ArticleThe Journal of biological chemistry2010
Discovery and Characterization of HemQ: an essential heme biosynthetic pathway component.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 77 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- The terminal heme synthetic enzyme, coproheme decarboxylase, negatively regulates heme uptake in Mycobacterium tuberculosis.The Journal of biological chemistry · 2026Article
- The role of conserved elements in an active site α-helix of coproheme decarboxylase.Journal of inorganic biochemistry · 2026Article
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Identification of SARS-CoV-2 3CLpro inhibitors from marine actinomycetes through integrated phylogeny-based metabolomics with functional screening and bioinformatic analysis.Scientific reports · 2025Article
- High-yield porphyrin production through metabolic engineering and biocatalysis.Nature biotechnology · 2025Article
- Insights into the flexibility of the domain-linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations.Protein science : a publication of the Protein Society · 2025Article
- Acquiring of photosensitivity by Mycobacterium tuberculosis in vitro and inside infected macrophages is associated with accumulation of endogenous Zn-porphyrins.Scientific reports · 2024Article
- The alternative coproporphyrinogen III oxidase (CgoN) catalyzes the oxygen-independent conversion of coproporphyrinogen III into coproporphyrin III.Frontiers in microbiology · 2024Article
- Regulation of heme biosynthesis via the coproporphyrin dependent pathway in bacteria.Frontiers in microbiology · 2024Review
- Production of copropophyrin III, biliverdin and bilirubin by the rufomycin producer,Frontiers in microbiology · 2023Article
- Exogenously Scavenged and Endogenously Synthesized Heme Are Differentially Utilized by Mycobacterium tuberculosis.Microbiology spectrum · 2022Article
- Cryptic specialized metabolites driveProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation.ACS catalysis · 2020Article
- In silico-guided engineering of Pseudomonas putida towards growth under micro-oxic conditions.Microbial cell factories · 2019Article
- Systems metabolic engineering ofJournal of biological engineering · 2019Article
- Biosynthesis of organic photosensitizer Zn-porphyrin by diphtheria toxin repressor (DtxR)-mediated global upregulation of engineered heme biosynthesis pathway in Corynebacterium glutamicum.Scientific reports · 2018Article
- Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes.Biochemistry · 2018Article
- Distinguishing Active Site Characteristics of Chlorite Dismutases with Their Cyanide Complexes.Biochemistry · 2018Article
- Coproheme decarboxylases - Phylogenetic prediction versus biochemical experiments.Archives of biochemistry and biophysics · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
Here we identify a previously undescribed protein, HemQ, that is required for heme synthesis in Gram-positive bacteria. We have characterized HemQ from Bacillus subtilis and a number of Actinobacteria. HemQ is a multimeric heme-binding protein. Spectroscopic studies indicate that this heme is high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule. The presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. Although the exact role played by HemQ remains to be characterized, to be fully functional in vitro it requires the presence of a bound heme. HemQ possesses minimal peroxidase activity, but as a catalase it has a turnover of over 10(4) min(-1). We propose that this activity may be required to eliminate hydrogen peroxide that is generated by each turnover of HemY. Given the essential nature of heme synthesis and the restricted distribution of HemQ, this protein is a potential antimicrobial target for pathogens such as Mycobacterium tuberculosis.
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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.