HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria (original) (raw)

Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin

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Proceedings of the National Academy of Sciences, 2015

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Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product

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The HemQ coprohaem decarboxylase generates reactive oxygen species: implications for the evolution of classical haem biosynthesis

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Hydrogen peroxide‐mediated conversion of coproheme to heme b by HemQ—lessons from the first crystal structure and kinetic studies

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A single mutation converts Alr5027 from cyanobacteria Nostoc sp. PCC 7120 to a heme-binding protein with heme-degrading ability

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Utilization of Heme as an Iron Source by Marine Alphaproteobacteria in the Roseobacter Clade

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Expression of the heme biosynthetic pathway genes hemCD, hemH, hemM and hemA of Escherichia coli

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Co-ordination of iron acquisition, iron porphyrin chelation and iron-protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens

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Hemerythrins in the microaerophilic bacteriumCampylobacter jejunihelp protect key iron-sulphur cluster enzymes from oxidative damage

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Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation

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The Heme Oxygenase(s)-Phytochrome System of Pseudomonas aeruginosa

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A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria

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Marine Alphaproteobacteria in the Utilization of Heme as an Iron Source by

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The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae

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Homologues of Neisserial Heme Oxygenase in Gram-Negative Bacteria: Degradation of Heme by the Product of the pigA Gene of Pseudomonas aeruginosa

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Unusual Heme Binding in the Bacterial Iron Response Regulator Protein: Spectral Characterization of Heme Binding to the Heme Regulatory Motif

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The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX

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Heme O biosynthesis in Escherichia coli: The cyoe gene in the cytochrome BO operon encodes a protoheme IX farnesyltransferase

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Heme Uptake by Microscilla marina and Evidence for Heme Uptake Systems in the Genomes of Diverse Marine Bacteria

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The Cytoplasmic Heme-binding Protein (PhuS) from the Heme Uptake System of Pseudomonas aeruginosa Is an Intracellular Heme-trafficking Protein to the δ-Regioselective Heme Oxygenase

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Discovery of a Gene Involved in a Third Bacterial Protoporphyrinogen Oxidase Activity through Comparative Genomic Analysis and Functional Complementation

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The Cytoplasmic Heme-binding Protein (PhuS) from the Heme Uptake System of Pseudomonas aeruginosa Is an Intracellular Heme-trafficking Protein to the -Regioselective Heme Oxygenase

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Heme proteins and metalloporphyrins: Redox chemistry and oxygen binding

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Plant Heme: Future Approach for Characterizing Hemolytic Bacteria

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Mitochondrial Contact Site and Cristae Organizing System (MICOS) Machinery Supports Heme Biosynthesis by Enabling Optimal Performance of Ferrochelatase

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Organization of the terminal two enzymes of the heme biosynthetic pathway. Orientation of protoporphyrinogen oxidase and evidence for a membrane complex

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Ferreira, G. C., Andrew, T. L., Karr, S. W. & Dailey, H. A. Organization of the terminal two enzymes of the heme biosynthetic pathway. Orientation of protoporphyrinogen oxidase and evidence for a membrane complex. J. Biol. Chem. 263, 3835-3839

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Characterization of heme protein expressed by ammonia-oxidizing bacteria under low dissolved oxygen conditions

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Biophysical Heme Binding Studies of Corynebacterium diphtheriae and Streptococcus pyogenes

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Peroxidase Activity and Involvement in the Oxidative Stress Response of Roseobacter denitrificans Truncated Hemoglobin

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