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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, Caiyong Chen, Barry H Paw   +2 more
exaly   +3 more sources

Heme dynamics and trafficking factors revealed by genetically encoded fluorescent heme sensors [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2016
SignificanceAll 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 eukaryoteSaccharomyces cerevisiae.
David A Hanna, Osiris Martínez-Guzman, Xiaojing Yuan   +2 more
exaly   +3 more sources

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Heme sensing and trafficking in fungi

Fungal Biology Reviews, 2023
Fungal pathogens cause life-threatening diseases in humans, and the increasing prevalence of these diseases emphasizes the need for new targets for therapeutic intervention. Nutrient acquisition during infection is a promising target, and recent studies highlight the contributions of endomembrane trafficking, mitochondria, and vacuoles in the sensing ...
Peng Xue, Eddy Sánchez-León, Djihane Damoo, Guanggan Hu, Won Hee Jung, James W. Kronstad   +5 more
openaire   +2 more sources

One ring to bring them all and in the darkness bind them: The trafficking of heme without deliverers

Biochimica Et Biophysica Acta - Molecular Cell Research, 2021
Heme, as a hydrophobic iron-containing organic ring, is lipid soluble and can interact with biological membranes. The very same properties of heme that nature exploits to support life also renders heme potentially cytotoxic. In order to utilize heme, while also mitigating its toxicity, cells are challenged to tightly control the concentration and ...
Ian G Chambers, Mathilda M Willoughby, Iqbal Hamza   +2 more
exaly   +3 more sources

Heme requirement and intracellular trafficking in Trypanosoma cruzi epimastigotes

Biochemical and Biophysical Research Communications, 2007
Epimastigotes multiplies in the insect midgut by taking up nutrients present in the blood meal including heme bound to hemoglobin of red blood cell. During blood meal digestion by vector proteases in the posterior midgut, hemoglobin is clipped off into amino acids, peptides, and free heme.
Pedro L Oliveira
exaly   +3 more sources

Heme biosynthesis and trafficking

Free Radical Biology and Medicine, 2018
Heme is an essential cofactor involved in a plethora of vital functions. Heme is required to be in most subcellular compartments, but the way, in which it is transported from the mitochondria - its site of synthesis - to those compartments is poorly understood.
Jonathan Dietz, Oleh Khalimonchuk, Iryna Bohovych, Amit Reddi, Amy Medlock, Osiris Martinez-Guzman   +5 more
openaire   +1 more source

Heme Trafficking and the Importance of Handling Nature’s Most Versatile Cofactor

Chemical Reviews
Heme is one of the most versatile cofactors in nature from its role in oxygen transport and sensing, bioenergetics, and enzyme catalysis and is therefore an ideal regulatory molecule in responding to the redox status of the cell. However, due to both its redox reactivity and hydrophobicity, heme requires tight regulation at the level of its synthesis ...
Angela Wilks
exaly   +3 more sources

Histidine residues are important for preserving the structure and heme binding to the C. elegans HRG-3 heme-trafficking protein

Journal of Biological Inorganic Chemistry, 2015
C. elegans is a heme auxotroph that requires environmental heme for sustenance. As such, worms utilize HRG-3, a small heme-trafficking protein, to traffic heme from the intestine to extra-intestinal tissues and embryos. However, how HRG-3 binds and delivers heme remains unknown.
Iqbal Hamza, Sharon Ruthstein, Hamza Iqbal   +2 more
exaly   +3 more sources

Identification of Two Heme-Binding Sites in the Cytoplasmic Heme-Trafficking Protein PhuS from Pseudomonas aeruginosa and Their Relevance to Function

Biochemistry, 2007
PhuS is a cytoplasmic, 39 kDa heme-binding protein from Pseudomonas aeruginosa. It has previously been shown to transfer heme to its cognate heme oxygenase. It is expressed from the phu operon, which encodes a group of proteins known to actively internalize and transport heme from host organisms. This study combines the spectral resolution of resonance
Darci R, Block, Gudrun S, Lukat-Rodgers, Kenton R, Rodgers, Angela, Wilks, Mehul N, Bhakta, Ila B, Lansky   +5 more
openaire   +2 more sources

Biosynthesis and trafficking of heme o and heme a: new structural insights and their implications for reaction mechanisms and prenylated heme transfer

Critical Reviews in Biochemistry and Molecular Biology, 2021
Elise D Rivett, Lim Heo, Michael Feig
exaly