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Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes

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Aminolevulinic Acid (ALA) as a Prodrug in Photodynamic Therapy of Cancer

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The human flavoproteome

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Lack of heme synthesis in a free-living eukaryote

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Bacterial heme biosynthesis and its biotechnological application

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The Iron Metallome in Eukaryotic Organisms

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Structure and function of radical SAM enzymes

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The Heme Biosynthetic Pathway of the Obligate Wolbachia Endosymbiont of Brugia malayi as a Potential Anti-filarial Drug Target

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Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing

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The Ins and Outs of Iron Homeostasis

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Radical S-Adenosylmethionine Enzyme Coproporphyrinogen III Oxidase HemN

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Structural basis of hereditary coproporphyria

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Crystal Structure of the Oxygen-dependant Coproporphyrinogen Oxidase (Hem13p) of Saccharomyces cerevisiae

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The Substrate Radical of Escherichia coli Oxygen-independent Coproporphyrinogen III Oxidase HemN

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Differential oxidative stress in oligodendrocytes and neurons after excitotoxic insults and protection by natural polyphenols

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A π-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase

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Genomic Characterization of Haemophilus parasuis SH0165, a Highly Virulent Strain of Serovar 5 Prevalent in China

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Porphyrin-Induced Protein Oxidation and Aggregation as a Mechanism of Porphyria-Associated Cell Injury

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Crystal Structure of Protoporphyrinogen Oxidase from Myxococcus xanthus and Its Complex with the Inhibitor Acifluorfen

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Intracellular Trafficking of Porphyrins

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A Novel Pathway for the Biosynthesis of Heme inArchaea: Genome-Based Bioinformatic Predictions and Experimental Evidence

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A conserved haem redox and trafficking pathway for cofactor attachment

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The Heme Synthesis Defect of Mutants Impaired in Mitochondrial Iron-Sulfur Protein Biogenesis Is Caused by Reversible Inhibition of Ferrochelatase

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Structural insight into human variegate porphyria disease

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Structure/Function Studies on a S-Adenosyl-l-methionine-dependent Uroporphyrinogen III C Methyltransferase (SUMT), a Key Regulatory Enzyme of Tetrapyrrole Biosynthesis

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Identification of <i>Escherichia coli</i> HemG as a Novel, Menadione-Dependent Flavodoxin with Protoporphyrinogen Oxidase Activity

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Subcellular Localization and Light-Regulated Expression of Protoporphyrinogen IX Oxidase and Ferrochelatase in Chlamydomonas reinhardtii

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Microarray analysis of zebrafish cloche mutant using amplified cDNA and identification of potential downstream target genes

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Evidence for Horizontal and Vertical Transmission of Mtr-Mediated Extracellular Electron Transfer among the Bacteria

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Heme biosynthesis and its regulation: towards understanding and improvement of heme biosynthesis in filamentous fungi

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An Intercellular Heme-Trafficking Protein Delivers Maternal Heme to the Embryo during Development in C. elegans

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TolC-Dependent Exclusion of Porphyrins in Escherichia coli

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Recent advances in the biosynthesis of modified tetrapyrroles: the discovery of an alternative pathway for the formation of heme and heme d 1

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Structural and functional comparison of HemN to other radical SAM enzymes

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Functional definition of the tobacco protoporphyrinogen IX oxidase substrate-binding site

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Unusual peroxide-dependent, heme-transforming reaction catalyzed by HemQ

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The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis

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Zn protoporphyrin IX is formed not from heme but from protoporphyrin IX

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The Tetrapyrrole Biosynthetic Pathway and Its Regulation in Rhodobacter capsulatus

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The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

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Metal and cofactor insertion

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Evolutionary Aspects and Regulation of Tetrapyrrole Biosynthesis in Cyanobacteria under Aerobic and Anaerobic Environments

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Complex formation between protoporphyrinogen IX oxidase and ferrochelatase during haem biosynthesis in Thermosynechococcus elongatus

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Functional Differentiation of Two Analogous Coproporphyrinogen III Oxidases for Heme and Chlorophyll Biosynthesis Pathways in the Cyanobacterium Synechocystis sp. PCC 6803

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Quantitative expression of candidate genes affecting eggshell color

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Is coproporphyrin III a copper-acquisition compound in Paracoccus denitrificans?

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Two Distinct Roles for Two Functional Cobaltochelatases (CbiK) in Desulfovibrio vulgaris Hildenborough

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Hemoproteins in Dissimilatory Sulfate- and Sulfur-Reducing Prokaryotes

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c -Type Cytochromes in Pelobacter carbinolicus

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Characterisation of Desulfovibrio vulgaris haem b synthase, a radical SAM family member

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Role of YHM1, encoding a mitochondrial carrier protein, in iron distribution of yeast

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Maintenance of small molecule redox homeostasis in mitochondria

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Accumulation ofS-adenosylmethionine induced oligopeptide transporters including BldK to regulate differentiation events inStreptomyces coelicolorM145

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Assessment of a systematic expression profiling approach in ENU-induced mouse mutant lines

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Reactions of Ferrous Coproheme Decarboxylase (HemQ) with O2 and H2O2 Yield Ferric Heme b

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Iron-Sulfur Protein Assembly in Human Cells

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Genomic, morphological, and biochemical analyses of a multi-metal resistant but multi-drug susceptible strain of Bordetella petrii from hospital soil

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The role of coproporphyrinogen III oxidase and ferrochelatase genes in heme biosynthesis and regulation in Aspergillus niger

Franken, A. C. W., Werner, E. R., Haas, H., Lokman, B. C., van den Hondel, C. A. M. J. J., Ram, A. F. J., de Weert, S., & Punt, P. J. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5274-2 · Cited by 21 · see citing works

Dissection of Porphyrin-Induced Conformational Dynamics in the Heme Biosynthesis Enzyme Ferrochelatase

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Iron in yeast: Mechanisms involved in homeostasis

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Sulfate-Reducing Bacteria Reveal a New Branch of Tetrapyrrole Metabolism

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Normal and abnormal heme biosynthesis. Part 7. Synthesis and metabolism of coproporphyrinogen-III analogues with acetate or butyrate side chains on rings C and D. Development of a modified model for the active site of coproporphyrinogen oxidase

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Normal and Abnormal Heme Biosynthesis. 6. Synthesis and Metabolism of a Series of Monovinylporphyrinogens Related to Harderoporphyrinogen. Further Insights into the Oxidative Decarboxylation of Porphyrinogen Substrates by Coproporphyrinogen Oxidase

Lash, T. D., Mani, U. N., Keck, A.-S., & Jones, M. A. (2010) · The Journal of Organic Chemistry · doi:10.1021/jo100083t · Cited by 17 · see citing works

Interactions of apomyoglobin with membranes: Mechanisms and effects on heme uptake

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Cellular Iron Physiology

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Biosynthesis of Heme and Vitamin B12

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The Translocator Protein as a Potential Molecular Target for Improved Treatment Efficacy in Photodynamic Therapy

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Refolding and Enzyme Kinetic Studies on the Ferrochelatase of the Cyanobacterium Synechocystis sp. PCC 6803

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Investigation by MD simulation of the key residues related to substrate-binding and heme-release in human ferrochelatase

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Analysis of human ferrochelatase iron binding via amide hydrogen/deuterium exchange mass spectrometry

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Transformation of Uroporphyrinogen III into Protohaem

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Import of hybrid forms of CYP11A1 into yeast mitochondria

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Structure model of ferrochelatase from Salmonella Typhi elucidating metalation mechanism

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Changes in serum parameters associated with iron metabolism in male rat exposed to lead

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Functional Characterization of Five Protoporphyrinogen oxidase Missense Mutations Found in Argentinean Variegate Porphyria Patients

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Analysis of the differential proteome of human erythroblasts during in vitro erythropoiesis by 2‐D DIGE

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Toxoplasma gondii harbors a hypoxia-responsive coproporphyrinogen dehydrogenase-like protein

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Identification and analysis of the Shewanella oneidensis major oxygen-independent coproporphyrinogen III oxidase gene

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Improving the Production of Cofactor-Containing Proteins: Production of Human Hemoglobin in Yeast

Ishchuk, O. P., Martínez, J. L., & Petranović, D. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9024-5_11 · Cited by 3 · see citing works

ДОНАЦІЇ КРОВІ І МЕТАБОЛІЗМ ЗАЛІЗА

Видиборець, С. В., & Дерпак, Ю. (2022) · Іnternational Science Group eBooks · doi:10.46299/979-8-88831-933-8 · Cited by 3 · see citing works

Characterisation of the flavin adenine dinucleotide binding region of Myxococcus xanthus protoporphyrinogen oxidase

Boateng, M. O., Corrigall, A. V., Sturrock, E. D., & Meissner, P. N. (2015) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2015.10.006 · Cited by 3 · see citing works

Post-Transcriptional Regulation of the Expression of Ferrochelatase by Its Variant mRNA

Sakaino, M., Kataoka, T., & Taketani, S. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp030 · Cited by 3 · see citing works

CPOP1 is a key enzyme required for nodule microenvironment control and successful symbiotic nitrogen fixation in Lotus japonicus

Tian, Y., Luo, Y., Li, Q., Zhang, Z., Guo, Y., & Yang, W. (2025) · Journal of Integrative Plant Biology · doi:10.1111/jipb.70037 · Cited by 2 · see citing works

The Biosynthesis of Hemes, Siroheme, Vitamin B12 and Linear Tetrapyrroles in Pseudomonads

Frankenberg‐Dinkel, N., Schobert, M., Moser, J., Raux, E., Graham, R. M., Warren, M. J., & Jahn, D. (2004) · Springer eBooks · doi:10.1007/978-1-4419-9088-4_4 · Cited by 2 · see citing works

Fe(III) heme sets an activation threshold for processing distinct groups of pri-miRNAs in mammalian cellsPreprint

Weitz, S. H., Quick-Cleveland, J., Jacob, J. P., Barr, I., Senturia, R., Koyano, K., Xiao, X. G., Weiss, S., & Guo, F. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.18.955294 · Cited by 2 · see citing works

CHAPTER 1: Literature review

Roth, C. (2018) · Nomos Verlagsgesellschaft mbH & Co. KG eBooks · doi:10.5771/9783845291000-41 · Cited by 2 · see citing works

Anaerobic bacteria: an investigation of metabolic important enzymes: a novel type of oxygen reductase and enzymes of the tetrapyrrole biosynthesis

Lobo, S. A. L. (2009) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

Heme biosynthesis: structure-activity studies of murine ferrochelatase

Shi, Z. (2006) · Digital Commons - University of South Florida (University of South Florida)

Identification and characterization of a heme responsive element in the hrg-1 promoter

Sinclair, J. W. (2008) · University Libraries (University of Maryland)

Universidad Michoacana de

de Hidalgo, S. N., & Farmacobiología, F. D. Q. (2010)

Structure and Function of Enzymes Involved in Tetrapyrrole Biosynthesis

Heinemann, I. U. (2007) · Digitale Bibliothek Braunschweig (Verbundzentrale Göttingen (VZG)) · doi:10.24355/dbbs.084-200710150200-0

Chapter 2 Mechanism and stereochemistry of the enzymes involved in the conversion of uroporphyrinogen III into haem

Akhtar, M. (1991) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60109-x · Cited by 18 · see citing works

Transformation of Uroporphyrinogen III into Protohaem

Cornah, J. E., & Smith, A. G. (2009) · Springer eBooks · doi:10.1007/978-0-387-78518-9_4 · Cited by 8 · see citing works

Complex formation between protoporphyrinogen IX oxidase and ferrochelatase during haem biosynthesis in Thermosynechococcus elongatus

Masoumi, A., Heinemann, I. U., Rohde, M., Koch, M., Jahn, M., & Jahn, D. (2008) · Microbiology · doi:10.1099/mic.0.2008/018705-0 · Cited by 41 · see citing works

Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis

Al‐Karadaghi, S., HANSSON, M. G., Nikonov, S. V., Jönsson, B., & Hederstedt, L. (1997) · Structure · doi:10.1016/s0969-2126(97)00299-2 · Cited by 186 · see citing works

In situ conversion of coproporphyrinogen to heme by murine mitochondria: Terminal steps of the heme biosynthetic pathway

Proulx, K. L., Woodard, S. I., & Dailey, H. A. (1993) · Protein Science · doi:10.1002/pro.5560020703 · Cited by 48 · see citing works