Results 21 to 30 of about 11,485 (176)
Iron and Porphyrin Trafficking in Heme Biogenesis [PDF]
Journal of Biological Chemistry, 2010 Iron is an essential element for diverse biological functions. In mammals, the majority of iron is enclosed within a single prosthetic group: heme. In metazoans, heme is synthesized via a highly conserved and coordinated pathway within the mitochondria.
Iman J, Schultz +3 more
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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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Heme dynamics and trafficking factors revealed by genetically encoded fluorescent heme sensors [PDF]
Proceedings of the National Academy of Sciences, 2016 Significance All heme-dependent functions require the mobilization of labile heme (LH), of which there is little understanding of its nature and dynamics. To probe LH pools, we developed genetically encoded fluorescent heme sensors and deployed them in the unicellular eukaryote Saccharomyces ...
David A, Hanna +8 more
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Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins. [PDF]
Biochemistry, 2016 Cytochromes c require covalent attachment of heme via two thioether bonds at conserved CXXCH motifs, a process accomplished in prokaryotes by eight integral membrane proteins (CcmABCDEFGH), termed System I. Heme is trafficked from inside the cell to outside (via CcmABCD) and chaperoned (holoCcmE) to the cytochrome c synthetase (CcmF/H). Purification of
Sutherland MC, Rankin JA, Kranz RG.
europepmc +4 more sources
From Synthesis to Utilization: The Ins and Outs of Mitochondrial Heme
Cells, 2020 Heme is a ubiquitous and essential iron containing metallo-organic cofactor required for virtually all aerobic life. Heme synthesis is initiated and completed in mitochondria, followed by certain covalent modifications and/or its delivery to apo ...
Samantha A. Swenson +5 more
doaj +1 more source
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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Identification of the Mitochondrial Heme Metabolism Complex. [PDF]
PLoS ONE, 2015 Heme is an essential cofactor for most organisms and all metazoans. While the individual enzymes involved in synthesis and utilization of heme are fairly well known, less is known about the intracellular trafficking of porphyrins and heme, or regulation ...
Amy E Medlock +6 more
doaj +1 more source
Structure-Function Analysis of the Bifunctional CcsBA Heme Exporter and Cytochrome
mBio, 2018 Although intracellular heme trafficking must occur for heme protein assembly, only a few heme transporters have been unequivocally discovered and nothing is known about their structure or mechanisms.
Molly C. Sutherland +5 more
doaj +1 more source
Heme Oxygenase-1 Regulates Myeloid Cell Trafficking in AKI [PDF]
Journal of the American Society of Nephrology, 2015 Renal ischemia-reperfusion injury is mediated by a complex cascade of events, including the immune response, that occur secondary to injury to renal epithelial cells. We tested the hypothesis that heme oxygenase-1 (HO-1) expression, which is protective in ischemia-reperfusion injury, regulates trafficking of myeloid-derived immune cells in the kidney ...
Travis D, Hull +10 more
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Genetic screens reveal CCDC115 as a modulator of erythroid iron and heme trafficking [PDF]
American Journal of Hematology, 2020 AbstractTransferrinâbound iron (TBI), the physiological circulating iron form, is acquired by cells through the transferrin receptor (TfR1) by endocytosis. In erythroid cells, most of the acquired iron is incorporated into heme in the mitochondria. Cellular trafficking of heme is indispensable for erythropoiesis and many other essential biological ...
Amin Sobh +9 more
openaire +2 more sources