ArticleThe Journal of biological chemistry2013
IruO is a reductase for heme degradation by IsdI and IsdG proteins in Staphylococcus aureus.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- The roles of Asn7 and Trp67 in tuning the ferryl haem form ofDalton transactions (Cambridge, England : 2003) · 2026Article
- Article
- Analysis of Benzoate 1,2-Dioxygenase Identifies Shared Electron Transfer Components With DxnA1A2 in Rhizorhabdus wittichii RW1.Journal of basic microbiology · 2025Article
- Functional Diversity of Homologous Oxidoreductases-Tuning of Substrate Specificity by a FAD-Stacking Residue for Iron Acquisition and Flavodoxin Reduction.Antioxidants (Basel, Switzerland) · 2023Article
- Ruffling is essential for Staphylococcus aureus IsdG-catalyzed degradation of heme to staphylobilin.Journal of inorganic biochemistry · 2022Article
- Structure-function characterization of the mono- and diheme forms of MhuD, a noncanonical heme oxygenase from Mycobacterium tuberculosis.The Journal of biological chemistry · 2022Article
- Heme-Dependent Siderophore Utilization Promotes Iron-Restricted Growth of the Staphylococcus aureusJournal of bacteriology · 2021Article
- Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development.International journal of molecular sciences · 2020Review
- The heme-sensitive regulator SbnI has a bifunctional role in staphyloferrin B production byThe Journal of biological chemistry · 2019Article
- Iron Acquisition in Mycobacterium tuberculosis.Chemical reviews · 2019Review
- Tight binding of heme to Staphylococcus aureus IsdG and IsdI precludes design of a competitive inhibitor.Metallomics : integrated biometal science · 2017Article
- Reactions of Ferrous Coproheme Decarboxylase (HemQ) with OBiochemistry · 2017Article
- Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Heme uptake in bacterial pathogens.Current opinion in chemical biology · 2014Review
- Heme oxygenation and the widening paradigm of heme degradation.Archives of biochemistry and biophysics · 2014Review
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Staphylococcus aureus is a common hospital- and community-acquired bacterium that can cause devastating infections and is often multidrug-resistant. Iron acquisition is required by S. aureus during an infection, and iron acquisition pathways are potential targets for therapies. The gene NWMN2274 in S. aureus strain Newman is annotated as an oxidoreductase of the diverse pyridine nucleotide-disulfide oxidoreductase (PNDO) family. We show that NWMN2274 is an electron donor to IsdG and IsdI catalyzing the degradation of heme, and we have renamed this protein IruO. Recombinant IruO is a FAD-containing NADPH-dependent reductase. In the presence of NADPH and IruO, either IsdI or IsdG degraded bound heme 10-fold more rapidly than with the chemical reductant ascorbic acid. Varying IsdI-heme substrate and monitoring loss of the heme Soret band gave a K(m) of 15 ± 4 μM, a k(cat) of 5.2 ± 0.7 min(-1), and a k(cat)/K(m) of 5.8 × 10(3) M(-1) s(-1). From HPLC and electronic spectra, the major heme degradation products are 5-oxo-δ-bilirubin and 15-oxo-β-bilirubin (staphylobilins), as observed with ascorbic acid. Although heme degradation by IsdI or IsdG can occur in the presence of H2O2, the addition of catalase and superoxide dismutase did not disrupt NADPH/IruO heme degradation reactions. The degree of electron coupling between IruO and IsdI or IsdG remains to be determined. Homologs of IruO were identified by sequence similarity in the genomes of Gram-positive bacteria that possess IsdG-family heme oxygenases. A phylogeny of these homologs identifies a distinct clade of pyridine nucleotide-disulfide oxidoreductases likely involved in iron uptake systems. IruO is the likely in vivo reductant required for heme degradation by S. aureus.
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