Heme in pathophysiology: a matter of scavenging, metabolism and trafficking across cell membranes [PDF]
Frontiers in Pharmacology, 2014 Heme (iron-protoporphyrin IX) is an essential co-factor involved in multiple biological processes: oxygen transport and storage, electron transfer, drug and steroid metabolism, signal transduction, and micro RNA processing.
Deborah eChiabrando +4 more
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Hemoglobin Endocytosis and Intracellular Trafficking: A Novel Way of Heme Acquisition by Leishmania
Pathogens, 2022 Leishmania species are causative agents of human leishmaniasis, affecting 12 million people annually. Drugs available for leishmaniasis are toxic, and no vaccine is available. Thus, the major thrust is to identify new therapeutic targets.
Irshad Ansari +2 more
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Heme Gazing: Illuminating Eukaryotic Heme Trafficking, Dynamics, and Signaling with Fluorescent Heme Sensors. [PDF]
Biochemistry, 2017 Heme (iron protoporphyrin IX) is an essential protein prosthetic group and signaling molecule required for most life on Earth. All heme-dependent processes require the dynamic and rapid mobilization of heme from sites of synthesis or uptake to hemoproteins present in virtually every subcellular compartment.
Hanna DA, Martinez-Guzman O, Reddi AR.
europepmc +4 more sources
Intracellular iron and heme trafficking and metabolism in developing erythroblasts. [PDF]
Metallomics, 2017 Vertebrate red blood cells (RBCs) arise from erythroblasts in the human bone marrow through a process known as erythropoiesis.
Kafina MD, Paw BH.
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Regulation of intracellular heme trafficking revealed by subcellular reporters. [PDF]
Proc Natl Acad Sci U S A, 2016 Significance The intracellular and extracellular trafficking of heme, a hydrophobic and potentially cytotoxic cofactor in proteins such as hemoglobin, remains an underexplored area. While cellular heme can be derived exogenously or from de novo synthesis, it is unclear if there is differential trafficking of heme ...
Yuan X +8 more
europepmc +5 more sources
Key roles of GAPDH, Hsp90, and NO in heme trafficking. [PDF]
J Inorg BiochemIntracellular trafficking of mitochondrial heme to create functional heme proteins presents a fundamental challenge in animal cells. This article provides some background on heme allocation, discusses some of the concepts, and then reviews research from the last two decades that has uncovered unexpected and important roles for glyceraldehyde 3 ...
Stuehr DJ +6 more
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A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin. [PDF]
J Biol Chem, 2023 Fusobacterium nucleatum is an opportunistic oral pathogen that is associated with various cancers. To fulfill its essential need for iron, this anaerobe will express heme uptake machinery encoded at a single genetic locus. The heme uptake operon includes HmuW, a class C radical SAM-dependent methyltransferase that degrades heme anaerobically to release
McGregor AK +6 more
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Interaction of holoCcmE with CcmF in heme trafficking and cytochrome c biosynthesis. [PDF]
J Mol Biol, 2014 The periplasmic heme chaperone holoCcmE is essential for heme trafficking in the cytochrome c biosynthetic pathway in many bacteria, archaea, and plant mitochondria. This pathway, called system I, involves two steps: (i) formation and release of holoCcmE (by the ABC-transporter complex CcmABCD) and (ii) delivery of the heme in holoCcmE to the putative ...
San Francisco B, Kranz RG.
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Trafficking of Heme and Porphyrins in Metazoa [PDF]
Chemical Reviews, 2009 A half century ago, Max Perutz and John Kendrew determined the crystal structure of two heme-containing proteins – hemoglobin and myoglobin, respectively 1,2. These landmark discoveries created the foundation for a detailed biochemical understanding of how protein structure influences and affects its ability to bind and carry oxygen. Perutz and Kendrew
Scott, Severance, Iqbal, Hamza
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The CcmC:heme:CcmE complex in heme trafficking and cytochrome c biosynthesis. [PDF]
J Mol Biol, 2010 A superfamily of integral membrane proteins is characterized by a conserved tryptophan-rich region (called the WWD domain) in an external loop at the inner membrane surface. The three major members of this family (CcmC, CcmF, and CcsBA) are each involved in cytochrome c biosynthesis, yet the function of the WWD domain is unknown.
Richard-Fogal C, Kranz RG.
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