolution of chelatase form and function. Finally, the structure of a periplasmic form of Desulfovibrio vulgaris Hildenborough CbiK reveals a novel tetrameric arrangement of its subunits that are stabilized by the presence of a heme b cofactor. Whereas retaining colbaltochelatase activity, this protein has acquired a central cavity with the potential to chaperone or transport metals across the periplasmic space, thereby evolving a new use for an ancient protein subunit.

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  • All tetrapyrrole class II chelatases derive from a common ancestor that evolved through duplication to give rise to CbiXL, CbiK, HemH (PpfC/CpfC) and SirB (ShfC).

    “In addition, all tetrapyrrole class II chelatases derive from a common ancestor [143, 144], that evolved through duplication to give rise to CbiXL, CbiK, HemH (PpfC/CpfC) and SirB (ShfC).”

    From Evidence for corrin biosynthesis in the last universal common ancestor (2025) · cites this paper as [143]

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Metadata

Authors
Romão, C. V., Ladakis, D., Lobo, S. A. L., Carrondo, M. A., Brindley, A. A., Deery, E., Matias, P. M., Pickersgill, R. W., Saraiva, L. M., & Warren, M. J.
Affiliations
  • Universidade Nova de Lisboa (PT)
  • University of Kent (GB)
  • Queen Mary University of London (GB)
  • Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República (EAN), 2780-157 Oeiras, Portugal;
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2010-12-20
Volume
108
Issue
1
Pages
97-102
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.1014298108
PMC
PMC3017170
OpenAlex
W2025993663
Cited by
51
References
1
Citations by year
2026: 3 · 2025: 3 · 2024: 5 · 2022: 5 · 2021: 3 · 2020: 5 · 2019: 7 · 2018: 1 · 2017: 4 · 2016: 3 · 2014: 3 · 2013: 1 · 2012: 7
FWCI
1.16
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Kent Academic Repository (University of Kent) (submittedVersion)
  • UEA Digital Repository (University of East Anglia) (submittedVersion)
Funders
Biotechnology and Biological Sciences Research Council (BB/D016568/1, BB/E002137, BB/E002137/1, BB/E024203, C20271/2, BB/D016568)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
vitamin B12 biosynthesis, heme biosynthesis, Archaeoglobus fulgidus, Salmonella enterica, Desulfovibrio vulgaris Hildenborough, sirohydrochlorin, protein oligomerization, protein evolution, metal ion insertion, crystal structure
MeSH terms
Cobalt, Crystallization, Ferrochelatase, Multigene Family, Models, Molecular, Porphyrins, Uroporphyrins, Vitamin B 12, Desulfovibrio vulgaris, Evolution, Molecular, Archaeoglobus fulgidus, Salmonella enterica, Catalytic Domain

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