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JOURNAL ARTICLE
Membrane-Bound Flavocytochrome MsrQ Is a Substrate of the Flavin Reductase Fre in Escherichia coli .
Christelle Caux, Bruno Guigliarelli, Corinne Vivès, Frédéric Biaso, Marius Horeau, Hawra Hassoune, Isabelle Petit-Hartlein, Céline Juillan-Binard, Stephane Torelli, Franck Fieschi, Vincent Nivière
MsrPQ is a new type of methionine sulfoxide reductase (Msr) system found in bacteria. It is specifically involved in the repair of periplasmic methionine residues that are oxidized by hypochlorous acid. MsrP is a periplasmic molybdoenzyme that carries out the Msr activity, whereas MsrQ, an integral membrane-bound hemoprotein, acts as the physiological partner of MsrP to provide electrons for catalysis. Although MsrQ (YedZ) was associated since long with a protein superfamily named FRD (ferric reductase domain), including the eukaryotic NADPH oxidases and STEAP proteins, its biochemical properties are still sparsely documented...
September 22, 2021: ACS Chemical Biology
#22
JOURNAL ARTICLE
Matthew R Dent, Anthony W DeMartino, Jesús Tejero, Mark T Gladwin
Interdisciplinary research at the interface of chemistry, physiology, and biomedicine have uncovered pivotal roles of nitric oxide (NO) as a signaling molecule that regulates vascular tone, platelet aggregation, and other pathways relevant to human health and disease. Heme is central to physiological NO signaling, serving as the active site for canonical NO biosynthesis in nitric oxide synthase (NOS) enzymes and as the highly selective NO binding site in the soluble guanylyl cyclase receptor. Outside of the primary NOS-dependent biosynthetic pathway, other hemoproteins, including hemoglobin and myoglobin, generate NO via the reduction of nitrite...
July 27, 2021: Inorganic Chemistry
#23
JOURNAL ARTICLE
Daniel T Murray, Kevin L Weiss, Christopher B Stanley, Gergely Nagy, M Elizabeth Stroupe
Sulfite reductase (SiR), a dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP), reduces sulfur for biomass incorporation. Electron transfer within SiR requires intra- and inter-subunit interactions that are mediated by the relative position of each protein, governed by flexible domain movements. Using small-angle neutron scattering, we report the first solution structures of SiR heterodimers containing a single copy of each subunit. These structures show how the subunits bind and how both subunit binding and oxidation state impact SiRFP's conformation...
March 12, 2021: Journal of Structural Biology
#24
REVIEW
Meysam Zarezadeh, Ahmad Saedisomeolia, Mahoor Shekarabi, Masoud Khorshidi, Mohammad Reza Emami, Daniel J Müller
BACKGROUND: Cytochrome P450s (CYPs) are a class of hemoproteins involved in drug metabolism. It has been reported that body composition, proportion of dietary macronutrients, fasting and nutritional status can interfere with the activity of drug-metabolizing CYPs. OBJECTIVES: The present systematic review was conducted to summarize the effect of obesity, weight reduction, macronutrients, fasting and malnutrition on the CYP-mediated drug metabolism. METHODS: PubMed (Medline), Scopus, Embase and Cochrane Library databases and Google Scholar were searched up to June 2020 to obtain relevant studies...
September 2021: European Journal of Nutrition
#25
JOURNAL ARTICLE
A V Kuzikov, T V Bulko, P I Koroleva, R A Masamrekh, S S Babkina, A A Gilep, V V Shumyantseva
The electroanalytical characteristics of recombinant cytochrome P450 3A4 (P450 3A4) immobilized on the surface of screen-printed graphite electrodes modified with multi-walled carbon nanotubes have been studied. The role and the influence of graphite working electrode modification with carbon nanotubes on electroanalytical characteristics of cytochrome P450 3A4 have been demonstrated. The conditions for the immobilization of cytochrome P450 3A4 on the obtained screen-printed graphite electrodes modified with carbon multi-walled nanotubes have been optimized...
January 2020: Biomedit︠s︡inskai︠a︡ Khimii︠a︡
#26
JOURNAL ARTICLE
Oliver F Brandenberg, David C Miller, Ulrich Markel, Anissa Ouald Chaib, Frances H Arnold
Here we report a cytochrome P450 variant that catalyzes C2 -amidation of 1-methylindoles with tosyl azide via nitrene transfer. Before evolutionary optimization the enzyme exhibited two undesired side reactivities resulting in reduction of the putative iron-nitrenoid intermediate or cycloaddition between the two substrates to form triazole products. We speculated that triazole formation was a promiscuous cycloaddition activity of the P450 heme domain, while sulfonamide formation likely arose from surplus electron transfer from the reductase domain...
September 6, 2019: ACS Catalysis
#27
JOURNAL ARTICLE
Catalase-Like Antioxidant Activity is Unaltered in Hypochlorous Acid Oxidized Horse Heart Myoglobin.
Gulfam Ahmad, Belal Chami, Mary El Kazzi, Xiaosuo Wang, Maria Tereza S Moreira, Natasha Hamilton, Aung Min Maw, Thomas W Hambly, Paul K Witting
Activated neutrophils release myeloperoxidase that produces the potent oxidant hypochlorous acid (HOCl). Exposure of the oxygen transport protein horse heart myoglobin (hhMb) to HOCl inhibits Iron III (Fe(III))-heme reduction by cytochrome b 5 to oxygen-binding Iron II (Fe(II))Mb. Pathological concentrations of HOCl yielded myoglobin oxidation products of increased electrophoretic mobility and markedly different UV/Vis absorbance. Mass analysis indicated HOCl caused successive mass increases of 16 a.m.u., consistent serial addition of molecular oxygen to the protein...
September 18, 2019: Antioxidants (Basel, Switzerland)
#28
JOURNAL ARTICLE
K Theyagarajan, Duraisamy Saravanakumar, Sellappan Senthilkumar, Kathavarayan Thenmozhi
Herein, we have designed and demonstrated a facile and effective platform for the covalent anchoring of a tetrameric hemoprotein, hemoglobin (Hb). The platform comprises of naphthyl substituted amine functionalized gel type hydrophobic ionic liquid (NpNH2 -IL) through which the heme protein was covalently attached over a glassy carbon electrode (Hb-NpNH2 -IL/GCE). UV-vis and FT-IR spectral results confirmed that the Hb on NpNH2 -IL retains its native structure, even after being covalently immobilized on NpNH2 -IL platform...
July 18, 2019: Scientific Reports
#29
JOURNAL ARTICLE
Montse Olivé, Martin Engvall, Gianina Ravenscroft, Macarena Cabrera-Serrano, Hong Jiao, Carlo Augusto Bortolotti, Marcello Pignataro, Matteo Lambrughi, Haibo Jiang, Alistair R R Forrest, Núria Benseny-Cases, Stefan Hofbauer, Christian Obinger, Gianantonio Battistuzzi, Marzia Bellei, Marco Borsari, Giulia Di Rocco, Helena M Viola, Livia C Hool, Josep Cladera, Kristina Lagerstedt-Robinson, Fengqing Xiang, Anna Wredenberg, Francesc Miralles, Juan José Baiges, Edoardo Malfatti, Norma B Romero, Nathalie Streichenberger, Christophe Vial, Kristl G Claeys, Chiara S M Straathof, An Goris, Christoph Freyer, Martin Lammens, Guillaume Bassez, Juha Kere, Paula Clemente, Thomas Sejersen, Bjarne Udd, Noemí Vidal, Isidre Ferrer, Lars Edström, Anna Wedell, Nigel G Laing
Myoglobin, encoded by MB, is a small cytoplasmic globular hemoprotein highly expressed in cardiac myocytes and oxidative skeletal myofibers. Myoglobin binds O2, facilitates its intracellular transport and serves as a controller of nitric oxide and reactive oxygen species. Here, we identify a recurrent c.292C>T (p.His98Tyr) substitution in MB in fourteen members of six European families suffering from an autosomal dominant progressive myopathy with highly characteristic sarcoplasmic inclusions in skeletal and cardiac muscle...
March 27, 2019: Nature Communications
#30
JOURNAL ARTICLE
Kazuo Kobayashi
Pulse radiolysis is a powerful method for generating highly reduced or oxidized species and free radicals. Combined with fast time-resolved spectroscopic measurement, we can monitor the reactions of intermediate species on time scales ranging from picoseconds to seconds. The application of pulse radiolysis to water generates hydrated electrons (eaq - ) and specific radicals, rendering this technique useful for investigating a number of biological redox processes. The first pulse radiolysis redox investigations explored in this review involved intramolecular electron transfer processes in protein with multiple electron-accepting sites...
February 11, 2019: Chemical Reviews
#31
JOURNAL ARTICLE
Xiyan Li, Xin Wang, Michael P Snyder
Metformin elicits pleiotropic effects that are beneficial for treating diabetes, and as well as particular cancers and aging. In spite of its importance, a convincing and unifying mechanism to explain how metformin operates is lacking. Here we describe investigations into the mechanism of metformin action through heme and hemoprotein(s). Metformin suppresses heme production by 50% in yeast, and this suppression requires mitochondria function, which is necessary for heme synthesis. At high concentrations comparable to those in the clinic, metformin also suppresses heme production in human erythrocytes, erythropoietic cells and hepatocytes by 30-50%; the heme-targeting drug artemisinin operates at a greater potency...
December 15, 2018: G3: Genes—Genomes—Genetics
#32
JOURNAL ARTICLE
Uladzimir Barayeu, Mike Lange, Lucía Méndez, Jürgen Arnhold, Oleg I Shadyro, Maria Fedorova, Jörg Flemmig
Cytochrome c (cyt c) is a small hemoprotein involved in electron shuttling in the mitochondrial respiratory chain and is now also recognized as an important mediator of apoptotic cell death. Its role in inducing programmed cell death is closely associated with the formation of a complex with the mitochondrion-specific phospholipid cardiolipin (CL), leading to a gain of peroxidase activity. Yet the molecular mechanisms behind this gain and eventual cyt c auto-inactivation via its release from mitochondria membranes remains largely unknown...
December 12, 2018: Journal of Biological Chemistry
#33
JOURNAL ARTICLE
Bezalel A Bacon, Yilin Liu, James R Kincaid, Elizabeth M Boon
A novel family of bacterial hemoproteins named NosP has been discovered recently; its members are proposed to function as nitric oxide (NO) responsive proteins involved in bacterial group behaviors such as quorum sensing and biofilm growth and dispersal. Currently, little is known about molecular activation mechanisms in NosP. Here, functional studies were performed utilizing the distinct spectroscopic characteristics associated with the NosP heme cofactor. NosPs from Pseudomonas aeruginosa ( Pa), Vibrio cholerae ( Vc), and Legionella pneumophila ( Lpg) were studied in their ferrous unligated forms as well as their ferrous CO, ferrous NO, and ferric CN adducts...
October 30, 2018: Biochemistry
#34
JOURNAL ARTICLE
Marisa R Cepeda, Lauren McGarry, Joseph M Pennington, J Krzystek, M Elizabeth Stroupe
The siroheme-containing subunit from the multimeric hemoflavoprotein NADPH-dependent sulfite reductase (SiR/SiRHP) catalyzes the six electron-reduction of SO3 2- to S2- . Siroheme is an iron-containing isobacteriochlorin that is found in sulfite and homologous siroheme-containing nitrite reductases. Siroheme does not work alone but is covalently coupled to a Fe4 S4 cluster through one of the cluster's ligands. One long-standing hypothesis predicted from this observation is that the environment of one iron-containing cofactor influences the properties of the other...
May 28, 2018: Biochimica et Biophysica Acta. Proteins and Proteomics
#35
JOURNAL ARTICLE
Ciara M Shaver, Nancy Wickersham, J Brennan McNeil, Hiromasa Nagata, Adam Miller, Stuart R Landstreet, Jamie L Kuck, Joshua M Diamond, David J Lederer, Steven M Kawut, Scott M Palmer, Keith M Wille, Ann Weinacker, Vibha N Lama, Maria M Crespo, Jonathan B Orens, Pali D Shah, Chadi A Hage, Edward Cantu, Mary K Porteous, Gundeep Dhillon, John McDyer, Julie A Bastarache, Jason D Christie, Lorraine B Ware
Primary graft dysfunction (PGD) is acute lung injury within 72 hours of lung transplantation. We hypothesized that cell-free hemoglobin (CFH) contributes to PGD by increasing lung microvascular permeability and tested this in patients, ex vivo human lungs, and cultured human lung microvascular endothelial cells. In a nested case control study of 40 patients with severe PGD at 72 hours and 80 matched controls without PGD, elevated preoperative CFH was independently associated with increased PGD risk (odds ratio [OR] 2...
January 25, 2018: JCI Insight
#36
REVIEW
Marcin Lewandowski, Krzysztof Gwozdzinski
Nitroxides are stable free radicals that contain a nitroxyl group with an unpaired electron. In this paper, we present the properties and application of nitroxides as antioxidants and anticancer drugs. The mostly used nitroxides in biology and medicine are a group of heterocyclic nitroxide derivatives of piperidine, pyrroline and pyrrolidine. The antioxidant action of nitroxides is associated with their redox cycle. Nitroxides, unlike other antioxidants, are characterized by a catalytic mechanism of action associated with a single electron oxidation and reduction reaction...
November 22, 2017: International Journal of Molecular Sciences
#37
JOURNAL ARTICLE
Ciara M Shaver, Nancy Wickersham, J Brennan McNeil, Hiromasa Nagata, Gillian Sills, Jamie L Kuck, David R Janz, Julie A Bastarache, Lorraine B Ware
RATIONALE: Cell-free hemoglobin (CFH) is a potent oxidant associated with poor clinical outcomes in a variety of clinical settings. Recent studies suggest that acetaminophen (APAP), a specific hemoprotein reductant, can abrogate CFH-mediated oxidative injury and organ dysfunction. Preoperative plasma CFH levels are independently associated with primary graft dysfunction (PGD) after lung transplant ( 1 ). OBJECTIVES: Our objectives were to determine whether CFH would increase lung vascular permeability in the isolated perfused human lung and whether APAP would limit these effects...
September 2017: Annals of the American Thoracic Society
#38
REVIEW
Jagdish Rai
Natural heme proteins may have heme bound to poly-peptide chain as a cofactor via noncovalent forces or heme as a prosthetic group may be covalently bound to the proteins. Nature has used porphyrins in diverse functions like electron transfer, oxidation, reduction, ligand binding, photosynthesis, signaling, etc. by modulating its properties through diverse protein matrices. Synthetic chemists have tried to utilize these molecules in equally diverse industrial and medical applications due to their versatile electro-chemical and optical properties...
August 30, 2017: Current Protein & Peptide Science
#39
JOURNAL ARTICLE
Nino A Espinas, Koichi Kobayashi, Yasushi Sato, Nobuyoshi Mochizuki, Kaori Takahashi, Ryouichi Tanaka, Tatsuru Masuda
Heme is involved in various biological processes as a cofactor of hemoproteins located in various organelles. In plant cells, heme is synthesized by two isoforms of plastid-localized ferrochelatase, FC1 and FC2. In this study, by characterizing Arabidopsis T-DNA insertional mutants, we showed that the allocation of heme is differentially regulated by ferrochelatase isoforms in plant cells. Analyses of weak (fc1-1) and null (fc1-2) mutants suggest that FC1-producing heme is required for initial growth of seedling development...
2016: Frontiers in Plant Science
#40
JOURNAL ARTICLE
Chihiro Kitatsuji, Kozue Izumi, Shusuke Nambu, Masaki Kurogochi, Takeshi Uchida, Shin-ichiro Nishimura, Kazuhiro Iwai, Mark R O'Brian, Masao Ikeda-Saito, Koichiro Ishimori
The Bradyrhizobium japonicum transcriptional regulator Irr (iron response regulator) is a key regulator of the iron homeostasis, which is degraded in response to heme binding via a mechanism that involves oxidative modification of the protein. Here, we show that heme-bound Irr activates O2 to form highly reactive oxygen species (ROS) with the "active site conversion" from heme iron to non-heme iron to degrade itself. In the presence of heme and reductant, the ROS scavenging experiments show that Irr generates H2O2 from O2 as found for other hemoproteins, but H2O2 is less effective in oxidizing the peptide, and further activation of H2O2 is suggested...
January 5, 2016: Scientific Reports
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