The Trypanosoma cruzi Protein TcHTE Is Critical for Heme Uptake. [PDF]
Trypanosoma cruzi, the etiological agent of Chagas' disease, presents nutritional requirements for several metabolites. It requires heme for the biosynthesis of several heme-proteins involved in essential metabolic pathways like mitochondrial cytochromes
Marcelo L Merli +6 more
doaj +1 more source
Protein interactions with heme are vital for pathogenic bacteria, particularly in the utilization of heme as an iron source [PDF]
Iron is an essential nutrient for many pathogenic bacteria, and the most abundant source of the metal in the host is heme. Heme is often degraded by a heme oxygenase, and the first such enzyme (HO-1) was discovered in mammals.
Lyles, Kristin V
core +1 more source
Genome-wide analysis reveals novel genes essential for heme homeostasis in Caenorhabditis elegans. [PDF]
Heme is a cofactor in proteins that function in almost all sub-cellular compartments and in many diverse biological processes. Heme is produced by a conserved biosynthetic pathway that is highly regulated to prevent the accumulation of heme--a cytotoxic,
Scott Severance +7 more
doaj +1 more source
Toxoplasma gondii contains an essential plastid organelle called the apicoplast that is necessary for fatty acid, isoprenoid, and heme synthesis. Perturbations affecting apicoplast function or inheritance lead to parasite death.
Parvathi Madhavi Devarakonda +2 more
doaj +1 more source
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins. [PDF]
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
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 [PDF]
The uptake and utilization of heme as an iron source is a receptor-mediated process in bacterial pathogens and involves a number of proteins required for internalization and degradation of heme. In the following report we provide the first in-depth spectroscopic and functional characterization of a cytoplasmic heme-binding protein PhuS from the ...
Ila B, Lansky +5 more
openaire +2 more sources
Active Turnover of Heme in Hibernation Period in Mammals
Heme oxygenase (HO)-1 plays an important role during hibernation by catalyzing the degradation of heme to biliverdin/bilirubin, ferrous iron, and carbon monoxide, which activates the protective mechanisms against stress. In this context, it was important
Phil Jun Lee +5 more
doaj +1 more source
Cytochrome c Biogenesis: Mechanisms for Covalent Modifications and Trafficking of Heme and for Heme-Iron Redox Control [PDF]
SUMMARY Heme is the prosthetic group for cytochromes, which are directly involved in oxidation/reduction reactions inside and outside the cell. Many cytochromes contain heme with covalent additions at one or both vinyl groups. These include farnesylation at one vinyl in hemes
Robert G, Kranz +3 more
openaire +2 more sources
Genes important for catalase activity in Enterococcus faecalis. [PDF]
Little in general is known about how heme proteins are assembled from their constituents in cells. The Gram-positive bacterium Enterococcus faecalis cannot synthesize heme and does not depend on it for growth.
Michael Baureder, Lars Hederstedt
doaj +1 more source
Iron-tracking strategies: Chaperones capture iron in the cytosolic labile iron pool
Cells express hundreds of iron-dependent enzymes that rely on the iron cofactors heme, iron-sulfur clusters, and mono-or di-nuclear iron centers for activity.
Caroline C. Philpott +6 more
doaj +1 more source

