Evidence map›Paper›PMID 21969545›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Molecular hijacking of siroheme for the synthesis of heme and d1 heme.

Shilpa Bali, Andrew D Lawrence, Susana A Lobo, Lígia M Saraiva, Bernard T Golding, David J Palmer, Mark J Howard, Stuart J Ferguson, Martin J Warren

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.0field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Review
  3. The Keto Functions of Heme dChembiochem : a European journal of chemical biology · 2026
    Article
  4. Comparative genomics of theISME communications · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Multi-modular metabolic engineering of heme synthesis inSynthetic and systems biotechnology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Microbial Synthesis of HemeMolecules (Basel, Switzerland) · 2023
    Review
  16. Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022
    Review
  17. Review
  18. Article
  19. RadicalJournal of the American Chemical Society · 2022
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Shilpa BaliDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
Andrew D Lawrence
Susana A Lobo
Lígia M Saraiva
Bernard T Golding
David J Palmer
Mark J Howard
Stuart J Ferguson
Martin J Warren
University of Kent · GBNewcastle University · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E022944/1Biotechnology and Biological Sciences Research Council BBE0229441Biotechnology and Biological Sciences Research Council BB/E024203Biotechnology and Biological Sciences Research Council BB/E024203/1Wellcome Trust 091163/Z/10/Z
6 · The paper itself

Abstract

Modified tetrapyrroles such as chlorophyll, heme, siroheme, vitamin B(12), coenzyme F(430), and heme d(1) underpin a wide range of essential biological functions in all domains of life, and it is therefore surprising that the syntheses of many of these life pigments remain poorly understood. It is known that the construction of the central molecular framework of modified tetrapyrroles is mediated via a common, core pathway. Herein a further branch of the modified tetrapyrrole biosynthesis pathway is described in denitrifying and sulfate-reducing bacteria as well as the Archaea. This process entails the hijacking of siroheme, the prosthetic group of sulfite and nitrite reductase, and its processing into heme and d(1) heme. The initial step in these transformations involves the decarboxylation of siroheme to give didecarboxysiroheme. For d(1) heme synthesis this intermediate has to undergo the replacement of two propionate side chains with oxygen functionalities and the introduction of a double bond into a further peripheral side chain. For heme synthesis didecarboxysiroheme is converted into Fe-coproporphyrin by oxidative loss of two acetic acid side chains. Fe-coproporphyrin is then transformed into heme by the oxidative decarboxylation of two propionate side chains. The mechanisms of these reactions are discussed and the evolutionary significance of another role for siroheme is examined.

Indexed as

Chromatography, High Pressure LiquidHemeOxygenHemeOxygensiroheme

Identifiers

PMID21969545
PMCPMC3215036
OpenAlexW2120476410

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.