Loading...
  • dioxygen
  • DOI: 10.1186/s12870-015-0562-x Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. (wikipedia.org)
  • binds
  • gene in human beings.48 Increased expression of the gene is connected with various types of cancer.49 This gene is an associate from the methionyl aminopeptidase family and encodes a protein that binds to cobalt or manganese ions.48 Literature recommended that MetAP2 takes on a crucial role within the growth of various kinds of tumors via advertising angiogenesis. (recyclers-info.com)
  • ENDOR spectroscopy was used to determine that the substrate directly binds to the Fe(II)/Fe(III) di-iron center of MIOX most likely through the O1 atom of myo-inositol. (wikipedia.org)
  • In muscles cells, iron binds myoglobin, which regulates its release. (wikipedia.org)
  • redox
  • Our research focuses on understanding the redox and hydrolysis-mineralization mechanisms by which iron is acquired and released by ferritin. (unh.edu)
  • Thus, iron plays a vital role in the catalysis of enzymatic reactions that involve electron transfer (reduction and oxidation, redox). (wikipedia.org)
  • structures
  • Barge LM, Doloboff IJ, White LM, Russell MJ, Kanik I (2012) Characterization of iron-phosphate-silicate chemical garden structures. (springer.com)
  • Based on detailed analyses of 15-lipoxygenase 1 and stabilized 5-lipoxygenase, lipoxygenase structures consist of a 15 kilodalton N-terminal beta barrel domain, a small (e.g. ~0.6 kilodalton) linker inter-domain (see protein domain#Domains and protein flexibility), and a relatively large C-terminal catalytic domain which contains the non-heme iron critical for the enzymes' catalytic activity. (wikipedia.org)
  • This work resulted in his sharing with John Kendrew the 1962 Nobel Prize in Chemistry for their studies of the structures of globular proteins. (wikipedia.org)
  • Comparison of amino acid sequences has revealed the following consensus sequence: Cys-Xaa-His-(Xaa)15-17-Cys-Xaa-Xaa-His The crystal structures of a number of Rieske proteins are known. (wikipedia.org)
  • residues
  • Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal methionine residues from nascent proteins. (wikipedia.org)
  • For proteins with small, uncharged penultimate N-terminal residues, a methionine aminopeptidase can cleave the methionine residue. (wikipedia.org)
  • metabolism
  • Our research program is devoted to studies of the bioinorganic and biophysical chemistry of metalloproteins, in particular those proteins involved in the metabolism of iron, i.e. ferritin and transferrin. (unh.edu)
  • In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism. (wikipedia.org)
  • In mammals and humans, 2OG-dependent dioxygenase have functional roles in biosyntheses (e.g. collagen biosynthesis and L-carnitine biosynthesis), post-translational modifications (e.g. protein hydroxylation), epigenetic regulations (e.g. histone and DNA demethylation), as well as sensors of energy metabolism. (wikipedia.org)
  • Human iron metabolism is the set of chemical reactions that maintain human homeostasis of iron at both the systemic and cellular level. (wikipedia.org)
  • Hematologists have been especially interested in systemic iron metabolism because iron is essential for red blood cells, where most of the human body's iron is contained. (wikipedia.org)
  • Understanding iron metabolism is also important for understanding diseases of iron overload, such as hereditary hemochromatosis, and iron deficiency, such as iron deficiency anemia. (wikipedia.org)
  • MetAP2
  • peptide-methionine ⇌ {\displaystyle \rightleftharpoons } peptide + methionine MetAP2 is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. (wikipedia.org)
  • MetAP2 shows activity in the presence of Zn(II), Co(II), Mn(II), and Fe(II) ions, and various authors have argued any given metal ion is the physiological one: some in the presence of iron, others in cobalt, others in manganese, and yet others in the presence of zinc. (wikipedia.org)
  • Rieske
  • He is well known for his structural enzymology work on Rieske non-heme iron oxygenases and Alcohol Dehydrogenases His research on cockroach protein gain lot of popularity in the scientific community and the media. (wikipedia.org)
  • molecules
  • The two iron centers are coordinated by various amino acids and water molecules as shown in complex with the myo-inositol substrate. (wikipedia.org)
  • Disease-causing bacteria do this in many ways, including releasing iron-binding molecules called siderophores and then reabsorbing them to recover iron, or scavenging iron from hemoglobin and transferrin. (wikipedia.org)
  • novel
  • Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation. (uio.no)
  • Identification and characterization of a novel human methyltransferase modulating hsp70 Protein function through lysine methylation. (uio.no)
  • bacteria
  • Typical intracellular labile iron concentrations in bacteria are 10-20 micromolar, though they can be 10-fold higher in anaerobic environment, where free radicals and reactive oxygen species are scarcer. (wikipedia.org)
  • If bacteria are to survive, then they must obtain iron from their environment. (wikipedia.org)
  • That means that iron-deprived bacteria reproduce more slowly. (wikipedia.org)
  • biochemistry
  • Biochemistry) any of a group of enzymes that contain a derivative of riboflavin linked to a protein and catalyse oxidation in cells. (thefreedictionary.com)
  • In addition we have an interest in vanadium biochemistry and in proteins that play a role in shell biomineralization in mollusks. (unh.edu)
  • The identification of this non-heme iron protein, now known as an iron-sulfur protein, is significant to multiple areas of biochemistry and microbiology. (asm.org)
  • structural
  • We seek to understand the structural attributes by which this unusual protein is capable of reversibly storing such large quantities of iron (4500 Fe/protein). (unh.edu)
  • Our work is directed at understanding the spectral, structural and kinetic properties of the protein as they relate to its function in vivo. (unh.edu)
  • For example, significant protein structural changes have been observed upon substrate binding for human prolyl hydroxylase isoform 2 (PHD2), a 2OG-dependent dioxygenase that is involved in oxygen sensing, and isopenicillin N synthase (IPNS), a microbial 2OG-dependent dioxygenase. (wikipedia.org)
  • Mutations
  • Mutations in either of these proteins render Arabidopsis thaliana plants hypersensitive to salt stress. (asm.org)
  • enzyme
  • This enzyme belongs to the family of oxidoreductases, that use iron-sulfur proteins as electron donors and NAD+ or NADP+ as electron acceptors. (wikipedia.org)
  • Binding of the enzyme to the thylakoid membrane involves a polyproline type II helix created between two FNR monomers and several proline rich integral membrane proteins. (wikipedia.org)
  • The binding of the FNR to the integral membrane proteins on the thylakoid membrane is enhanced under acidic conditions, so recruitment and binding of FNR to the thylakoid membrane may be a method of storing and stabilizing the enzyme in the dark when photosynthesis is not occurring. (wikipedia.org)
  • Inositol oxygenase, also commonly referred to as myo-inositol oxygenase (MIOX), is a non-heme di-iron enzyme that oxidizes myo-inositol to glucuronic acid. (wikipedia.org)
  • The enzyme employs a unique four-electron transfer at its Fe(II)/Fe(III) coordination sites and the reaction proceeds through the direct binding of myo-inositol followed by attack of the iron center by diatomic oxygen. (wikipedia.org)
  • For example, assays were developed to study ligand binding, enzyme kinetics, modes of inhibition as well as protein conformational change. (wikipedia.org)
  • fold
  • The second domain is at the carboxyl terminus of the protein and contains an alpha helix-beta strand fold. (wikipedia.org)
  • initiates
  • In response to a systemic bacterial infection, the immune system initiates a process known as iron withholding. (wikipedia.org)
  • identical
  • In 1825 J. F. Engelhard discovered that the ratio of iron to protein is identical in the hemoglobins of several species. (wikipedia.org)
  • For example, the most common hemoglobin sequences in humans and chimpanzees are nearly identical, differing by only one amino acid in both the alpha and the beta globin protein chains[citation needed]. (wikipedia.org)
  • superoxide
  • Like other di-iron oxygenases, the iron coordination centers are buried deep inside the protein presumably to protect the cell from the superoxide and radical reaction intermediates that are formed. (wikipedia.org)
  • Hemoglobin
  • Purely inorganic substances such as iron are often required in essential organic reactions, e.g. oxygen binding in the hemoglobin family. (wikipedia.org)
  • Hemoglobin is involved in the transport of other gases: It carries some of the body's respiratory carbon dioxide (about 20-25% of the total) as carbaminohemoglobin, in which CO2 is bound to the globin protein. (wikipedia.org)
  • The oxygen-carrying protein hemoglobin was discovered by Hünefeld in 1840. (wikipedia.org)
  • In 1851, German physiologist Otto Funke published a series of articles in which he described growing hemoglobin crystals by successively diluting red blood cells with a solvent such as pure water, alcohol or ether, followed by slow evaporation of the solvent from the resulting protein solution. (wikipedia.org)
  • Heme groups are part of hemoglobin, a protein found in red blood cells that serves to transport oxygen from the lungs to the tissues. (wikipedia.org)
  • When this occurs, the sequestration of iron appears to be the major cause of the syndrome of anemia of chronic disease, in which not enough iron is available to produce enough hemoglobin-containing red blood cells. (wikipedia.org)
  • enzymes
  • Any of a group of enzymes containing flavin bound to protein and acting as dehydrogenation catalysts in biological reactions. (thefreedictionary.com)
  • are a family of (non-heme), iron-containing enzymes most of which catalyze the dioxygenation of polyunsaturated fatty acids in lipids containing a cis,cis-1,4- pentadiene into cell signaling agents that serve diverse roles as autocrine signals that regulate the function of their parent cells, paracrine signals that regulate the function of nearby cells, and endocrine signals that regulate the function of distant cells. (wikipedia.org)
  • atom
  • This binding step positions the myo-inositol prior to the catalytic steps which involve attack of an iron center by diatomic oxygen followed by abstraction of a myo-inositol hydrogen atom. (wikipedia.org)
  • The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. (wikipedia.org)
  • sulfur
  • An iron-sulfur molybdenum flavoprotein. (qmul.ac.uk)
  • In Type II systems, the reduced pyridine nucleotide first reduces an FAD-containing reductase which subsequently transfers electrons one at a time to a 2Fe,2S iron-sulfur protein. (springer.com)
  • Proteins can contain iron as part of different cofactors, such as iron-sulfur clusters (Fe-S) and heme groups, both of which are assembled in mitochondria. (wikipedia.org)
  • Iron is present in the iron-sulfur clusters and heme groups of the electron transport chain proteins that generate a proton gradient that allows ATP synthase to synthesize ATP (chemiosmosis). (wikipedia.org)
  • bound
  • Structure of a heterogeneous, glycosylated, lipid-bound, in vivo-grown protein crystal at atomic resolution from the viviparous cockroach Diploptera punctata. (wikipedia.org)
  • The molecule also carries the important regulatory molecule nitric oxide bound to a globin protein thiol group, releasing it at the same time as oxygen. (wikipedia.org)
  • Iron bound to proteins or cofactors such as heme is safe. (wikipedia.org)
  • manganese
  • TB causing bacterium can reside within macrophages which are an iron rich environment and Borrelia burgdorferi utilises manganese in place of iron. (wikipedia.org)
  • found
  • Ferritin - The ferritins are a class of iron storage proteins found widely distributed among the animal, plant and microbial kingdoms. (unh.edu)
  • Studies have shown that one cockroach protein crystals contain more than three times the energy found in an equivalent amount of buffalo milk. (wikipedia.org)
  • This protein is also found in the hooves and horns of different animals. (wikipedia.org)
  • flavoprotein
  • The proteins belonging to this group are ferredoxins, which represent the iron-sulphur cluster that performs the intermediate step in the electron transfer chain, transferring electrons from the flavoprotein to the terminal dioxygenase (Bertini et al. (thefreedictionary.com)
  • oxygen-transport
  • abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates (with the exception of the fish family Channichthyidae) as well as the tissues of some invertebrates. (wikipedia.org)
  • The human body needs iron for oxygen transport. (wikipedia.org)
  • biological
  • The biological membrane is composed of lipids and proteins. (slideshare.net)
  • In 1962, Len and two colleagues at DuPont introduced the name ferredoxin for the electron-transferring protein they purified from C. pasteurianum during their study of biological nitrogen fixation. (asm.org)