The Role of Cytochrome C in the Electron Transport Chain
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Structure-Function Relationship of Metalloproteins
RESEARCH ACTIVITIES Structure-Function Relationship of Metalloproteins Department of Life and Coordination-Complex Molecular Science Division of Biomolecular Functions FUJII, Hiroshi Associate Professor KURAHASHI, Takuya Assistant Professor CONG, Zhiqi IMS Fellow OHTSUKI, Akimichi Post-Doctoral Fellow WANG, Chunlan Graduate Student TANIZAWA, Misako Secretary Metalloproteins are a class of biologically important A d4 high-spin manganese(III) ion forms a Robin-Day Class II macromolecules, which have various functions such as oxygen mixed-valence system, in which electron transfer is occurring transport, electron transfer, oxidation, and oxygenation. These between the localized phenoxyl radical and the phenolate. This diverse functions of metalloproteins have been thought to is in clear contrast to a d8 low-spin nickel(II) ion with the depend on the ligands from amino acid, coordination struc- same salen ligand, which induces a delocalized radical (Robin- tures, and protein structures in immediate vicinity of metal Day Class III) over the two phenolate rings, as previously ions. In this project, we are studying the relationship between reported by others. The present findings point to a fascinating the electronic structures of the metal active sites and reactivity possibility that electron transfer could be drastically modu- of metalloproteins. lated by exchanging the metal ion that bridges the two redox centers. 1. One-Electron Oxidation of One-electron Oxidation Electronically-Diverse Manganese(III) and N N N N Nickel(II) Salen Complexes: Transition from M M R O O R R O O R Localized to Delocalized Mixed-Valence tBu tBu 3+ 2+ tBu tBu Ligand Radicals1) M = Mn , Ni t R = Bu, OCH3, Ph Electron Transfer Ligand radicals from salen complexes are unique mixed- Figure 1. -
SUPPLEMENTARY DATA Data Supplement To
SUPPLEMENTARY DATA Data supplement to Perivascular adipose tissue controls insulin-stimulated perfusion, mitochondrial protein expression and glucose uptake in muscle through adipomuscular microvascular anastomoses Surname first author Turaihi Authors & Affiliations Turaihi, Alexander H MD1; Serné, Erik H, MD PhD2; Molthoff, Carla FM PhD3; Koning, Jasper J PhD4; Knol, Jaco PhD6; Niessen, Hans W MD PhD5; Goumans, Marie Jose TH PhD7; van Poelgeest, Erik M MD1; Yudkin, John S MD PhD8; Smulders, Yvo M MD PhD2; Connie R Jimenez, PhD6; van Hinsbergh, Victor WM PhD1; Eringa, Etto C PhD1 ©2020 American Diabetes Association. Published online at http://diabetes.diabetesjournals.org/lookup/suppl/doi:10.2337/db18-1066/-/DC1 SUPPLEMENTARY DATA Western immunoblotting Skeletal muscle samples were lysed up in 1D‐sample buffer (10% glycerol, 62.5 mmol/L Tris (pH 6.8), 2% w/v LDS, 2% w/v DTT) and protein concentration was determined using Pierce 660‐nm protein assay (Thermo scientific, Waltham, MA USA 02 451; 22 660) according to the manufacturer's instructions. Heat shock protein 90 immunoblotting was performed by application of samples (5 µg protein) on 4‐15% Criterion TGX gels (Biorad, Veenendaal, the Netherlands, 5 671 084) and semi‐dry blotting onto PVDF membranes (GE Healthcare‐Fisher, RPN1416F), incubated overnight with rat monoclonal HSP90 antibody (1:1000 dilution) after blocking with 5% milk in TBS‐T (137 mM NaCl, 20 mmol/L Tris pH 7.0 and 0.1% (v/v) Tween [Sigma‐Aldrich, P7949]). After 2 hours incubation with anti-rat, horse radish peroxidase-coupled secondary antibody (Thermo Fisher 62-9520), the blot was stained using ECL‐prime (Fisher scientific, 10 308 449) and analysed on an AI‐600 imaging system (GE Healthcare, Life Sciences). -
The Role of Methemoglobin and Carboxyhemoglobin in COVID-19: a Review
Journal of Clinical Medicine Review The Role of Methemoglobin and Carboxyhemoglobin in COVID-19: A Review Felix Scholkmann 1,2,*, Tanja Restin 2, Marco Ferrari 3 and Valentina Quaresima 3 1 Biomedical Optics Research Laboratory, Department of Neonatology, University Hospital Zurich, University of Zurich, 8091 Zurich, Switzerland 2 Newborn Research Zurich, Department of Neonatology, University Hospital Zurich, University of Zurich, 8091 Zurich, Switzerland; [email protected] 3 Department of Life, Health and Environmental Sciences, University of L’Aquila, 67100 L’Aquila, Italy; [email protected] (M.F.); [email protected] (V.Q.) * Correspondence: [email protected]; Tel.: +41-4-4255-9326 Abstract: Following the outbreak of a novel coronavirus (SARS-CoV-2) associated with pneumonia in China (Corona Virus Disease 2019, COVID-19) at the end of 2019, the world is currently facing a global pandemic of infections with SARS-CoV-2 and cases of COVID-19. Since severely ill patients often show elevated methemoglobin (MetHb) and carboxyhemoglobin (COHb) concentrations in their blood as a marker of disease severity, we aimed to summarize the currently available published study results (case reports and cross-sectional studies) on MetHb and COHb concentrations in the blood of COVID-19 patients. To this end, a systematic literature research was performed. For the case of MetHb, seven publications were identified (five case reports and two cross-sectional studies), and for the case of COHb, three studies were found (two cross-sectional studies and one case report). The findings reported in the publications show that an increase in MetHb and COHb can happen in COVID-19 patients, especially in critically ill ones, and that MetHb and COHb can increase to dangerously high levels during the course of the disease in some patients. -
Mitochondrial Cytochrome C Oxidase As a Target Site for Daunomycin in K-562 Cells and Heart Tissue1
[CANCER RESEARCH 53. 1072-1078. March I. 1993] Mitochondrial Cytochrome c Oxidase as a Target Site for Daunomycin in K-562 Cells and Heart Tissue1 Lefkothea C. Papadopoulou and Asterios S. Tsiftsoglou2 iMhoratory of Pharmacology, Department of Pharmaceutical Sciences. Aristotle University' of Thesstiloniki. Thesstiloniki 540 (Ì6,Greece ABSTRACT cells like ADR (20); (/;) DAU interacts selectively with mitochondrial COX; these interactions appear to be specific in nature and may occur Daunomycin and other structurally related anthracyclines can cause in part via the prosthetic group of heme located in two of the several myelosuppression and cardiomyopathy. We explored the possible mecha- nism(s) by which daunomycin (DAU) interacts with target sites in neo- subunits of this enzyme; (c) DAU and ADR inhibited COX activity in plastic hemopoietic cells and heart tissue. We observed that | 'lli(. i|l) VI a dose-dependent fashion that was prevented by exogenously added interacts selectively with mitochondria! hemoproteins isolated from K-562 hemin. In light of these observations, we propose that mitochondrial cells and rat and bovine heart and forms relatively stable protein com COX may serve as a target site for DAU and presumably other plexes. Isolation, purification, and Chromatographie analysis of the mito anthracyclines on highly proliferating neoplastic cells and heart tissue. chondria! components complexed with [JH(G)]DAU revealed that one of the major components involved is cytochrome c oxidase (COX). Both DAU and ADR caused a dose-dependent inhibition of COX activity in vitro, an MATERIALS AND METHODS event prevented by exogenous hemin. The interaction of DAL with COX Chemicals and Biologicals. Hemin was purchased from Eastman Kodak appears to occur via more than one site, one of which at least appears to (Rochester. -
Identification of Alternative Mitochondrial Electron Transport
International Journal of Molecular Sciences Article Identification of Alternative Mitochondrial Electron Transport Pathway Components in Chickpea Indicates a Differential Response to Salinity Stress between Cultivars Crystal Sweetman * , Troy K. Miller, Nicholas J. Booth, Yuri Shavrukov , Colin L.D. Jenkins, Kathleen L. Soole and David A. Day College of Science & Engineering, Flinders University, GPO Box 5100, Adelaide SA 5001, Australia; troy.miller@flinders.edu.au (T.K.M.); nick.booth@flinders.edu.au (N.J.B.); yuri.shavrukov@flinders.edu.au (Y.S.); colin.jenkins@flinders.edu.au (C.L.D.J.); kathleen.soole@flinders.edu.au (K.L.S.); david.day@flinders.edu.au (D.A.D.) * Correspondence: crystal.sweetman@flinders.edu.au; Tel.: +61-8-82012790 Received: 25 April 2020; Accepted: 27 May 2020; Published: 28 May 2020 Abstract: All plants contain an alternative electron transport pathway (AP) in their mitochondria, consisting of the alternative oxidase (AOX) and type 2 NAD(P)H dehydrogenase (ND) families, that are thought to play a role in controlling oxidative stress responses at the cellular level. These alternative electron transport components have been extensively studied in plants like Arabidopsis and stress inducible isoforms identified, but we know very little about them in the important crop plant chickpea. Here we identify AP components in chickpea (Cicer arietinum) and explore their response to stress at the transcript level. Based on sequence similarity with the functionally characterized proteins of Arabidopsis thaliana, five putative internal (matrix)-facing NAD(P)H dehydrogenases (CaNDA1-4 and CaNDC1) and four putative external (inter-membrane space)-facing NAD(P)H dehydrogenases (CaNDB1-4) were identified in chickpea. -
Diabetes-Induced Mitochondrial Dysfunction in the Retina
Diabetes-Induced Mitochondrial Dysfunction in the Retina Renu A. Kowluru and Saiyeda Noor Abbas 4–9 PURPOSE. Oxidative stress is increased in the retina in diabetes, tase are downregulated. We have reported that the long- and antioxidants inhibit activation of caspase-3 and the devel- term administration of antioxidants inhibits the development opment of retinopathy. The purpose of this study was to of retinopathy in diabetic rats and in galactose-fed rats (another investigate the effect of diabetes on the release of cytochrome model of diabetic retinopathy),3 suggesting an important role c from mitochondria and translocation of Bax into mitochon- for oxidative stress in the development of retinopathy in dia- dria in the rat retina and in the isolated retinal capillary cells. betes. Oxidative stress is involved directly in the upregulation ETHODS of vascular endothelial growth factor in the retina during early M . Mitochondria and cytosol fractions were prepared 10 from retina of rats with streptozotocin-induced diabetes and diabetes. Recent studies from our laboratory have shown that from the isolated retinal endothelial cells and pericytes incu- oxidative stress plays an important role, not only in the devel- opment of retinopathy in diabetes, but also in the resistance of bated in 5 or 20 mM glucose medium for up to 10 days in the 11 presence of superoxide dismutase (SOD) or a synthetic mi- retinopathy to arrest after good glycemic control is initiated. metic of SOD (MnTBAP). The release of cytochrome c into the Capillary cells and neurons are lost in the retina before other histopathology is detectable, and apoptosis has been cytosol and translocation of the proapoptotic protein Bax into 12–15 the mitochondria were determined by the Western blot tech- implicated as one of the mechanism(s). -
Concepts and Tools for Mechanism and Selectivity Analysis in Synthetic Organic Electrochemistry
Concepts and tools for mechanism and selectivity analysis in synthetic organic electrochemistry Cyrille Costentina,1,2 and Jean-Michel Savéanta,1 aUniversité Paris Diderot, Sorbonne Paris Cité, Laboratoire d’Electrochimie Moléculaire, Unité Mixte de Recherche Université–CNRS 7591, 75205 Paris Cedex 13, France Contributed by Jean-Michel Savéant, April 2, 2019 (sent for review March 19, 2019; reviewed by Robert Francke and R. Daniel Little) As an accompaniment to the current renaissance of synthetic organic sufficient to record a current-potential response but small electrochemistry, the heterogeneous and space-dependent nature of enough to leave the substrates and cosubstrates (of the order of electrochemical reactions is analyzed in detail. The reactions that follow one part per million) almost untouched. Competition of the the initial electron transfer step and yield the products are intimately electrochemical/chemical events with diffusional transport under coupled with reactant transport. Depiction of the ensuing reactions precisely mastered conditions allows analysis of the kinetics profiles is the key to the mechanism and selectivity parameters. within extended time windows (from minutes to submicroseconds). Analysis is eased by the steady state resulting from coupling of However, for irreversible processes, these approaches are blind on diffusion with convection forced by solution stirring or circulation. reaction bifurcations occurring beyond the kinetically determining Homogeneous molecular catalysis of organic electrochemical reactions step, which are precisely those governing the selectivity of the re- of the redox or chemical type may be treated in the same manner. The same benchmarking procedures recently developed for the activation action. This is not the case of preparative-scale electrolysis accom- of small molecules in the context of modern energy challenges lead to panied by identification and quantitation of products. -
Arxiv:1706.09241V1 [Cond-Mat.Mtrl-Sci] 28 Jun 2017 Based Electrolyte Supercapacitors Remain Somewhat Sim- Confinement Might Have a Drastic Influence on the Sol- Ilar
Confinement Effects on an Electron Transfer Reaction in Nanoporous Carbon Electrodes Zhujie Li1;2;3, Guillaume Jeanmairet2;3, Trinidad M´endez-Morales1;2;3, Mario Burbano1;3, Matthieu Haefele1, Mathieu Salanne1;2;3 1Maison de la Simulation, CEA, CNRS, Univ. Paris-Sud, UVSQ, Universit´eParis-Saclay, F-91191 Gif-sur-Yvette, France 2Sorbonne Universit´es,UPMC Univ Paris 06, CNRS, Laboratoire PHENIX, F-75005 Paris, France and 3R´eseau sur le Stockage Electrochimique´ de l'Energie´ (RS2E), FR CNRS 3459, France∗ Nanoconfinement generally leads to drastic effect on the physical and chemical properties of ionic liquids. Here we investigate how the electrochemical reactivity in such media may be impacted inside nanoporous carbon electrodes. To this end, we study a simple electron transfer reaction using molecular dynamics simulations. The electrodes are held at constant electric potential by allowing the atomic charges on the carbon atoms to fluctuate. We show that the Fe3+=Fe2+ couple dissolved in an ionic liquid exhibits a deviation with respect to Marcus theory. This behavior is rationalized by the stabilization of a solvation state of the Fe3+ cation in the disordered nanoporous electrode that is not observed in the bulk. The simulation results are fitted with a recently proposed two solvation state model, which allows us to estimate the effect of such a deviation on the kinetics of electron transfer inside nanoporous electrodes. Nanoconfinement effects strongly impact on many liq- a supercapacitor16. Among the various questions raised uid properties, such as transport, diffusion coefficients, by this study, the most important ones are: How is the phase transitions, and solvation structures1{4. -
Concentration of NADH-Cytochrome B5 Reductase in Erythrocytes of Normal and Methemoglobinemic Individuals Measured with a Quantitative Radioimmunoblotting Assay
Concentration of NADH-cytochrome b5 reductase in erythrocytes of normal and methemoglobinemic individuals measured with a quantitative radioimmunoblotting assay. N Borgese, … , G Pietrini, S Gaetani J Clin Invest. 1987;80(5):1296-1302. https://doi.org/10.1172/JCI113205. Research Article The activity of NADH-cytochrome b5 reductase (NADH-methemoglobin reductase) is generally reduced in red cells of patients with recessive hereditary methemoglobinemia. To determine whether this lower activity is due to reduced concentration of an enzyme with normal catalytic properties or to reduced activity of an enzyme present at normal concentration, we measured erythrocyte reductase concentrations with a quantitative radioimmunoblotting method, using affinity-purified polyclonal antibodies against rat liver microsomal reductase as probe. In five patients with the "mild" form of recessive hereditary methemoglobinemia, in which the activity of erythrocyte reductase was 4-13% of controls, concentrations of the enzyme, measured as antigen, were also reduced to 7-20% of the control values. The concentration of membrane-bound reductase antigen, measured in the ghost fraction, was similarly reduced. Thus, in these patients, the reductase deficit is caused mainly by a reduction in NADH-cytochrome b5 reductase concentration, although altered catalytic properties of the enzyme may also contribute to the reduced enzyme activity. Find the latest version: https://jci.me/113205/pdf Concentration of NADH-Cytochrome b5 Reductase in Erythrocytes of Normal and Methemoglobinemic -
Coupling of Energy to Active Transport of Amino Acids in Escherichia Coli (Mutants/Membrane Vesicles/Ca,Mg-Atpase/Electron Transport/D-Lactate Dehydrogenase) ROBERT D
Proc. Nat. Acad. Sci. USA Vol. 69, No. 9, pp. 2663-2667, September 1972 Coupling of Energy to Active Transport of Amino Acids in Escherichia coli (mutants/membrane vesicles/Ca,Mg-ATPase/electron transport/D-lactate dehydrogenase) ROBERT D. SIMONI AND MARY K. SHALLENBERGER Department of Biological Sciences, Stanford University, Stanford, California 94305 Communicated by Charles Yanofsky, July 6, 1972 ABSTRACT Active transport of amino acids in isolated *to the lack of oxygen (3). Streptococcus faecalis, an anaerobe membrane vesicles of E. coli ML 308-225 is stimulated by that contains no electron-transport system, can carry out oxidation of D-lactate, and this stimulation is dependent the on electron transport [Kaback, H. R. & Milner, L. S. active membrane transport, presumably using energy- (1970) Proc. Nat. Acad. Sci. USA 66, 1008]. In attempting to yielding reactions of glycolysis (7). It has become essential to relate these results to amino-acid transport in intact relate the observations obtained with isolated vesicles to cells, we isolated mutants of E. coli ML 308-225 that physiological realities of intact cells. We have isolated cells contain defects in D-lactate dehydrogenase (EC 1.1.2.4) in various components involved in and electron transport. Intact cells of these mutants are that contain mutations normal for transport of proline and alanine. We also aerobic metabolism and have tested the effects of these muta- isolated mutants defective in Ca,Mg-stimulated ATPase tions on the ability to perform active transport of amino acids. (EC 3.6.1.3), which is responsible for coupling electron transport to the synthesis of ATP. -
Oxidation-Reduction Reactions
Oxidation-Reduction Reactions What is an Oxidation-Reduction, or Redox, reaction? Oxidation-reduction reactions, or redox reactions, are technically defined as any chemical reaction in which the oxidation number of the participating atom, ion, or molecule of a chemical compound changes. Some common redox reactions include fire, rusting of metals, browning of fruit, and photosynthesis. In simpler terms, redox reactions involve the transfer of electrons from one substance to another. In a redox reaction, electrons can never be “lost”; if one substance loses electrons, another substance must gain an equal number of electrons. Therefore, oxidation and reduction always happen at the same time; they are a matched set. What is Oxidation? Oxidation is the loss of electrons by an atom, ion, or molecule. The atom, ion, or molecule that is oxidized will become more positively charged. Oxidation may also involve the addition of oxygen or the loss of hydrogen. What is Reduction? Reduction is the gain of electrons by an atom, ion, or molecule. The atom, ion, or molecule that is reduced will become more negatively charged. Reduction may also involve the loss of oxygen or the gain of hydrogen. Tips for determining if an atom, ion, or compound has been Oxidized or Reduced: • Remembering one of the two following mnemonics can be of assistance in determining the difference between oxidation and reduction: 1) OIL RIG- Oxidation Is Loss (of electrons), Reduction Is Gain (of electrons) or 2) LEO GER- Loss of Electrons- Oxidation, Gain of Electrons- Reduction • Atoms of metals tend to lose electrons to form positive ions (oxidation) • Atoms of non-metals tend to gain electrons to form negative ions (reduction). -
Glycolysis Citric Acid Cycle Oxidative Phosphorylation Calvin Cycle Light
Stage 3: RuBP regeneration Glycolysis Ribulose 5- Light-Dependent Reaction (Cytosol) phosphate 3 ATP + C6H12O6 + 2 NAD + 2 ADP + 2 Pi 3 ADP + 3 Pi + + 1 GA3P 6 NADP + H Pi NADPH + ADP + Pi ATP 2 C3H4O3 + 2 NADH + 2 H + 2 ATP + 2 H2O 3 CO2 Stage 1: ATP investment ½ glucose + + Glucose 2 H2O 4H + O2 2H Ferredoxin ATP Glyceraldehyde 3- Ribulose 1,5- Light Light Fx iron-sulfur Sakai-Kawada, F Hexokinase phosphate bisphosphate - 4e + center 2016 ADP Calvin Cycle 2H Stroma Mn-Ca cluster + 6 NADP + Light-Independent Reaction Phylloquinone Glucose 6-phosphate + 6 H + 6 Pi Thylakoid Tyr (Stroma) z Fe-S Cyt f Stage 1: carbon membrane Phosphoglucose 6 NADPH P680 P680* PQH fixation 2 Plastocyanin P700 P700* D-(+)-Glucose isomerase Cyt b6 1,3- Pheophytin PQA PQB Fructose 6-phosphate Bisphosphoglycerate ATP Lumen Phosphofructokinase-1 3-Phosphoglycerate ADP Photosystem II P680 2H+ Photosystem I P700 Stage 2: 3-PGA Photosynthesis Fructose 1,6-bisphosphate reduction 2H+ 6 ADP 6 ATP 6 CO2 + 6 H2O C6H12O6 + 6 O2 H+ + 6 Pi Cytochrome b6f Aldolase Plastoquinol-plastocyanin ATP synthase NADH reductase Triose phosphate + + + CO2 + H NAD + CoA-SH isomerase α-Ketoglutarate + Stage 2: 6-carbonTwo 3- NAD+ NADH + H + CO2 Glyceraldehyde 3-phosphate Dihydroxyacetone phosphate carbons Isocitrate α-Ketoglutarate dehydogenase dehydrogenase Glyceraldehyde + Pi + NAD Isocitrate complex 3-phosphate Succinyl CoA Oxidative Phosphorylation dehydrogenase NADH + H+ Electron Transport Chain GDP + Pi 1,3-Bisphosphoglycerate H+ Succinyl CoA GTP + CoA-SH Aconitase synthetase