Results 41 to 50 of about 11,782 (206)
mBio, 2023 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
Iron: Biosynthesis and Significance of Heme [PDF]
, 2015 Heme exists as a prosthetic group in numerous enzymes and other hemeproteins, with which it is involved in oxygen transport and storage, electron transfer reactions, detoxification of xenobiotics, signal transduction, and transcriptional, translational ...
G.O. Latunde-Dada, Latunde-Dada, G. O.
core +1 more source
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]
Journal of Biological Chemistry, 2006 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
Frontiers in Physiology, 2020 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
CytochromecBiogenesis: Mechanisms for Covalent Modifications and Trafficking of Heme and for Heme-Iron Redox Control [PDF]
Microbiology and Molecular Biology Reviews, 2009 SUMMARYHeme 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 hemesoandaand thioether linkages to each vinyl in cytochromec(at CXXCH of the ...
Robert G, Kranz +3 more
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Genes important for catalase activity in Enterococcus faecalis. [PDF]
PLoS ONE, 2012 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
The Role of the Cytoplasmic Heme-binding Protein (PhuS) of Pseudomonas aeruginosa in Intracellular Heme Trafficking and Iron Homeostasis [PDF]
Journal of Biological Chemistry, 2009 The cytoplasmic heme-binding protein PhuS, encoded within the Fur-regulated Pseudomonas heme utilization (phu) operon, has previously been shown to traffic heme to the iron-regulated heme oxygenase (HO). We further investigate the role of PhuS in heme trafficking to HO on disruption of the phuS and hemO genes in a Pseudomonas aeruginosa siderophore ...
Ajinder P, Kaur +2 more
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Mucosal Immunology, 2022 Heme metabolism is a key regulator of inflammatory responses. Cobalt protoporphyrin IX (CoPP) is a heme analog and mimic that potently activates the NRF2/heme oxygenase-1 (HO-1) pathway, especially in monocytes and macrophages. We investigated the influence of CoPP on inflammatory responses using a murine model of colitis.
Rachel E.M. Schaefer +7 more
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Iron-tracking strategies: Chaperones capture iron in the cytosolic labile iron pool
Frontiers in Molecular Biosciences, 2023 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
The Mechanism of Heme Transfer from the Cytoplasmic Heme Binding Protein PhuS to the δ-Regioselective Heme Oxygenase of Pseudomonas aeruginosa† [PDF]
, 2016 The opportunistic pathogen Pseudomonas aeruginosa has evolved two outer membrane receptor-mediated uptake systems (encoded by the phu and has operons) by which it can utilize the hosts heme and hemeproteins as a source of iron. PhuS is a cytoplasmic heme
Mehul N. Bhakta (2526913) +1 more
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