ArticleJournal of bacteriology2006
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 60 citations in OpenAlex.
- Brucellosis: Bacteriology, pathogenesis, epidemiology and role of the metallophores in virulence: a review.Frontiers in cellular and infection microbiology · 2025Review
- Bradyrhizobium japonicum HmuP is an RNA-binding protein that positively controls hmuR operon expression by suppression of a negative regulatory RNA element in the 5' untranslated region.Molecular microbiology · 2024Article
- The Regulatory Protein ChuP Connects Heme and Siderophore-Mediated Iron Acquisition Systems Required forFrontiers in cellular and infection microbiology · 2022Article
- Heme Uptake and Utilization by Gram-Negative Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2019Review
- The affinity of MhuD for heme is consistent with a heme degrading function in vivo.Metallomics : integrated biometal science · 2018Article
- Ironing Out the Unconventional Mechanisms of Iron Acquisition and Gene Regulation inFrontiers in cellular and infection microbiology · 2017Review
- A bacterial iron exporter for maintenance of iron homeostasis.The Journal of biological chemistry · 2014Article
- The crimson conundrum: heme toxicity and tolerance in GAS.Frontiers in cellular and infection microbiology · 2014Article
- A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO.The Journal of biological chemistry · 2013Article
- Iron homeostasis in theAdvances in botanical research · 2013Article
- The bhuQ gene encodes a heme oxygenase that contributes to the ability of Brucella abortus 2308 to use heme as an iron source and is regulated by Irr.Journal of bacteriology · 2012Article
- Nutritional immunity: transition metals at the pathogen-host interface.Nature reviews. Microbiology · 2012Review
- HmuP is a coactivator of Irr-dependent expression of heme utilization genes in Bradyrhizobium japonicum.Journal of bacteriology · 2012Article
- Metal acquisition and virulence in Brucella.Animal health research reviews · 2012Review
- A battle for iron: host sequestration and Staphylococcus aureus acquisition.Microbes and infection · 2012Review
- Heme degrading protein HemS is involved in oxidative stress response of Bartonella henselae.PloS one · 2012Article
- Bacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.Microbiology (Reading, England) · 2011Article
- Staphylococcus lugdunensis IsdG liberates iron from host heme.Journal of bacteriology · 2011Article
- Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.Infection and immunity · 2010Review
- Bacteriophytochrome-dependent regulation of light-harvesting complexes in Rhodopseudomonas palustris anaerobic cultures.Current microbiology · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Utilization of heme by bacteria as a nutritional iron source involves the transport of exogenous heme, followed by cleavage of the heme macrocycle to release iron. Bradyrhizobium japonicum can use heme as an iron source, but no heme-degrading oxygenase has been described. Here, bioinformatics analyses of the B. japonicum genome identified two paralogous genes renamed hmuQ (bll7075) and hmuD (bll7423) that encode proteins with weak similarity to the heme-degrading monooxygenase IsdG from Staphylococcus aureus. The hmuQ gene is clustered with known heme transport genes in the genome. Recombinant HmuQ bound heme with a K(d) value of 0.8 microM and showed spectral properties consistent with a heme oxygenase. In the presence of a reductant, HmuQ catalyzed the degradation of heme and the formation of biliverdin. The hmuQ and hmuD genes complemented a Corynebacterium ulcerans heme oxygenase mutant in trans for utilization of heme as the sole iron source for growth. Furthermore, homologs of hmuQ and hmuD were identified in many bacterial genera, and the recombinant homolog from Brucella melitensis bound heme and catalyzed its degradation. The findings show that hmuQ and hmuD encode heme oxygenases and indicate that the IsdG family of heme-degrading monooxygenases is not restricted to gram-positive pathogenic bacteria.
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