ArticleBiochemistry2016
Chemistry and Molecular Dynamics Simulations of Heme b-HemQ and Coproheme-HemQ.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes.The FEBS journal · 2026Article
- Role of hydrogen sulfide in catalyzing the formation of NO-ferroheme.Nitric oxide : biology and chemistry · 2025Article
- Deciphering the role of the distal pocket in Staphylococcus aureus coproheme decarboxylase.Journal of inorganic biochemistry · 2025Article
- Electrochemical and Spectroscopic Characterization of Co-Neuroglobin: A Bioelectrocatalyst for HInorganic chemistry · 2025Article
- Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme.Biomolecules · 2023Article
- Reorienting Mechanism of Harderoheme in Coproheme Decarboxylase-A Computational Study.International journal of molecular sciences · 2022Article
- Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.Biochimica et biophysica acta. Proteins and proteomics · 2021Review
- X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.The Journal of biological chemistry · 2020Article
- Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.The FEBS journal · 2020Article
- Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation.ACS catalysis · 2020Article
- Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to HemeACS catalysis · 2019Article
- The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis.Journal of inorganic biochemistry · 2019Article
- Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes.Biochemistry · 2018Article
- Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields hemeThe Journal of biological chemistry · 2018Article
- Coproheme decarboxylases - Phylogenetic prediction versus biochemical experiments.Archives of biochemistry and biophysics · 2018Article
- Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.The Journal of biological chemistry · 2017Article
- Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ).Journal of the American Chemical Society · 2017Article
- Reactions of Ferrous Coproheme Decarboxylase (HemQ) with OBiochemistry · 2017Article
- Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.The FEBS journal · 2016Article
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Recently, a novel pathway for heme b biosynthesis in Gram-positive bacteria has been proposed. The final poorly understood step is catalyzed by an enzyme called HemQ and includes two decarboxylation reactions leading from coproheme to heme b. Coproheme has been suggested to act as both substrate and redox active cofactor in this reaction. In the study presented here, we focus on HemQs from Listeria monocytogenes (LmHemQ) and Staphylococcus aureus (SaHemQ) recombinantly produced as apoproteins in Escherichia coli. We demonstrate the rapid and two-phase uptake of coproheme by both apo forms and the significant differences in thermal stability of the apo forms, coproheme-HemQ and heme b-HemQ. Reduction of ferric high-spin coproheme-HemQ to the ferrous form is shown to be enthalpically favored but entropically disfavored with standard reduction potentials of -205 ± 3 mV for LmHemQ and -207 ± 3 mV for SaHemQ versus the standard hydrogen electrode at pH 7.0. Redox thermodynamics suggests the presence of a pronounced H-bonding network and restricted solvent mobility in the heme cavity. Binding of cyanide to the sixth coproheme position is monophasic but relatively slow (∼1 × 10(4) M(-1) s(-1)). On the basis of the available structures of apo-HemQ and modeling of both loaded forms, molecular dynamics simulation allowed analysis of the interaction of coproheme and heme b with the protein as well as the role of the flexibility at the proximal heme cavity and the substrate access channel for coproheme binding and heme b release. Obtained data are discussed with respect to the proposed function of HemQ in monoderm bacteria.
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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.