ArticleMetallomics : integrated biometal science2017
Tight binding of heme to Staphylococcus aureus IsdG and IsdI precludes design of a competitive inhibitor.
Article in Metallomics : integrated biometal science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- A periplasmic protein complex mediates arabinofuranosyltransferase activity and intrinsic drug resistance inScience advances · 2026Article
- The roles of Asn7 and Trp67 in tuning the ferryl haem form ofDalton transactions (Cambridge, England : 2003) · 2026Article
- Stabilization of the Ferryl═Oxoheme Form ofJournal of the American Chemical Society · 2025Article
- NosP Detection of Heme ModulatesBiochemistry · 2023Article
- An expandable, modular de novo protein platform for precision redox engineering.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Ruffling is essential for Staphylococcus aureus IsdG-catalyzed degradation of heme to staphylobilin.Journal of inorganic biochemistry · 2022Article
- Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022Review
- Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development.International journal of molecular sciences · 2020Review
- Structure of aBiochemistry · 2019Article
- Spectroscopic Evidence for Electronic Control of Heme Hydroxylation by IsdG.Inorganic chemistry · 2019Article
- Heme catabolism in the causative agent of anthrax.Molecular microbiology · 2019Article
- The heme-sensitive regulator SbnI has a bifunctional role in staphyloferrin B production byThe Journal of biological chemistry · 2019Article
- The affinity of MhuD for heme is consistent with a heme degrading function in vivo.Metallomics : integrated biometal science · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The micromolar equilibrium constants for heme dissociation from IsdG and IsdI reported in the literature call into question whether these enzymes are actually members of the iron-regulated surface determinant system of Staphylococcus aureus, which harvests heme iron from a host during infection. In order to address this question, the heme dissociation constants for IsdG and IsdI were reevaluated using three approaches. The heme dissociation equilibrium constants were measured using a UV/Vis absorption-detected assay analyzed with an assumption-free model, and using a newly developed fluorescence-detected assay. The heme dissociation rate constants were estimated using apomyoglobin competition assays. Analyses of the UV/Vis absorption data revealed a critical flaw in the previous measurements; heme is 99.9% protein-bound at the micromolar concentrations needed for UV/Vis absorption spectroscopy, which renders accurate equilibrium constant measurement nearly impossible. However, fluorescence can be measured for more dilute samples, and analyses of these data resulted in dissociation equilibrium constants of 1.4 ± 0.6 nM and 12.9 ± 1.3 nM for IsdG and IsdI, respectively. Analyses of the kinetic data obtained from apomyoglobin competition assays estimated heme dissociation rate constants of 0.022 ± 0.002 s
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Registered trials
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