DOCSLIB.ORG

82182065.Pdf

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
82182065.Pdf A42 HEMOGLOBINHIEMOGLOBIN AND MYOGLODINISYOGLOBIN M-Poe107 MPos108 LOW TEMPERATURE RECOMBINATION OF MbO, USING FOURIER TIME-RESOLVED X-RAY ABSORPTION SPECTROSCOPY ON A 5 ps TRANSFORM INFRARED SPECTROSCOPY. ((M. Halterman, L. M. Miller, and TIMESCALE. ((M.R. Chance, M.D. Wort, L.M. Miller, E.M. Scheuring, A. Xie, M. R. Chance)) Albert Einstein College of Medicine., Bronx, NY 10461. D.E. Sidelinger)) Albert Einstein Col of Med., Bronx, NY 10461 The binding of oxygen to hemoglobin and myoglobin is one of the most X-ray absorption spectroscopy (XAS) is unmatched in measuring metal-ligand important reactions in human cells. Essential to understanding the binding distances in solution while the dynamics of evolving systems is a subject of process is the study of intermediate states. To date, the intermediate states intense interest in biophysics currently. We report the design and successful involved in carbon monoxide binding are much better understood than those testing of a system for collecting time-resolved XAS data on a 5ps timescale. of oxygen binding. However, recent studies have shown that 02 and CO have The system is based on the use of a germanium energy resolving detector and significantly different rebinding intermediates (M. Chance, et. al., Biochemistry, a fast multichannel scaling (FMS) board, both from Canberra Ind. The output 29, 1990, p. 5537). Vibrational spectroscopic methods have indicated several of a single Ge channel is amplified and connected to the FMS board. The data bands for MbO2 ligand stretching modes (Potter, et. al., Biochemistry, 26, acquisition sequence is controlled by a digital delay generator, which also 1987, p. 4699). However, it is uncertain whether these bands correspond to controls the firing of a (doubled) Nd-YAG laser (output 100 mW, 532 nm, 10 various protein conformations, as they do for MbCO. If the multiple bands Hz). Software control allows the windowing of the x-ray fluorescence peak of have different rebinding kinetics, this supports multiple steric and electronic interest, which is then laid down in directly accessed memory with specifed environments of the distal histidine. time widths. A typical experiment laid down 8192 channels of data, each We present the results of low temperature recombination of 02 with myoolobin counting a 5 ps interval. For testing of the system, we used a well using Fourier Transform Infrared Spectroscopy (FTIR). The bound state of characterized chemical system, that of rebinding of carbon monoxide with oxymyoglobin exhibits three infrared bands of interest at 1090 cm', 1115 myoglobin after a laser flash at low-temperature. To date, we are aware of only cm', and 1 135 cm". Upon photolysis, the intensity of each band is reduced. one previous attempt to perform XAS in a time-resolved fashion on (300) ps After warming, the 02 and myoglobin recombine and the bands reappear. timescales ID. Mills, et. al., Science, 223, 1984, p. 811). In one experiment, Kinetic analysis of these bands helps to identify the presence of various protein an excellent x-ray edge was collected on 5pS timescales (4 mM MbCO, data conformations involved in the recombination process. Low-temperature collected every 4 eV, and 5000 sweeps at each energy). In a second recombination of samples at various pH's will demonstrate various protonation experiment, we demonstrated that with a 1 mM sample and 20 ps time states of the distal histidine. Also, we will present studies using isotopically resolution we could sit at a single x-ray wavelength, where the difference labelled 02 in order to identify those stretching modes directly related to the Fe- between the photolyzed and ligand bound spectra is the largest (kinetic 02 bond. This research is supported by a grant from the NIH, #HL-45892. spectrophotometry), and observe the photolysis and recombination of the sample. This work is supported by NIH grant HL-45892. M0Po109 M-PollO X-RAY ABSORPTION SPECTROSCOPY OF MBO AND MBCO REBINDING LIGAND CONCENTRATION DEPENDENCE OF THE REBIND- INTERMEDIATES. ((L.M. Miller, M.R. Chance M.D. Wirt, E.M. Scheuring)) Albert Einstein Col. ING RATE OF CO TO MYOGLOBIN. ((R. G. Philipp, R. M. Ernst, of Med., Bronx, NY 10461 G. U. Nienhaus, R. D. Young, H. Frauenfelder)) University of Illinois Recent studies have shown that MbO2 and MbCO have significantly different at Urbana-Champaign, Urbana, IL 61801.* rebinding intermediates. For example, the quantum yield of MbO2 photolysis at low temperature is 0.4 whereas that of MbCO is 1.0. X-ray absorption We compare the rate of rebinding of CO to myoglobin with the rate spectroscopy (XAS) can be used to study the differences between these two predicted for a bimolecular process. The measurements probe rebinding rebinding processes. XAS is especially sensitive to iron displacement from the kinetics in a glycerol/water solvent using flash photolysis over a wide heme plane and charge density on the iron atom. When a ligand is photolyzed from hemoglobin and myoglobin, the displacement and charge density of the range of time and temperature. We have used a pressure cell which Iron change, resulting in changes In the x-ray edge position and the XANES allows CO pressures of 0-200 atm, with a corresponding CO concentra- region of bound versus photolyzed hemoglobin or myoolobin. The x-ray tion which ranges from the low to high concentration limits. absorption spectrum of bound MbO2 was obtained at high resolution using 0.5 eV steps across the x-ray edge. First derivatives of the edge spectra are used 'This work supported by the Office of Naval Research. to accurately define the charge density on the central metal. The position of the MbO, edge can now be well defined at 7125.4 eV. In comparison, we find the x-ray edge position of MbCO to be at 7123.9 eV, indicating a significant difference in iron environments between the bound MbCO and MbO2. This result is consistent with studies that have shown a hydrogen bond between oxygen (but not CO) and the distal histidine of myoglobin. This hydrogen bond is stabilized by charge reorganization from the iron to the oxygen, resulting in a loss of charge density on the iron. This loss of charge density is reflected in the x-ray edge by a shift to higher energy. Additionally, we have collected x-ray edge and EXAFS spectra of photolyzed MbO2; both the x-ray edge and the XANES region show differences between the photolyzed and unphotolyzed MbO2.This work has been supported by NIH grant HL-45892. M-Poesll M-P0o112 A- AND B-STATE TRANSITIONS IN MYOGLOBIN ((K. Chu, J.R. INFRARED FLASH PHOTOLYSIS EXPERIMENTS ON THE TAXONOMIC Mourant, Y. Abadan, H. Frauenfelder, G.U. Nienhaus and R.D. Young)) SUBSTATES OF MYOGLOBIN ((Don C. Lamb, Bradley T. Banko, Hans Department of Physics, University of Illinois, 1110 W. Green St., Ur- ausn«feder, G. Ulrich Nienhaus and Robert D. Young)) Deatment of bana, IL 61801. Physics, University of Illinois at UrbanChampag, 1110 W. Green St., Ur- bana, Illinois 61801 FTIR spectroscopy on low temperature photoproducts of sperm Sperm whale carbonmaymyoglobin exhibits at least three spectroscop- whale carbonmonoxymyoglobin has revealed much information about icaily ditin able infrared stretch bands. They are Interpreted as three ligand rebinding dynamics in proteins. Several spectroscopic lines are different taxonomic substates,1 refered to as Ao, A1 and A3. Flash pho- observed around 1950 cm-' and 2150 cm-'; these are CO stretch bands tolysis piments have been performed on the Individual A substates by corresponding to conformational substates of the ligand bound (A sub- monitorng at slected wavelegths in the infrared The three temperature- states) and photolysed (B substates) protein-ligand system. The A and independent distnbutions of activation anthalpies for ligand rebinding after B substates undergo three separate classes of transitions following pho- photolysis, g(H), are detamined firom the low temperature kinetics (5OK - tolysis. Upon absorption of a visible photon by the heme, the ligand 160K) for the different A substates. Thes g(H) distributions are compared - heme bond breaks, resulting in an A-B transition. The resulting B for sample at different pH. The g(H) distributions are alao compared to those substates are not in thermal equilibrium and a B-RB exchange occurs. determined using teperature derivative spectroscopy. At temperatur above Finally, the ligand rebinds to the protein (B-_A). We use isothermal 180K, we describe the kinetics with temperature-dependent distributions of kinetics and temperature derivative spectroscopy to identify and char- rate coeffcients, f(A). The mexlmm entropy method was used to calculate acterize the tunneling and thermally activated transitions. (This work the f(A) for temperatures above 180K. The f(A) distributions provide addi- supported by the NSF and the NIH.) tlonal insight into the entrance and escape ofcarbon monouide from the heme pocket as wel as protein motins. This work is supported with grants from the NIH, the NSF and the ONR. 1H. Fafelder, S.G. SIgsa sad P.G. Wolyaes,Sc,mns254, 1559 (1991). HEMOGLOBIN AND MYOGLOBIN A43*AA M-Pos13 M-Posl14 MOLECULAR DYNAMICS SIMULATIONS OF LIGAND DISSOCIATION OXYGEN BINDING TO SINGLE CRYSTALS OF HEMOGLOBIN IN THE AND REBINDING IN MYOGLOBIN. ((Olivier Schaad, Huan-Xiang Zhou, T QUATERNARY STRUCTURE. ((A. Mozzarelli, C. Rivetti, G. L. Rossi, E. Eric R. Henry, Attila Szabo and William A. Eaton)) Laboratory of Chemical R. Henry, and W. A. Eaton)) Institute of Biochemical Sciences, University Physics, NIDDK, NIH, Bethesda, MD 20892 of Parma, and Laboratory of Chemical Physics, NIDDK, NIH, Bethesda, MD 20892. We have begun to study the kinetics of NO rebinding to myoglobin following photodissociation by molecular dynamics simulations. The Microspectrophotometry was used to measure reversible oxygen binding simulations included the complete protein molecule with all hydrogen atoms curves for single crystals of hemoglobin in the T quatemary structure.
Load more

Recommended publications
  • Families and the Structural Relatedness Among Globular Proteins
    Protein Science (1993), 2, 884-899. Cambridge University Press. Printed in the USA. Copyright 0 1993 The Protein Society -~~ ~~~~ ~ Families and the structural relatedness among globular proteins DAVID P. YEE AND KEN A. DILL Department of Pharmaceutical Chemistry, University of California, San Francisco, California94143-1204 (RECEIVEDJanuary 6, 1993; REVISEDMANUSCRIPT RECEIVED February 18, 1993) Abstract Protein structures come in families. Are families “closely knit” or “loosely knit” entities? We describe a mea- sure of relatedness among polymer conformations. Based on weighted distance maps, this measure differs from existing measures mainly in two respects: (1) it is computationally fast, and (2) it can compare any two proteins, regardless of their relative chain lengths or degree of similarity. It does not require finding relative alignments. The measure is used here to determine the dissimilarities between all 12,403 possible pairs of 158 diverse protein structures from the Brookhaven Protein Data Bank (PDB). Combined with minimal spanning trees and hier- archical clustering methods,this measure is used to define structural families. It is also useful for rapidly searching a dataset of protein structures for specific substructural motifs.By using an analogy to distributions of Euclid- ean distances, we find that protein families are not tightly knit entities. Keywords: protein family; relatedness; structural comparison; substructure searches Pioneering work over the past 20 years has shown that positions after superposition. RMS is a useful distance proteins fall into families of related structures (Levitt & metric for comparingstructures that arenearly identical: Chothia, 1976; Richardson, 1981; Richardson & Richard- for example, when refining or comparing structures ob- son, 1989; Chothia & Finkelstein, 1990).
    [Show full text]
  • The Effects of Temperature on Hemoglobin in Capitella Teleta
    THE EFFECTS OF TEMPERATURE ON HEMOGLOBIN IN CAPITELLA TELETA by Alexander M. Barclay A thesis submitted to the Faculty of the University of Delaware in partial fulfillment of the requirements for the degree of Master of Science in Marine Studies Summer 2013 c 2013 Alexander M. Barclay All Rights Reserved THE EFFECTS OF TEMPERATURE ON HEMOGLOBIN IN CAPITELLA TELETA by Alexander M. Barclay Approved: Adam G. Marsh, Ph.D. Professor in charge of thesis on behalf of the Advisory Committee Approved: Mark A. Moline, Ph.D. Director of the School of Marine Science and Policy Approved: Nancy M. Targett, Ph.D. Dean of the College of Earth, Ocean, and Environment Approved: James G. Richards, Ph.D. Vice Provost for Graduate and Professional Education ACKNOWLEDGMENTS I extend my sincere gratitude to the individuals that either contributed to the execution of my thesis project or to my experience here at the University of Delaware. I would like to give special thanks to my adviser, Adam Marsh, who afforded me an opportunity that exceeded all of my prior expectations. Adam will say that I worked very independently and did not require much guidance, but he served as an inspiration and a role model for me during my studies. Adam sincerely cares for each of his students and takes the time and thought to tailor his research program to fit each person's interests. The reason that I initially chose to work in Adam's lab was that he expressed a genuine excitement for science and for his lifes work. His enthusiasm resonated with me and helped me to find my own exciting path in science.
    [Show full text]
  • Prediction of the Amount of Secondary Structure in a Globular Protein from Its Aminoacid Compositionj (Helix/Pl-Sheet/Turns) W
    Proc. Nat. Acad. Sci. USA Vol. 70, No. 10, pp. 2809-2813, October 1973 Prediction of the Amount of Secondary Structure in a Globular Protein from Its Aminoacid Compositionj (helix/pl-sheet/turns) W. R. KRIGBAUM AND SARA PARKEY KNLTTTON Gross Chemical Laboratory, Duke University, Durham, North Carolina 27706 Communicated by Walter Gordy, June 22, 1973 ABSTRACT Multiple regression is used to obtain rela- so reference was made to the published crystal structures tionships for predicting the amount of secondary structure where ambiguities arose. Regions not included in the above in a protein molecule from a knowledge of its aminoacid composition. We tested these relations using 18 proteins of categories were termed coil. Assignments of secondary struc- known structure, but omitting the protein to be predicted. tural regions appear in Table 1. Since residues may be assipned Independent predictions were made for the two sub- to more than one category (e.g., the last residues of a helical chains of hemoglobin and insulin. The average errors for region and the first ones of a turn), then percentages do not these 20 chains or subchains are: helix ± 7.1%, p-sheet necessarily add up to 100% for any protein. ± 6.9%, turn ± 4.2%, and coil ± 5.7%. A second set of rela- tions yielding somewhat inferior predictions is given for We recognize at the outset that this data base contains the case in which Asp and Asn, and Glu and Gln, are not errors of at least two types. First, there are some remaining differentiated. Predictions are also listed for 15 proteins uncertainties in the primary structures.
    [Show full text]
  • Edinburgh Research Explorer
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Edinburgh Research Explorer Edinburgh Research Explorer Transcriptome profiling of developmental and xenobiotic responses in a keystone soil animal, the oligochaete annelid Lumbricus rubellus Citation for published version: Owen, J, Hedley, BA, Svendsen, C, Wren, J, Jonker, MJ, Hankard, PK, Lister, LJ, Stürzenbaum, SR, Morgan, AJ, Spurgeon, DJ, Blaxter, ML & Kille, P 2008, 'Transcriptome profiling of developmental and xenobiotic responses in a keystone soil animal, the oligochaete annelid Lumbricus rubellus' BMC Genomics, vol. 9, no. 266, pp. -. DOI: 10.1186/1471-2164-9-266 Digital Object Identifier (DOI): 10.1186/1471-2164-9-266 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: BMC Genomics Publisher Rights Statement: This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim.
    [Show full text]
  • From Protein Corona to Colloidal Self-Assembly
    From Protein Corona to Colloidal Self-Assembly: The Importance of Protein Size in Protein-Nanoparticle Interactions Laurent Marichal, Jéril Degrouard, Anouchka Gatin, Nolwenn Raffray, Jean-Christophe Aude, Yves Boulard, Sophie Combet, Fabrice Cousin, Stéphane Hourdez, Jean Mary, et al. To cite this version: Laurent Marichal, Jéril Degrouard, Anouchka Gatin, Nolwenn Raffray, Jean-Christophe Aude, et al.. From Protein Corona to Colloidal Self-Assembly: The Importance of Protein Size in Protein-Nanoparticle Interactions. Langmuir, American Chemical Society, 2020, 36, pp.8218-8230. 10.1021/acs.langmuir.0c01334. cea-02883393 HAL Id: cea-02883393 https://hal-cea.archives-ouvertes.fr/cea-02883393 Submitted on 29 Jun 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. From Protein Corona to Colloidal Self-Assembly: The Importance of Protein Size in Protein- Nanoparticle Interactions Laurent Marichal a,b *, Jéril Degrouard c, Anouchka Gatin a, Nolwenn Raffray a, Jean-Christophe Aude b, Yves Boulard b, Sophie Combet d, Fabrice Cousin d, Stéphane Hourdez e, Jean Mary e, Jean- Philippe Renault a, Serge Pin a* aUniversité Paris-Saclay, CEA, CNRS, NIMBE, 91190 Gif-sur-Yvette, France bUniversité Paris-Saclay, CEA, CNRS, I2BC, B3S, 91190 Gif-sur-Yvette, France cUniversité Paris-Saclay, CNRS, Laboratoire de Physique des Solides, 91405 Orsay, France dUniversité Paris-Saclay, Laboratoire Léon-Brillouin, UMR 12 CEA-CNRS, CEA-Saclay, 91191 Gif-sur-Yvette Cedex, France eSorbonne Université, CNRS, Lab.
    [Show full text]
  • Molecular Weights of the Blood Pigments of the Invertebrates
    MARCH 4, 1933 NATURE invertebrates possess red blood corpuscles. So far, Letters to the Editor we have only had the opportunity of studying the respiratory proteins from two such species. It is [The Editor does not hold himself responsible for noteworthy that in both cases low sedimentation opinions expressed by his correspondents. Neither constants were found. can he undertake to return, nor to correspond with The constancy of the molecular weights of the the writers of, rejected manuscripts intended for this respiratory blood proteins within various animal or any other part of NATURE. No notice is taken groups becomes still more puzzling when the following of anonymous communications.] facts are taken into consideration. The erythro­ Molecular Weights of the Blood Pigments of the cruorin and the chlorocruorin of the polychoote Invertebrates worms, the erythrocruorin of Planorbis and the hoomocyanin of Calocharis, the erythrocruorin of the BY means of the ultra-centrifugal method, it has polychoote worms and the hoomocyanin of Sepia and recently been shown that the red blood pigment of probably the erythrocruorin of Daphnia and the the annelids is not identical with the hoomoglobin of hoomocyanin of Eupagurus have identical sedimenta­ the vertebrates as was previously assumed, but is a tion constants and therefore probably identical protein more allied to chlorocruorin and hoomocyanin molecular weights. The measurement of the absorp­ with regard to molecular weight'. It was suggested tion of light in the visible part of the spectrum for that a comparative study of the properties of the the blood proteins of the gastropods has further respiratory proteins throughout the animal kingdom shown that the hoomocyanins of Helix, Paludina and might bring to light interesting relationships between Littorina, which have the same molecular weight, the various groups of animals.
    [Show full text]
  • Erythrocruorin: a Possible Model (Proteins/Steady State/Photochemical Efficiency) G
    Proc. Nat. Acad. Sci. USA Vol. 72, No. 11, pp. 4313-4316, November 1975 Biochemistry Kinetics of binding of carbon monoxide to Lumbricus erythrocruorin: A possible model (proteins/steady state/photochemical efficiency) G. M. GIACOMETTI, A. FOCESI*, B. GIARDINA, M. BRUNORI, AND J. WYMAN C.N.R. Center of Molecular Biology, Institutes of Chemistry and Biochemistry, Faculty of Medicine of the University of Rome and the Regina Elena Institute for Cancer Research, Rome, Italy Contributed by J. Wynan, August 18,1975 ABSTRACT This paper represents a kinetic study of the A millimolar stock solution of carbon monoxide was pre- binding of carbon monoxide by Lumbricus erythrocruorin. pared by equilibrating degassed distilled water with gaseous Observations on the quantum yield and the relaxation of the CO at 1 atm (101.3 kPa) of partial pressure at 200. system both to equilibrium and to the steady state realized in The intensity of the photodissociating light, both in the the presence of constant illumination under various condi- flash and in the steady-state (continuous light) experiments, tions are reported. The results, besides indicating the exis- filters. The photolysis tence of at east two types of binding sites, give indications was controlled by the use of neutral as to the behavior of a complex polyfunctional molecule, apparatus was the same as that previously described (4). such as an enzyme, working under steady-state conditions. Kinetic experiments were analyzed with a Hewlett-Pack- ard model 9830 A desk computer. Photochemical efficiency This paper is a sequel to an earlier one on the binding of car- was determined by the "pulse method" previously described bon monoxide by erythrocruorin, the giant respiratory pro- (5).
    [Show full text]
  • Structure of Ferrous Forms of the Yellow Lupin Leghemoglobin T
    STRUCTURE OF FERROUS FORMS OF THE YELLOW LUPIN LEGHEMOGLOBIN T. N. SAFONO VA, A. V. TEPL YAKO V, G. V. OBMOL 0 VA, A. N. POPOV, I. P. KURANOVA, E. H. HARUTYUNYAN Institute of Crystallography , USSR Academy of Sciences , Moscow Legume hemoglobin - leghemoglobin (Lb) - was discovered by Kubo [ 1 ] in root nodules of leguminous plants. These nodules are a natu- ral nitrogen-fixing system which is a result of the symbiosis of high plants with the bacteria Rhysobium. Lb does not directly take part in nitrogen fi- xation. Possessing very high affinity for oxygen (Pso = 0.05 torr), Lb has a high combination rate constant k = 118 tM-'- sec' and a comparatively fast dissociation rate constant k = 4.4 sec' [2]. These properties mean that Lb may, on the one hand, maintain proper tension of oxygen in nodules and, on the other hand, provide transport of oxygen. In many respects (magnetic susceptibility data, spectroscopic data, etc.) Lb resembles animal hemoglobins and myoglobins. Its molecular weight is about 17000. Lb has the same type of polypeptide chain folding as other hemoglobins. Lb consists of 7 a-helices and a porphyrine group - the heme group (figure 1). We have studied deoxy-Lb and three ferrous complexes of leghemol- gobin with CO, NO and 0,. In nodules Lb was detected only in oxy and deoxy ferrous states. All experimental data sets were collected on a CARD-diffractometer with a multiwire detector at the Institute of Crystallography in Moscow [3]. Experimental data for LbO, were obtained in the atmosphere of argon at -20" C.
    [Show full text]
  • Expression, Purification, and Characterization of Mammalian and Earthworm Hemoglobins
    Expression, Purification, and Characterization of Mammalian and Earthworm Hemoglobins Dissertation Presented in Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the Graduate School of The Ohio State University By Jacob James Elmer, B.S. Chemical and Biomolecular Engineering Graduate Program The Ohio State University 2011 Dissertation Committee: Andre F. Palmer, Advisor David Wood Jessica Winter 1 Copyright by Jacob James Elmer 2011 2 Abstract The frequent shortages, risks of disease transmission, and storage issues associated with donated blood illustrate a significant demand for a red blood cell (RBC) substitute. Such a substitute should be able to effectively transport oxygen throughout the body with minimal side effects. Several hemoglobin-based oxygen carriers (HBOCs) have been developed and clinically tested, but they have all caused severe side effects. The problems associated with these HBOCs may all be attributed to removing hemoglobin from the RBC. Therefore, this work focuses on the use of the extracellular hemoglobin of the earthworm Lumbricus terrestris (LtEc) as a new class of HBOC. Since earthworms lack RBCs, their hemoglobin is freely dissolved in the bloodstream and has already adapted to solve many of the challenges facing modern synthetic HBOCs. It has a lower rate of oxidation, avoids harmful side reactions with nitric oxide (NO), and it is extremely stable. We have developed a novel purification technique to highly purify large amounts of LtEc at costs that are comparable to donated blood. The LtEc product also transports oxygen similarly to human blood. Transfusion of LtEc into hamsters does not elicit the harmful side effects observed with other HBOCs and preliminary studies have not revealed any immune or allergic reactions in vivo.
    [Show full text]
  • Harnessing the Evolutionary Information on Oxygen Binding Proteins Through Support Vector Machines Based Modules
    Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules Citation: Muthukrishnan, Selvaraj and Puri, Munish 2018, Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules, BMC research notes, vol. 11: 290, pp. 1-8. DOI: http://www.dx.doi.org/10.1186/s13104-018-3383-9 © 2018, The Authors Reproduced by Deakin University under the terms of the Creative Commons Attribution Licence Downloaded from DRO: http://hdl.handle.net/10536/DRO/DU:30113373 DRO Deakin Research Online, Deakin University’s Research Repository Deakin University CRICOS Provider Code: 00113B Muthukrishnan and Puri BMC Res Notes (2018) 11:290 https://doi.org/10.1186/s13104-018-3383-9 BMC Research Notes RESEARCH NOTE Open Access Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules Selvaraj Muthukrishnan1,2* and Munish Puri2,3* Abstract Objectives: The arrival of free oxygen on the globe, aerobic life is becoming possible. However, it has become very clear that the oxygen binding proteins are widespread in the biosphere and are found in all groups of organisms, including prokaryotes, eukaryotes as well as in fungi, plants, and animals. The exponential growth and availability of fresh annotated protein sequences in the databases motivated us to develop an improved version of “Oxypred” for identifying oxygen-binding proteins. Results: In this study, we have proposed a method for identifying oxy-proteins with two diferent sequence similar- ity cutofs 50 and 90%. A diferent amino acid composition based Support Vector Machines models was developed, including the evolutionary profles in the form position-specifc scoring matrix (PSSM).
    [Show full text]
  • Annelids in Extreme Aquatic Environments: Diversity, Adaptations and Evolution
    diversity Review Annelids in Extreme Aquatic Environments: Diversity, Adaptations and Evolution Christopher J. Glasby 1,2,*, Christer Erséus 3 and Patrick Martin 4 1 Natural Sciences, Museum & Art Gallery Northern Territory, PO Box 4646, Darwin, NT 0801, Australia 2 Research Institute for the Environment and Livelihoods, Charles Darwin University, Casuarina, NT 0810, Australia 3 Systematics and Biodiversity, Department of Biological and Environmental Sciences, University of Gothenburg, Box 463, SE-405 30 Göteborg, Sweden; [email protected] 4 Royal Belgian Institute of Natural Sciences, Taxonomy and Phylogeny, 29 rue Vautier, B-1000 Brussels, Belgium; [email protected] * Correspondence: [email protected] Abstract: We review the variety of morphological, physiological and behavioral modifications that annelids have acquired to cope with environments either unsuitable for, or on the limits of, survival for most animals. We focus on polychaetes (excluding sipunculans and echiurans) and clitellates (oligochaetes and leeches) and source information mostly from the primary literature. We identified many modifications common to both polychaetes and clitellates, and others that are specific to one or the other group. For example, certain land-adapted polychaetes show reduction in nuchal organs, epidermal ciliation and receptor cells, and other coastal polychaetes use adhesive glands and glue-reinforced tubes to maintain position in surf zones, while oligochaetes, with their simple body plans, appear to be ‘pre-adapted’ to life underground. Modifications common to both groups include the ability to construct protective cocoons, make cryoprotective substances such as Citation: Glasby, C.J.; Erséus, C.; antifreeze and heat shock proteins, develop gills, transform their bodies into a home for symbiotic Martin, P.
    [Show full text]
  • The Evolution of Land Plant Hemoglobins
    Plant Science 191–192 (2012) 71–81 Contents lists available at SciVerse ScienceDirect Plant Science jo urnal homepage: www.elsevier.com/locate/plantsci Review The evolution of land plant hemoglobins a b c a,∗ Consuelo Vázquez-Limón , David Hoogewijs , Serge N. Vinogradov , Raúl Arredondo-Peter a Laboratorio de Biofísica y Biología Molecular, Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, 62210 Cuernavaca, Morelos, Mexico b Institute of Physiology and Zürich Center for Integrative Human Physiology (ZIHP), University of Zürich, Zürich, Switzerland c Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, MI 48201, USA a r t i c l e i n f o a b s t r a c t Article history: This review discusses the evolution of land plant hemoglobins within the broader context of eukaryote Received 13 March 2012 hemoglobins and the three families of bacterial globins. Most eukaryote hemoglobins, including metazoan Received in revised form 24 April 2012 globins and the symbiotic and non-symbiotic plant hemoglobins, are homologous to the bacterial 3/3- Accepted 25 April 2012 fold flavohemoglobins. The remaining plant hemoglobins are homologous to the bacterial 2/2-fold group Available online 4 May 2012 2 hemoglobins. We have proposed that all eukaryote globins were acquired via horizontal gene transfer concomitant with the endosymbiotic events responsible for the origin of mitochondria and chloroplasts. Keywords: Although the 3/3 hemoglobins originated in the ancestor of green algae and plants prior to the emergence Hemoglobin Non-symbiotic of embryophytes at about 450 mya, the 2/2 hemoglobins appear to have originated via horizontal gene Leghemoglobin transfer from a bacterium ancestral to present day Chloroflexi.
    [Show full text]