scholarly journals Genome Mining inStreptomyces. Elucidation of the Role of Baeyer−Villiger Monooxygenases and Non-Heme Iron-Dependent Dehydrogenase/Oxygenases in the Final Steps of the Biosynthesis of Pentalenolactone and Neopentalenolactone

Biochemistry ◽  
2011 ◽  
Vol 50 (10) ◽  
pp. 1739-1754 ◽  
Author(s):  
Myung-Ji Seo ◽  
Dongqing Zhu ◽  
Saori Endo ◽  
Haruo Ikeda ◽  
David E. Cane
Keyword(s):  
Genome Mining ◽  
Heme Iron ◽  
Non Heme Iron

scholarly journals The role of dietary non-heme iron load and peripheral nerve inflammation in the development of peripheral neuropathy (PN) in obese non-diabetic leptin-deficient ob/ob mice

2019 ◽  
Vol 41 (4) ◽  
pp. 341-353 ◽  
Author(s):  
Joanna Kosacka ◽  
Katrin Woidt ◽  
Klaus V. Toyka ◽  
Sabine Paeschke ◽  
Nora Klöting ◽  
...  
Keyword(s):  
Peripheral Neuropathy ◽  
Peripheral Nerve ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Iron Load

Role of non-heme iron in the physiology and pathophysiology of NO

1994 ◽  
Vol 1 ◽  
pp. 19
Author(s):  
A. Mülsch ◽  
M. Böse ◽  
P. Mordvintcev ◽  
R. Busse
Keyword(s):  
Heme Iron ◽  
Non Heme Iron

Special Delivery: The Role of Iron Chaperones in the Distribution of Iron in Developing Red Cells

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. SCI-45-SCI-45
Author(s):  
Caroline C. Philpott ◽  
Avery G Frey ◽  
Moon-Suhn Ryu ◽  
Daniel Palenchar ◽  
Justin Wildemann ◽  
...  
Keyword(s):  
Heme Iron ◽  
Human Cells ◽  
Erythroid Cell ◽  
Iron Sulfur Clusters ◽  
Non Heme Iron ◽  
Iron Sulfur ◽  
Iron Enzymes ◽  
Dinuclear Iron ◽  
Iron Delivery

Abstract Iron is an essential nutrient for every cell in the human body, yet it can also be a potent cellular toxin. Iron is essential because enzymes that require iron co-factors (namely, heme, iron-sulfur clusters, mononuclear and diiron centers) are involved in virtually every major metabolic process in the cell. Hundreds of iron, zinc, copper, and manganese proteins are expressed in human cells, yet little is known about the mechanisms by which these metalloproteins acquire their native metal ligands and avoid mis-metallation. Significant advances have been made in understanding the delivery of iron to iron-dependent enzymes in the cytosol. Poly(rC)-binding proteins (PCBPs) are multifunctional adaptors that mediate interactions between single-stranded nucleic acids, iron cofactors, and other proteins, affecting the fate and activity of the components of these interactions. PCBP1 is an iron-binding protein that delivers iron to ferritin in human cells via a direct protein-protein interaction and can be described as an iron chaperone. PCBP2, a human paralog of PCBP1, is also involved in the delivery of iron to ferritin, both in yeast cells and in human cells, suggesting that PCBP1 and PCBP2 work together in iron delivery. PCBP1 and PCBP2 can also deliver iron to the two major families of non-heme iron enzymes: the mononuclear and dinuclear iron-dependent oxygenases. The prolyl hydroxylases (PHDs) are mononuclear iron enzymes that regulate the degradation of hypoxia inducible factor 1 (HIF1). Misregulation of the HIF transcription factors leads to the development of a variety of cancers in humans. Cells depend on the iron chaperones PCBP1 and PCBP2 to maintain iron in the enzymatic active site of PHDs and the related enzyme, asparagyl hydroxylase and to maintain proper regulation of HIF1a, especially under conditions of iron limitation. Deoxyhypusine hydroxylase (DOHH) is a dinuclear iron enzyme that is required for the posttranslational modification of a single lysine residue on eukaryotic initiation factor 5A (eIF5A). EIF5A and the conversion of this conserved lysine to hypusine are essential in all eukaryotes, as it enables the translation of peptides containing polyproline sequences. We found that cells depleted of PCBP1 or PCBP2 exhibited reduced activity of DOHH, which was due to a loss of iron in the active site of the enzyme. Thus, PCBPs are basic components of a cytosolic iron delivery system that serves both of the major classes of non-heme iron enzymes in the cytosol. Recent work has indicated that a second type of iron delivery system in the cytosol is mediated by a monothiol glutaredoxin, Glrx3, which, in vitro, can bind and transfer iron-sulfur clusters to recipient apo-iron-sulfur proteins. We have determined that PCBP1 directly interacts with Glrx3-containing complexes and can affect the coordination of iron-sulfur clusters by Glrx3. The huge flux of iron through the developing erythroid cell represents unique challenges for the utilization of cellular iron. We have examined the role of PCBPs as iron chaperones in terminal erythroid differentiation. The role of ferritin in erythroid cell maturation is controversial, but our data indicate that ferritin, PCBPs and NCOA4 are critical factors in erythrocyte development. The flux of iron through ferritin via the lysosome appears to be critical for the transfer of iron to mitochondria for heme synthesis. Disclosures No relevant conflicts of interest to declare.

scholarly journals Role of the Nitric Oxide (NO) in the Regulation of Steroidogenesis in Placenta During Physiological Pregnancy and Preeclampsia (Experimental Study)

2019 ◽  
Vol 42 (1) ◽  
pp. 1-11
Author(s):  
Tamar V. Sanikidze ◽  
Levan A. Cheishvili ◽  
Nana V. Kipiani ◽  
Eka R. Shekiladze ◽  
Nina V. Kipiani ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Transport Proteins ◽  
Heme Iron ◽  
Paramagnetic Resonance ◽  
Non Heme Iron ◽  
Last Stage ◽  
Electron Transport Proteins ◽  
Electron Paramagnetic ◽  
Dependent Mechanism

AbstractThe aim of the study was to establish the role of nitric oxide (NO) in the regulation of steroidogenesis in the placenta during physiological pregnancy and experimental preeclampsia (PE) in rats. EPR centers of the placenta, free NO and its metabolites were determined by the Electron Paramagnetic Resonance (EPR) method. At the last stage of pregnancy in the EPR spectra of the rats’ placenta with PE alterations of the signals intensity of mitochondrial steroidogenic electron transport proteins were detected: the FeS-centers of adrenodoxin decreased, the ferricytochrome P-450 increased, the free NO content decreased, and the complexes of NO with heme (HbNO) and non-heme iron (FeSNO) were detected. These data indicate the violation of placental steroidogenesis, which is confirmed by a decrease in the level of progesterone in blood. Therefore, the nitrosylation of mitochondrial proteins is an important redox-dependent mechanism of regulation of the intensity of steroidogenesis.

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