ArticleThe Journal of biological chemistry2016
Time-resolved Studies of IsdG Protein Identify Molecular Signposts along the Non-canonical Heme Oxygenase Pathway.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- The roles of Asn7 and Trp67 in tuning the ferryl haem form ofDalton transactions (Cambridge, England : 2003) · 2026Article
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Stabilization of the Ferryl═Oxoheme Form ofJournal of the American Chemical Society · 2025Article
- Second-sphere tuning of analogues for the ferric-hydroperoxoheme form of Mycobacterium tuberculosis MhuD.Journal of inorganic biochemistry · 2023Article
- Ruffling is essential for Staphylococcus aureus IsdG-catalyzed degradation of heme to staphylobilin.Journal of inorganic biochemistry · 2022Article
- Spectroscopic Evidence for Electronic Control of Heme Hydroxylation by IsdG.Inorganic chemistry · 2019Article
- A Single Mutation in the Mycobacterium tuberculosis Heme-Degrading Protein, MhuD, Results in Different Products.Biochemistry · 2019Article
- Iron Acquisition in Mycobacterium tuberculosis.Chemical reviews · 2019Review
- Fur regulation of Staphylococcus aureus heme oxygenases is required for heme homeostasis.International journal of medical microbiology : IJMM · 2018Article
- From Host Heme To Iron: The Expanding Spectrum of Heme Degrading Enzymes Used by Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2018Review
- 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
- The Effectors and Sensory Sites of Formaldehyde-responsive Regulator FrmR and Metal-sensing Variant.The Journal of biological chemistry · 2016Article
- Monooxygenase Substrates Mimic Flavin to Catalyze Cofactorless Oxygenations.The Journal of biological chemistry · 2016Article
- Transcriptomic analysis illuminates genes involved in chlorophyll synthesis after nitrogen starvation in Acaryochloris sp. CCMEE 5410.Photosynthesis research · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
IsdGs are heme monooxygenases that break open the tetrapyrrole, releasing the iron, and thereby allowing bacteria expressing this protein to use heme as a nutritional iron source. Little is currently known about the mechanism by which IsdGs degrade heme, although the products differ from those generated by canonical heme oxygenases. A synthesis of time-resolved techniques, including in proteo mass spectrometry and conventional and stopped-flow UV/visible spectroscopy, was used in conjunction with analytical methods to define the reaction steps mediated by IsdG from Staphylococcus aureus and their time scales. An apparent meso-hydroxyheme (forming with k = 0.6 min(-1), pH 7.4, 10 mm ascorbate, 10 μm IsdG-heme, 22 °C) was identified as a likely common intermediate with the canonical heme oxygenases. Unlike heme oxygenases, this intermediate does not form with added H2O2 nor does it convert to verdoheme and CO. Rather, the next observable intermediates (k = 0.16 min(-1)) were a set of formyloxobilin isomers, similar to the mycobilin products of the IsdG homolog from Mycobacterium tuberculosis (MhuD). These converted in separate fast and slow phases to β-/δ-staphylobilin isomers and formaldehyde (CH2O). Controlled release of this unusual C1 product may support IsdG's dual role as both an oxygenase and a sensor of heme availability in S. aureus.
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