ArticleThe Journal of biological chemistry2012
Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 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
- A Dynamic Substrate is Required for MhuD-Catalyzed Degradation of Heme to Mycobilin.Biochemistry · 2021Article
- Spectroscopic Evidence for Electronic Control of Heme Hydroxylation by IsdG.Inorganic chemistry · 2019Article
- Iron Acquisition in Mycobacterium tuberculosis.Chemical reviews · 2019Review
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Monooxygenase Substrates Mimic Flavin to Catalyze Cofactorless Oxygenations.The Journal of biological chemistry · 2016Article
- Evolutionary relationships between heme-binding ferredoxin α + β barrels.BMC bioinformatics · 2016Article
- Structure-based Mechanistic Insights into Terminal Amide Synthase in Nosiheptide-Represented Thiopeptides Biosynthesis.Scientific reports · 2015Article
- 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
- Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme.Archives of biochemistry and biophysics · 2015Review
- Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.Accounts of chemical research · 2014Article
- Crystallographic and spectroscopic insights into heme degradation by Mycobacterium tuberculosis MhuD.Inorganic chemistry · 2014Article
- IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus.The Journal of infectious diseases · 2014Article
- Article
- The influence of heme ruffling on spin densities in ferricytochromes c probed by heme core 13C NMR.Inorganic chemistry · 2013Article
- IruO is a reductase for heme degradation by IsdI and IsdG proteins in Staphylococcus aureus.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
IsdG and IsdI are paralogous heme degrading enzymes from the bacterium Staphylococcus aureus. Heme bound by these enzymes is extensively ruffled such that the meso-carbons at the sites of oxidation are distorted toward bound oxygen. In contrast, the canonical heme oxygenase family degrades heme that is bound with minimal distortion. Trp-66 is a conserved heme pocket residue in IsdI implicated in heme ruffling. IsdI variants with Trp-66 replaced with residues having less bulky aromatic and alkyl side chains were characterized with respect to catalytic activity, heme ruffling, and electrochemical properties. The heme degradation activity of the W66Y and W66F variants was approximately half that of the wild-type enzyme, whereas the W66L and W66A variants were inactive. A crystal structure and NMR spectroscopic analysis of the W66Y variant reveals that heme binds to this enzyme with less heme ruffling than observed for wild-type IsdI. The reduction potential of this variant (-96 ± 7 mV versus standard hydrogen electrode) is similar to that of wild-type IsdI (-89 ± 7 mV), so we attribute the diminished activity of this variant to the diminished heme ruffling observed for heme bound to this enzyme and conclude that Trp-66 is required for optimal catalytic activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.