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Heme iron

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https://www.readbyqxmd.com/read/28819889/visualization-of-57-fe-labeled-heme-isotopic-fine-structure-and-localization-of-regions-of-erythroblast-maturation-in-mouse-spleen-by-maldi-fticr-ms-imaging
#1
Makoto Kihara, Yukari Matsuo-Tezuka, Mariko Noguchi-Sasaki, Keigo Yorozu, Mitsue Kurasawa, Yasushi Shimonaka, Michinori Hirata
Epoetin beta pegol (continuous erythropoiesis receptor activator; C.E.R.A.), or methoxy-polyethylene glycol-modified epoetin beta, is a long-acting erythropoiesis stimulating agent (ESA) that effectively maintains hemoglobin levels. It promotes proliferation of erythroid progenitor cells in hematopoietic organs and leads to increased reticulocyte and hemoglobin levels. However, the detailed erythropoietic effects of various ESAs on their target organs have yet to be clarified, and new approaches are needed to analyze tissue iron localization with structural information...
August 17, 2017: Journal of the American Society for Mass Spectrometry
https://www.readbyqxmd.com/read/28815214/chlamydomonas-reinhardtii-lfo1-is-an-isdg-family-heme-oxygenase
#2
Lisa J Lojek, Allison J Farrand, Jennifer H Wisecaver, Crysten E Blaby-Haas, Brian W Michel, Sabeeha S Merchant, Antonis Rokas, Eric P Skaar
Heme is essential for respiration across all domains of life. However, heme accumulation can lead to toxicity if cells are unable to either degrade or export heme or its toxic by-products. Under aerobic conditions, heme degradation is performed by heme oxygenases, enzymes which utilize oxygen to cleave the tetrapyrrole ring of heme. The HO-1 family of heme oxygenases has been identified in both bacterial and eukaryotic cells, whereas the IsdG family has thus far been described only in bacteria. We identified a hypothetical protein in the eukaryotic green alga Chlamydomonas reinhardtii, which encodes a protein containing an antibiotic biosynthesis monooxygenase (ABM) domain consistent with those associated with IsdG family members...
July 2017: MSphere
https://www.readbyqxmd.com/read/28808058/reductions-in-the-mitochondrial-abc-transporter-abcb10-affect-the-transcriptional-profile-of-heme-biosynthesis-genes
#3
Alexandra Seguin, Naoko Takahashi-Makise, Yvette Y Yien, Nicholas C Huston, Jared C Whitman, Gabriel Musso, Jared A Wallace, Thomas Bradley, Hector Bergonia, Martin D Kafina, Mitsuyo Matsumoto, Kazuhiko Igarashi, John D Phillips, Barry H Paw, Jerry Kaplan, Diane M Ward
ATP-binding cassette subfamily B member 10 (Abcb10) is a mitochondrial ABC transporter that complexes with mitoferrin1 and ferrochelatase to enhance heme biosynthesis in developing red blood cells. Reductions in Abcb10 levels have been shown to reduce mitoferrin1 protein levels and iron import into mitochondria resulting in reduced heme biosynthesis. As an ABC transporter, Abcb10 binds and hydrolyzes ATP, but its transported substrate is unknown. Here, we determined that decreases in Abcb10 did not result in protoporphyrin IX accumulation in morphant treated zebrafish embryos nor in differentiated Abcb10-specific shRNA murine Friend erythroleukemia (MEL) cells in which Abcb10 was specifically silenced with shRNA...
August 14, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28795723/intracellular-iron-and-heme-trafficking-and-metabolism-in-developing-erythroblasts
#4
Martin D Kafina, Barry H Paw
Vertebrate red blood cells (RBCs) arise from erythroblasts in the human bone marrow through a process known as erythropoiesis. Iron uptake is a crucial hallmark, essential for heme biosynthesis in the differentiating erythroblasts, which are dedicated to producing hemoglobin. Erythropoiesis is facilitated by a network of intracellular transport proteins, chaperones, and circulating hormones. Intracellular iron is targeted to the mitochondria for incorporation into a porphyrin ring to form heme and cytosolic iron-sulfur proteins, including Iron Regulatory Protein 1 (IRP1)...
August 10, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28794014/iron-affects-ire1-clustering-propensity-and-the-amplitude-of-endoplasmic-reticulum-stress-signaling
#5
Nir Cohen, Michal Breker, Anush Bakunts, Kristina Pesek, Ainara Chas, Josepmaria Argemí, Andrea Orsi, Lihi Gal, Silvia Chuartzman, Yoav Wigelman, Felix Jonas, Peter Walter, Robert Ernst, Tomás Aragón, Eelco van Anken, Maya Schuldiner
The unfolded protein response (UPR) allows cells to adjust secretory pathway capacity according to need. Ire1, the endoplasmic reticulum (ER) stress sensor and central activator of the UPR is conserved from the budding yeast Saccharomyces cerevisiae to humans. Under ER stress conditions, Ire1 clusters into foci that enable optimal UPR activation. To discover factors that affect Ire1 clustering, we performed a high-content screen using a whole-genome yeast mutant library expressing Ire1-mCherry. We imaged the strains following UPR induction and found 154 strains that displayed alterations in Ire1 clustering...
August 9, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28793787/the-roles-of-nrf2-in-modulating-cellular-iron-homeostasis
#6
Michael John Kerins, Aikseng Ooi
SIGNIFICANCE: Iron and oxygen are intimately linked: iron is an essential nutrient utilized as a cofactor in enzymes for oxygen transport, oxidative phosphorylation, and metabolite oxidation. However, excess labile iron facilitates the formation of oxygen-derived free radicals capable of damaging biomolecules. Therefore, biological utilization of iron is a tightly regulated process. The nuclear factor (erythroid-derived 2)-like 2 (NRF2) transcription factor, which can respond to oxidative and electrophilic stress, regulates several genes involved in iron metabolism...
August 10, 2017: Antioxidants & Redox Signaling
https://www.readbyqxmd.com/read/28791741/molecular-dynamics-study-on-the-apo-and-holo-forms-of-5-lipoxygenase
#7
Juan Torras, Mauro Maccarrone, Enrico Dainese
Lipoxygenases (LOXs) are non-heme iron containing enzymes catalyzing the dioxygenation of polyunsaturated fatty acids. LOX catalytic activity depends on the presence of iron in the active site and the iron removal is also able to affect the membrane binding properties of the enzyme. Leukotrienes biosynthesis is initiated by the action of 5-LOX at the level of nuclear membrane and the mechanism of enzyme-membrane interaction is thought to involve structural flexibility and conformational changes at the level of the protein tertiary structure...
August 8, 2017: Biotechnology and Applied Biochemistry
https://www.readbyqxmd.com/read/28790371/unraveling-heme-detoxification-in-the-malaria-parasite-by-in-situ-correlative-x-ray-fluorescence-microscopy-and-soft-x-ray-tomography
#8
Sergey Kapishnikov, Daniel Grolimund, Gerd Schneider, Eva Pereiro, James G McNally, Jens Als-Nielsen, Leslie Leiserowitz
A key drug target for malaria has been the detoxification pathway of the iron-containing molecule heme, which is the toxic byproduct of hemoglobin digestion. The cornerstone of heme detoxification is its sequestration into hemozoin crystals, but how this occurs remains uncertain. We report new results of in vivo rate of heme crystallization in the malaria parasite, based on a new technique to measure element-specific concentrations at defined locations in cell ultrastructure. Specifically, a high resolution correlative combination of cryo soft X-ray tomography has been developed to obtain 3D parasite ultrastructure with cryo X-ray fluorescence microscopy to measure heme concentrations...
August 8, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28771589/structural-and-mutational-analyses-of-the-leptospira-interrogans-virulence-related-heme-oxygenase-provide-insights-into-its-catalytic-mechanism
#9
Anabel Soldano, Sebastián Klinke, Lisandro H Otero, Mario Rivera, Daniela L Catalano-Dupuy, Eduardo A Ceccarelli
Heme oxygenase from Leptospira interrogans is an important virulence factor. During catalysis, redox equivalents are provided to this enzyme by the plastidic-type ferredoxin-NADP+ reductase also found in L. interrogans. This process may have evolved to aid this bacterial pathogen to obtain heme-iron from their host and enable successful colonization. Herein we report the crystal structure of the heme oxygenase-heme complex at 1.73 Å resolution. The structure reveals several distinctive features related to its function...
2017: PloS One
https://www.readbyqxmd.com/read/28769992/salivary-proline-rich-protein-may-reduce-tannin-iron-chelation-a-systematic-narrative-review
#10
REVIEW
Nicole M Delimont, Sara K Rosenkranz, Mark D Haub, Brian L Lindshield
BACKGROUND: Tannins are often cited for antinutritional effects, including chelation of non-heme iron. Despite this, studies exploring non-heme iron bioavailability inhibition with long-term consumption have reported mixed results. Salivary proline-rich proteins (PRPs) may mediate tannin-antinutritional effects on non-heme iron bioavailability. AIM: To review evidence regarding biochemical binding mechanisms and affinity states between PRPs and tannins, as well as effects of PRPs on non-heme iron bioavailability with tannin consumption in vivo...
2017: Nutrition & Metabolism
https://www.readbyqxmd.com/read/28768416/manganese-and-cobalt-in-the-nonheme-metal-binding-site-of-a-biosynthetic-model-of-heme-copper-oxidase-superfamily-confer-oxidase-activity-through-redox-inactive-mechanism
#11
Julian H Reed, Yelu Shi, Qianhong Zhu, Saumen Chakraborty, Evan N Mirts, Igor D Petrik, Ambika Bhagi-Damodaran, Matthew Ross, Pierre Moënne-Loccoz, Yong Zhang, Yi Lu
The presence of nonheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzymatic activity of reducing O2 to H2O, but the exact mechanism the nonheme metal ion uses to confer and fine-tune the activity remains to be understood. We report that manganese and cobalt can bind to the same nonheme site and confer HCO activity in a heme-nonheme biosynthetic model in myoglobin. While the initial rates of O2 reduction by the Mn, Fe and Co derivatives are similar, the percentage of reaction active species formation are 7%, 4% and 1% and the total turnovers are 5...
August 3, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28760705/adaptation-to-metabolic-dysfunction-during-aging-making-the-best-of-a-bad-situation
#12
REVIEW
S Michal Jazwinski, James C Jiang, Sangkyu Kim
Mitochondria play a central role in energy metabolism in the process of oxidative phosphorylation. As importantly, they are key in several anabolic processes, including amino acid biosynthesis, nucleotide biosynthesis, heme biosynthesis, and the formation of iron‑sulfur clusters. Mitochondria are also engaged in waste removal in the urea cycle. Their activity can lead to the formation of reactive oxygen species which have damaging effects in the cell. These organelles are dynamic, undergoing cycles of fission and fusion which can be coupled to their removal by mitophagy...
July 29, 2017: Experimental Gerontology
https://www.readbyqxmd.com/read/28760394/molecular-structure-of-foxe-the-putative-iron-oxidase-of-rhodobacter-ferrooxidans-sw2
#13
Luis Pereira, Ivo H Saraiva, A Sofia F Oliveira, Cláudio M Soares, Ricardo O Louro, Carlos Frazão
The ancient metabolism of photoferrotrophy is likely to have played a key role in the biogeochemical cycle of iron on Early Earth leading to the deposition of Banded Iron Formations prior to the emergence of oxygenic photosynthesis. Extant organisms still performing this metabolism provide a convenient window to peer into its molecular mechanisms. Here we report the molecular structure of FoxE, the putative terminal iron oxidase of Rhodobacter ferrooxidans SW2. This protein is organized as a trimer with two hemes and a disulfide bridge per monomer...
July 29, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28759066/structural-changes-and-picosecond-to-second-dynamics-of-cytochrome-c-in-interaction-with-nitric-oxide-in-ferrous-and-ferric-redox-states
#14
Sergei G Kruglik, Byung-Kuk Yoo, Jean-Christophe Lambry, Jean-Louis Martin, Michel Negrerie
Apart from its role in electron transfer, mitochondrial cytochrome c also plays a role in apoptosis and is subject to nitrosylation. The cleavage of the Fe-Met80 bond plays a role in several processes including the release of Cyt c from mitochondria or increase of its peroxidase activity. Nitrosylation of Cyt c precludes the reformation of the disrupted Fe-Met80 bond and was shown to occur during apoptosis. These physiological properties are associated with a conformational change of the heme center of Cyt c...
August 16, 2017: Physical Chemistry Chemical Physics: PCCP
https://www.readbyqxmd.com/read/28758386/active-sites-of-o2-evolving-chlorite-dismutases-probed-by-halides-hydroxides-and-new-iron-ligand-vibrational-correlations
#15
Zachary Geeraerts, Kenton R Rodgers, Jennifer DuBois, Gudrun S Lukat-Rodgers
O2-evolving chlorite dismutases (Clds) fall into two subfamilies, which efficiently convert ClO2(-) to O2 and Cl(-). The Cld from Dechloromonas aromatica (DaCld) represents the chlorite-decomposing homopentameric enzymes found in perchlorate and chlorate respiring bacteria. The Cld from the Gram-negative, human pathogen Klebsiella pneumoniae (KpCld) is representative of the second subfamily, comprising homodimeric enzymes having truncated N-termini. Here steric and nonbonding properties of the DaCld and KpCld active sites have been probed via kinetic, thermodynamic and spectroscopic behaviors of their fluorides, chlorides and hydroxides...
July 31, 2017: Biochemistry
https://www.readbyqxmd.com/read/28756878/heme-oxygenase-1-a-new-druggable-target-in-the-management-of-chronic-and-acute-myeloid-leukemia
#16
REVIEW
Loredana Salerno, Giuseppe Romeo, Maria N Modica, Emanuele Amata, Valeria Sorrenti, Ignazio Barbagallo, Valeria Pittalà
Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin. By means of these catabolic end-products and by removal of pro-oxidant heme, HO-1 exerts antioxidant, antiapoptotic, and immune-modulating effects, leading to overall cytoprotective and beneficial functions in mammalian cells. Therefore, HO-1 is considered a survival molecule in various stress-related conditions...
July 20, 2017: European Journal of Medicinal Chemistry
https://www.readbyqxmd.com/read/28756660/spectroscopy-and-dft-calculations-of-a-flavo-diiron-enzyme-implicate-new-diiron-site-structures
#17
Andrew C Weitz, Nitai Giri, Jonathan D Caranto, Donald M Kurtz, Emile L Bominaar, Michael P Hendrich
Flavo-diiron proteins (FDPs) are non-heme iron containing enzymes that are widespread in anaerobic bacteria, archaea, and protozoa, serving as the terminal components to dioxygen and nitric oxide reductive scavenging pathways in these organisms. FDPs contain a dinuclear iron active site similar to that in hemerythrin, ribonucleotide reductase, and methane monooxygenase, all of which can bind NO and O2. However, only FDP competently turns over NO to N2O. Here, EPR and Mössbauer spectroscopies allow electronic characterization of the diferric and diferrous species of FDP...
August 16, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28746897/parkinsonian-features-in-aging-gfap-hmox1-transgenic-mice-overexpressing-human-ho-1-in-the-astroglial-compartment
#18
Wei Song, Marisa Cressatti, Hillel Zukor, Adrienne Liberman, Carmela Galindez, Hyman M Schipper
Epigenetic influences mediating brain iron deposition, oxidative mitochondrial injury, and macroautophagy in Parkinson disease and related conditions remain enigmatic. Here, we show that selective overexpression of the stress protein, heme oxygenase-1 (HO-1) in astrocytes of GFAP.HMOX1 transgenic mice between 8.5 and 19 months of age results in nigrostriatal hypodopaminergia associated with locomotor incoordination and stereotypy; downregulation of tyrosine hydroxylase, DAT, LMX1B, Nurr1, Pitx3 and DJ-1 mRNA and/or protein; overproduction of α-synuclein and ubiquitin; oxidative stress; basal ganglia siderosis; mitochondrial damage/mitophagy; and augmented GABAergic systems (increased GABA, GAD67 and reelin)...
June 28, 2017: Neurobiology of Aging
https://www.readbyqxmd.com/read/28746878/the-type-vi-secretion-system-engages-a-redox-regulated-dual-functional-heme-transporter-for-zinc-acquisition
#19
Meiru Si, Yao Wang, Bing Zhang, Chao Zhao, Yiwen Kang, Haonan Bai, Dawei Wei, Lingfang Zhu, Lei Zhang, Tao G Dong, Xihui Shen
The type VI secretion system was recently reported to be involved in zinc acquisition, but the underlying mechanism remains unclear. Here, we report that Burkholderia thailandensis T6SS4 is involved in zinc acquisition via secretion of a zinc-scavenging protein, TseZ, that interacts with the outer membrane heme transporter HmuR. We find that HmuR is a redox-regulated dual-functional transporter that transports heme iron under normal conditions but zinc upon sensing extracellular oxidative stress, triggered by formation of an intramolecular disulfide bond...
July 25, 2017: Cell Reports
https://www.readbyqxmd.com/read/28731922/a-novel-g-55040074delt-in-alas2-gene-resulting-in-a-monomeric-protein-and-severe-sideroblastic-anemia-phenotype
#20
Prateek Bhatia, Aditya Singh, Avani Hedge
Sideroblastic anemias are a rare group of disorders resulting from defective iron incorporation during heme synthesis and hence characterized by anemia and presence of ringed sideroblasts in bone marrow. The most common form is an X-linked disorder caused by mutations in ALAS2 gene. In the current paper, a case of X-linked sideroblastic anemia caused by a novel homozygous deletional mutation in exon 10 of ALAS2 gene is presented. The female infant developed moderately severe anemia at 6 months of age, which did not improve despite adequate nutritional support...
August 2017: Journal of Pediatric Hematology/oncology
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