ArticleBMC microbiology2008
Functional identification of HugZ, a heme oxygenase from Helicobacter pylori.
Article in BMC microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- Mechanism of Enhancement by the FeChemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Carbon monoxide-producing probioticiScience · 2026Article
- Rv3839-Rv3840 links the endogenous heme biosynthesis pathway with Mycobacterium tuberculosis adaptation to nitric oxide and iron limitation stress.PLoS genetics · 2026Article
- Rv3839-Rv3840 links the endogenous heme biosynthesis pathway withbioRxiv : the preprint server for biology · 2026Article
- Heme and CO metabolism by the canonical human heme oxygenases.Journal of inorganic biochemistry · 2026Review
- Methanotroph Methylotuvimicrobium alcaliphilum 20Z-3E as a fumarate producer: transcriptomic analysis and the role of malic enzyme.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Selection Maintains Photosynthesis in a Symbiotic Cyanobacterium Despite Redundancy With its Fern Host.Molecular biology and evolution · 2025Article
- Exploring Large Protein Sequence Space through Homology- and Representation-based Hierarchical Clustering.Molecular biology and evolution · 2025Article
- CDKN2A somatic copy number amplification in normal tissues surrounding gastric carcinoma reduces cancer metastasis risk in droplet digital PCR analysis.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2024Article
- Directed evolution ofChemical science · 2024Article
- A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria.Nature communications · 2024Article
- Infant diarrheal disease in rhesus macaques impedes microbiome maturation and is linked to uncultured Campylobacter species.Communications biology · 2024Article
- HemU and TonB1 contribute to hemin acquisition inFrontiers in cellular and infection microbiology · 2024Article
- ALA_PDT Promotes Ferroptosis-Like Death ofAntioxidants (Basel, Switzerland) · 2022Article
- Hydrogen Sulfide and Carbon Monoxide Tolerance in Bacteria.Antioxidants (Basel, Switzerland) · 2021Review
- Heme Uptake and Utilization by Gram-Negative Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2019Review
- From Host Heme To Iron: The Expanding Spectrum of Heme Degrading Enzymes Used by Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2018Review
- Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.Microbiology and molecular biology reviews : MMBR · 2016Review
- Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.Accounts of chemical research · 2014Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIron is recognized as an important trace element, essential for most organisms including pathogenic bacteria. HugZ, a protein related to heme iron utilization, is involved in bacterial acquisition of iron from the host. We previously observed that a hugZ homologue is correlated with the adaptive colonization of Helicobacter pylori (H. pylori), a major gastro-enteric pathogen. However, its exact physiological role remains unclear.
resultsA gene homologous to hugZ, designated hp0318, identified in H. pylori ATCC 26695, exhibits 66% similarity to cj1613c of Campylobacter jejuni NCTC 11168. Soluble 6 x His fused-HugZ protein was expressed in vitro. Hemin-agrose affinity analysis indicated that the recombinant HugZ protein can bind to hemin. Absorption spectroscopy at 411 nm further revealed a heme:HugZ binding ratio of 1:1. Enzymatic assays showed that purified recombinant HugZ protein can degrade hemin into biliverdin and carbon monoxide in the presence of either ascorbic acid or NADPH and cytochrome P450 reductase. The biochemical and enzymatic characteristics agreed closely with those of Campylobacter jejuni Cj1613c protein, implying that hp0318 is a functional member of the HugZ family. A hugZ deletion mutant was obtained by homologous recombination. This mutant strain showed poor growth when hemoglobin was provided as the source of iron, partly because of its failure to utilize hemoglobin efficiently. Real-time quantitative PCR also confirmed that the expression of hugZ was regulated by iron levels.
conclusionThese findings provide biochemical and genetic evidence that hugZ (hp0318) encodes a heme oxygenase involved in iron release/uptake in H. pylori.
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