Results 21 to 30 of about 11,782 (206)
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.
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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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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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HEME Trafficking by the Cytochrome C Biogenesis Pathways [PDF]
Biophysical Journal, 2017 Cytochromes function in electron transport chains to perform critical cellular functions, such as respiration and photosynthesis. Cytochromes c are unique due to their requirement for the covalent attachment of heme via two thioether bonds at a conserved CXXCH motif. Three pathways have been identified for cytochrome c maturation: System I (prokaryotes)
Molly C. Sutherland +2 more
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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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Ferric reductase-related proteins mediate fungal heme acquisition
eLife, 2022 Heme can serve as iron source in many environments, including the iron-poor animal host environment. The fungal pathobiont Candida albicans expresses a family of extracellular CFEM hemophores that capture heme from host proteins and transfer it across ...
Udita Roy +6 more
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Structures of the CcmABCD heme release complex at multiple states
Nature Communications, 2022 Bacterial ABC transporter complex CcmABCD, a part of cytochrome c maturation system, transfers heme from one binding partner (CcmC) to another (CcmE). Here authors describe high resolution cryo-EM structures of CcmABCD in multiple states and propose a ...
Jiao Li +14 more
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Structural basis of membrane machines that traffick and attach heme to cytochromes
Journal of Biological Chemistry, 2023 We evaluate cryoEM and crystal structures of two molecular machines that traffick heme and attach it to cytochrome c (cyt c), the second activity performed by a cyt c synthase. These integral membrane proteins, CcsBA and CcmF/H, both covalently attach heme to cyt c, but carry it out via different mechanisms.
Jonathan Q. Huynh +2 more
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