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  • Biosynthesis
  • Here, we present the discovery of two non-heme iron- and α-ketoglutarate-dependent enzymes that carry out atypical reactions, C-C bond formation and epimerization, in nogalamycin biosynthesis. (pnas.org)
  • Here, we show that the unusual C5′′-C2 carbocyclization is catalyzed by the non-heme iron α-ketoglutarate (α-KG)-dependent SnoK in the biosynthesis of the anthracycline nogalamycin. (pnas.org)
  • Heme biosynthesis is induced during erythroid differentiation and is coordinated with the expression of genes involved in globin formation and iron acquisition/transport. (hindawi.com)
  • Defects of heme biosynthesis in developing erythroblasts can have profound medical implications, as represented by sideroblastic anemia. (hindawi.com)
  • We note the proximity of genes encoding enzymes of the heme biosynthesis pathway to genetic loci linked to sporadic, late-onset AD. (hindawi.com)
  • Uridine affects liver protein glycosylation, insulin signaling, and heme biosynthesis. (nih.gov)
  • Evaluation of the effects of uridine on liver heme biosynthesis and insulin signaling activity. (nih.gov)
  • carbon monoxide
  • Carbon monoxide released from the reaction of free heme in the bloodstream of someone with the sickle-cell trait is believed to lessen the effects of cerebral malaria. (wikipedia.org)
  • In mitochondria and chloroplasts, these cytochromes are often combined in electron transport and related metabolic pathways: A distinct family of cytochromes is the cytochrome P450 family, so named for the characteristic Soret peak formed by absorbance of light at wavelengths near 450 nm when the heme iron is reduced (with sodium dithionite) and complexed to carbon monoxide. (wikipedia.org)
  • Proteins
  • The JILA researchers use photon echo spectroscopy to study the motions of proteins associated with or attached to heme groups. (colorado.edu)
  • Understanding these motions will help scientists figure out how heme proteins accomplish their important work inside our cells. (colorado.edu)
  • It has catalytic function within heme or iron-sulfur clusters, or directly bound to proteins. (pnas.org)
  • We report that short-term uridine administration in C57BL/6J mice increases liver protein glycosylation profiles, reduces phosphorylation level of insulin signaling proteins, and activates the HRI-eIF-2α-ATF4 heme-deficiency stress response pathway. (nih.gov)
  • other important types include heme A and heme C. Isolated hemes are commonly designated by capital letters while hemes bound to proteins are designated by lower case letters. (wikipedia.org)
  • The structure of heme C including the absolute stereochemical configuration about the thioether bonds was first presented for the vertebrate protein and is now extended to many other heme C containing proteins. (wikipedia.org)
  • For instance, those proteins containing several heme C groups are involved with multiple electron transfer reactions, particularly important is the 6 electron reduction required to reduce atmospheric nitrogen into two organic ammonia molecules. (wikipedia.org)
  • It is common for the heme C to amino acid ratio to be high for bacterial hemeproteins, so the interiors of some cytochrome c proteins appear packed with many heme C groups compared with other hemeproteins. (wikipedia.org)
  • Hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX-1 and COX-2 enzymes (cyclooxygenase) of recent fame, also contain heme B at one of two active sites. (wikipedia.org)
  • In the 1920s, Keilin rediscovered these respiratory pigments and named them the cytochromes, or "cellular pigments", and classified these heme proteins, on the basis of the position of their lowest energy absorption band in the reduced state, as cytochromes a (605 nm), b (~565 nm), and c (550 nm). (wikipedia.org)
  • oxidative stress
  • Once heme enters the lipid bilayer within the cell, it is readily capable of increasing oxidative stress to levels that can significantly exceed the antioxidant mechanisms and capacity of the cell. (ahajournals.org)
  • Their findings are significant because they demonstrate a novel mechanism that implicates heme-dependent oxidative stress in atherosclerotic progression. (ahajournals.org)
  • cellular
  • From these facts, it is clear that dissociation of iron from heme moieties and subsequent cellular release constitute a major component of iron homeostasis. (pnas.org)
  • centre
  • In terms of molecular mechanisms, the enzyme facilitates the intramolecular hydroxylation of one meso carbon centre in the heme. (wikipedia.org)
  • methyl group
  • Heme A is similar to heme o, in that both have this farnesyl addition at position 2 but heme O does not have the formyl group at position 8, still containing the methyl group. (wikipedia.org)
  • metabolic
  • Elimination of heme from the milieu enables generation of three products that influences numerous metabolic changes in the cell. (sigmaaldrich.com)
  • Citation
  • citation needed] Several kinds of cytochrome exist and can be distinguished by spectroscopy, exact structure of the heme group, inhibitor sensitivity, and reduction potential. (wikipedia.org)
  • citation needed] Three types of cytochrome are distinguished by their prosthetic groups: The definition of cytochrome c is not defined in terms of the heme group. (wikipedia.org)