Relevant bibliographies by topics / Proton transfer reactions

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Proton transfer reactions'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 January 2023

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Journal articles on the topic "Proton transfer reactions"

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Mijatović, Tea, Suzana Szilner, Lorenzo Corradi, Franco Galtarossa, Samuel Bakes, Daniele Brugnara, Gabriele Carozzi, et al. "Multinucleon transfer reactions and proton transfer channels." EPJ Web of Conferences 223 (2019): 01039. http://dx.doi.org/10.1051/epjconf/201922301039.

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Transfer reactions have always been of great importance for nuclear structure and reaction mechanism studies. So far, in multinucleon transfer studies, proton pickup channels have been completely identified in atomic and mass numbers at energies close to the Coulomb barrier only in few cases. We measured the multinucleon transfer reactions in the 40Ar+208Pb system near the Coulomb barrier, by employing the PRISMA magnetic spectrometer. By using the most neutron-rich stable 40Ar beam we could populate, besidesneutron pickup and proton stripping channels, also neutron stripping and proton pickup channels. Comparison ofcross sections between different systems with the 208Pb target and with projectiles going from neutron-poor to neutron-rich nuclei, as well as between the data and GRAZING calculations, was carried out.Finally, recent results concerning the measurement of the excitation function from the Coulomb barrier to far below for the 92Mo+54Fe system, where both proton stripping and pickup channels were populated with similar strength, will be discussed.
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Brzezinski, Peter, Joachim Reimann, and Pia Ädelroth. "Molecular architecture of the proton diode of cytochrome c oxidase." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1169–74. http://dx.doi.org/10.1042/bst0361169.

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CytcO (cytochrome c oxidase) is a membrane-bound multisubunit protein which catalyses the reduction of O2 to H2O. The reaction is arranged topographically so that the electrons and protons are taken from opposite sides of the membrane and, in addition, it is also linked to proton pumping across the membrane. Thus the CytcO moves an equivalent of two positive charges across the membrane per electron transferred to O2. Proton transfer through CytcO must be controlled by the protein to prevent leaks, which would dissipate the proton electrochemical gradient that is maintained across the membrane. The molecular mechanism by which the protein controls the unidirectionality of proton-transfer (cf. proton diode) reactions and energetically links electron transfer to proton translocation is not known. This short review summarizes selected results from studies aimed at understanding this mechanism, and we discuss a possible mechanistic principle utilized by the oxidase to pump protons.
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Pavošević, Fabijan, Sharon Hammes-Schiffer, Angel Rubio, and Johannes Flick. "Cavity-Modulated Proton Transfer Reactions." Journal of the American Chemical Society 144, no. 11 (March 10, 2022): 4995–5002. http://dx.doi.org/10.1021/jacs.1c13201.

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Brzezinski, Peter. "Proton-transfer reactions in bioenergetics." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1458, no. 1 (May 2000): 1–5. http://dx.doi.org/10.1016/s0005-2728(00)00056-6.

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Pines, E., and D. Huppert. "Geminate recombination proton-transfer reactions." Chemical Physics Letters 126, no. 1 (April 1986): 88–91. http://dx.doi.org/10.1016/0009-2614(86)85121-1.

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Meot-Ner, Michael. "Entropy-driven proton-transfer reactions." Journal of Physical Chemistry 95, no. 17 (August 1991): 6580–85. http://dx.doi.org/10.1021/j100170a039.

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J�rgensen, Solvejg, and Kurt V. Mikkelsen. "Proton transfer reactions in solution." International Journal of Quantum Chemistry 77, no. 1 (2000): 221–39. http://dx.doi.org/10.1002/(sici)1097-461x(2000)77:1<221::aid-qua21>3.0.co;2-6.

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Kapral, Raymond, Styliani Consta, and Daniel Laria. "1996 Polanyi Award Lecture Proton reactions in clusters." Canadian Journal of Chemistry 75, no. 1 (January 1, 1997): 1–8. http://dx.doi.org/10.1139/v97-001.

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Reactions in mesoscopic, molecular clusters may proceed by mechanisms and with rates that differ from those in bulk solvents. Two examples of reactions in large, liquid-state, molecular clusters are described to illustrate the distinctive features of these reactions: acid dissociation and proton transfer in aprotic, polar solvents. Both of these reactions involve proton dynamics so methods for dealing with mixed quantum–classical systems must be utilized to investigate the reaction dynamics. Surface versus bulk solvation effects play an important role in determining the reaction mechanisms as do the strong cluster fluctuations. Mechanisms for proton transfer within clusters that have no bulk analogs will be described. Keywords: proton reactions, mesoscopic clusters.
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Schmickler, Wolfgang. "The transfer coefficient in proton transfer reactions." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 284, no. 2 (May 1990): 269–77. http://dx.doi.org/10.1016/0022-0728(90)85037-6.

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STUCHEBRUKHOV, ALEXEI A. "ELECTRON TRANSFER REACTIONS COUPLED TO PROTON TRANSLOCATION: CYTOCHROME OXIDASE, PROTON PUMPS, AND BIOLOGICAL ENERGY TRANSDUCTION." Journal of Theoretical and Computational Chemistry 02, no. 01 (March 2003): 91–118. http://dx.doi.org/10.1142/s0219633603000318.

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Cytochrome oxidase (COX) is the terminal component of electron transport chain of the respiratory system in mitochondria, and one of the key enzymes responsible for energy generation in cells. COX functions as a proton pump that utilizes free energy of oxygen reduction for translocation of protons across the mitochondrion membrane. The proton gradient created in the process is later utilized to drive synthesis of ATP. Although the structure of COX has been recently resolved, the molecular mechanism of proton pumping remains unknown. In this paper, general principles and possible molecular mechanisms of energy transformations in this enzyme will be discussed. The main question is how exactly chemical energy of oxygen reduction and water formation is transformed into a proton gradient; or, how exactly electron transfer reactions are utilized to translocate protons across the mitochondrion membrane against the electrochemical gradient. A key to the solution of this problem is in understanding correlated transport of electrons and protons. Here, theoretical models are discussed for coupled electron and proton transfer reactions in which an electron is tunneling over long distance between two redox cofactors, and a coupled proton is moving along a proton conducting channel in a classical, diffusion-like random walk fashion. Such reactions are typical for COX and other enzymes involved in biological energy transformations.
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Dissertations / Theses on the topic "Proton transfer reactions"

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Redondo, Marey Carmen-Maria. "Femtodynamics of double proton transfer reactions." Thesis, University College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.398981.

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Linares-Samaniego, Sandra I. "Excited state proton transfer in microheterogeneous conditions." Diss., Georgia Institute of Technology, 1997. http://hdl.handle.net/1853/27263.

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Papageorgiou, Alexia. "Influence of proton transfer kinetics and natural convection on Proton-Coupled Electron Transfer (PCET) reactions." Doctoral thesis, Universite Libre de Bruxelles, 2021. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/318308.

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Les phénomènes de transport de matière ainsi que la cinétique des réactions chimiques sont des processus importants en électrochimie car ceux-ci contrôlent le courant mesuré. Dans ce contexte, nous nous intéressons à de simples réactions électrochimiques et à la classe des réactions de transfert couplés électrons-protons (PCET), jouant un rôle important dans les phénomènes biologiques et la conversion d’énergie. Ces réactions impliquent le transfert d’électron(s) et de proton(s) et sont représentées par un schéma carré. Alors que la cinétique de transfert d’électrons est largement étudiée, la cinétique de transfert de protons l’est plus rarement. Ces réactions sont en effet supposées être très rapides alors qu’il existe des situations où les réactions de protonation constituent l’étape limitante. La première partie de la thèse consiste à étudier la cinétique des réactions de protonation en tenant compte de la catalyse de Brönsted. Par le biais de simulations numériques, nous montrons que la catalyse augmente la réversibilité des voltampérogrammes cycliques, à des pH où le transfert couplé s’opère. Les prédictions numériques ont été comparées aux données expérimentales et les résultats sont encourageants car une même tendance est observée. L’accord quantitatif n’est cependant pas satisfaisant à ce stade. Les phénomènes de transport étant connus pour affecter les processus à l’électrode, la seconde partie de la thèse est consacrée à l’étude de l’influence de la convection. Nous commençons par présenter les différentes raisons qui peuvent expliquer les déviations expérimentales par rapport à la diffusion seule, comme la convection naturelle induite par des gradients de densité ou de tension superficielle. Nous présentons le concept de convection spontanée associé aux mouvements microscopiques de la solution. Bien que les fondements théoriques de la convection spontanée soient discutables, la théorie permet de reproduire les résultats d’un certain nombre d’expériences, souvent pratiquées en conditions non contrôlées. Ensuite, nous évaluons l’influence de la convection naturelle sur de simples réactions électrochimiques, avant de passer à l’étude des réactions PCET. Les simulations numériques nous ont permis de prévoir la déviation des chronoampérogrammes par rapport à une situation diffusive en fonction de la durée de l’expérience et de la contribution de chaque espèce à la densité de la solution. Pour une électrode située au bord supérieur, la production d’espèces plus denses amène une déviation du courant plus importante, dû au développement d’instabilités hydrodynamiques. La convection due aux gradients de densité est supposée être accentuée lorsque que les réactions électrochimiques sont couplées avec des réactions chimiques, ce qui est la définition même des PCET. Cependant, nous avons conclu à un impact négligeable de celles-ci, sauf pour de faibles valeurs de constantes cinétiques. Pour conclure, nous avons évalué d’une part l’impact de la convection due aux effets Marangoni et d’autre part son couplage à la convection induite par des gradients de densité. L’influence de ces mouvements convectifs sur le courant résultant dépend des propriétés des réactifs et des produits de la réaction, mais également de la présence d’une surface libre.
Doctorat en Sciences
info:eu-repo/semantics/nonPublished
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Cooper, Ian Blake. "Photosynthetic water oxidation and proton-coupled electron transfer." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/26707.

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Thesis (Ph. D.)--Chemistry and Biochemistry, Georgia Institute of Technology, 2009.
Committee Chair: Bridgette Barry; Committee Member: El-Sayed, Mostafa; Committee Member: Fahrni, Christoph; Committee Member: Kröger, Nils; Committee Member: McCarty, Nael. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Fernandez, M. T. N. "Thermodynamics of proton transfer reactions in the gas phase." Thesis, University of Warwick, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.378296.

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Jenson, David L. Jenson. "Proton-coupled electron transfer and tyrosine D of phototsystem II." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/29667.

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Thesis (Ph. D.)--Chemistry and Biochemistry, Georgia Institute of Technology, 2010.
Committee Chair: Bridgette Barry; Committee Member: Ingeborg Schmidt-Krey; Committee Member: Jake Soper; Committee Member: Nils Kroger; Committee Member: Wendy Kelly. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Maza, William Antonio. "Reaction Enthalpy and Volume Profiles for Excited State Reactions Involving Electron Transfer and Proton-Coupled Electron Transfer." Scholar Commons, 2013. http://scholarcommons.usf.edu/etd/4539.

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Electron transfer, ET, and proton-coupled electron transfer, PCET, reactions are central to biological reactions involving catalysis, energy conversion and energy storage. The movement of electrons and protons in either a sequential or concerted manner are coupled in a series of elementary reaction steps in respiration and photosynthesis to harvest and convert energy consumed in foodstuffs or by absorption of light into high energy chemi-cal bonds in the form of ATP. These electron transfer processes may be modulated by conformational dynamics within the protein matrix or at the protein-protein interface, the energetics of which are still not well understood. Photoacoustic calorimetry is an estab-lished method of obtaining time-resolved reaction enthalpy and volume changes on the nanosecond to microsecond timescale. Photoacoustic calorimetry is used here to probe 1) the energetics and volume changes for ET between the self-assembled anionic uroporphy-rin:cytochrome c complex and the role of the observed volume changes in modulating ET within the complex, 2) the enthalpy and volume change for the excited state PCET reac-tion of a tyramine functionalized ruthenium(II) bis-(2,2'-bipyridine)(4-carboxy-4'-methyl-2,2'-bipyrine) meant to be a model for the tyrosine PCET chemistry carried out by cyto-chrome c oxidase and photosystem II, 3) the enthalpy and volume changes related to car-bon monoxide and tryptophan migration in heme tryptophan catabolic enzyme indoleam-ine 2,3-dioxygenase.
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Murphy, Christine Fecenko Thorp H. Holden. "Coupled electron proton transfer reactions in biological redox active substrates." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2009. http://dc.lib.unc.edu/u?/etd,2895.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2010.
Title from electronic title page (viewed Jun. 23, 2010). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Chemistry." Discipline: Chemistry; Department/School: Chemistry.
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Marks, David Roland Azoulai. "Femtosecond studies of excited-state proton transfer reactions in solutions." [S.l. : Amsterdam : s.n.] ; Universiteit van Amsterdam [Host], 2000. http://dare.uva.nl/document/82013.

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Meng, Kejie. "MECHANISTIC STUDIES OF PROTON-COUPLED ELECTRON TRANSFER REACTIONS INVOLVING ANTIOXIDANTS." VCU Scholars Compass, 2018. https://scholarscompass.vcu.edu/etd/5498.

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The objective of the research was to investigate proton-coupled electron transfer (PCET) reactions involving antioxidants to gain insight into the detailed mechanisms of glutathione (GSH), Trolox, and α-tocopherol (α-TOH). PCET reactions are complex redox reactions that transfer electrons and protons sequentially or in concert. These reactions are ubiquitous in natural or artificial processes that produce electrochemical energy that is extractable as electricity or as chemical fuels of high energy content. Examples of processes based on PCET are photosynthesis, respiration, nitrogen fixation, carbon dioxide reduction, redox fuel cells, and artificial photosynthesis. Antioxidants were selected as a PCET model to understand the coupling between proton transfer (PT) and electron transfer (ET) in order to elucidate structure-reactivity relationships under different experimental conditions. PCET reactions were studied with a set of electrochemical techniques to propose a preliminary mechanism that could be validated with digital simulations matching the electrochemical response. In some cases, other analytical techniques were used to aid in the system characterization. This thesis presents the results and discussion of the effects of oxidant-base pairs on the mediated oxidation of GSH, the -2e-/-H+ process of Trolox in aqueous and nonaqueous solvents with various pH values, and the particle collision electrolysis of α-tocopherol in oil-in-water emulsion droplets on an ultramicroelectrode. Ultimately our goal was to determine the kinetic and thermodynamic factors that control PCET reactions so that they can be applied in designing artificial systems for the production of energy using more abundant reagents with lower cost and better yields.
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Books on the topic "Proton transfer reactions"

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Bountis, T. Proton transfer in hydrogen-bonded systems. New York: Springer Science+Business Media, LLC, 1992.

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Fernandez, M. Tereza N. Thermodynamics of proton transfer reactions in the gas phase. [s.l.]: typescript, 1986.

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Ilczyszyn, Marek. Mechanizmy protonowania amin i ich analogów w aprotycznych rozpuszczalnikach. Wrocław: Wydawn. Uniwersytetu Wrocławskiego, 1996.

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Barker, David. [ Superior] 14C induced two proton transfer reactions on f-p shell nuclei. Birmingham: University of Birmingham, 1986.

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T, Elsässer, and Bakker Huib J, eds. Ultrafast hydrogen bonding dynamics and proton transfer processes in the condensed phase. Dordrecht: Kluwer Academic Publishers, 2002.

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Jankowski, Andrzej. Spektrofluorymetryczne badania nad mechanizmem przeniesienia protonu w biopolimerach. Wrocław: Wydawn. Uniwersytetu Wrocławskiego, 1996.

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Kryschi, Carola. Relaxation dynamics in molecular crystals. Berlin: Verlag Köster, 1994.

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Tucs, Eric R. Ligand and proton transfer reactions in a series of RePt and MnPt bimetallic systems. Ottawa: National Library of Canada, 1990.

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Ellis, Andrew M., and Christopher A. Mayhew. Proton Transfer Reaction Mass Spectrometry. Chichester, UK: John Wiley & Sons, Ltd, 2014. http://dx.doi.org/10.1002/9781118682883.

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Caldin, E. F., and Victor Gold. Proton-Transfer Reactions. Springer London, Limited, 2013.

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Book chapters on the topic "Proton transfer reactions"

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Borgis, Daniel, and James T. Hynes. "Proton Transfer Reactions." In The Enzyme Catalysis Process, 293–303. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-1607-8_20.

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Agmon, Noam. "Excited State Proton Transfer Reactions." In Theoretical and Computational Models for Organic Chemistry, 315–34. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3584-9_14.

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Grunwald, Ernest. "Ultra-Fast Proton-Transfer Reactions." In Progress in Physical Organic Chemistry, 317–58. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470171820.ch5.

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Minkin, Vladimir I., Boris Ya Simkin, and Ruslan M. Minyaev. "Electron and Proton Transfer Reactions." In Quantum Chemistry of Organic Compounds, 210–37. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-75679-5_9.

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DePuy, Charles H., and Veronica M. Bierbaum. "Proton Transfer Reactions of Anions." In Structure/Reactivity and Thermochemistry of Ions, 293–303. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3787-1_15.

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Jones, J. R. "Proton Transfer Reactions in Highly Basic Media." In Progress in Physical Organic Chemistry, 241–74. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470171882.ch5.

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Brenner, Sibylle, Sam Hay, Derren J. Heyes, and Nigel S. Scrutton. "Chapter 3. Experimental Approaches Towards Proton-Coupled Electron Transfer Reactions in Biological Redox Systems." In Proton-Coupled Electron Transfer, 57–88. Cambridge: Royal Society of Chemistry, 2011. http://dx.doi.org/10.1039/9781849733168-00057.

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Warren, Jeffrey J., and James M. Mayer. "Chapter 1. Application of the Marcus Cross Relation to Hydrogen Atom Transfer/Proton-Coupled Electron Transfer Reactions." In Proton-Coupled Electron Transfer, 1–31. Cambridge: Royal Society of Chemistry, 2011. http://dx.doi.org/10.1039/9781849733168-00001.

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Fukuzumi, Shunichi. "Proton-Coupled Electron Transfer in Hydrogen and Hydride Transfer Reactions." In Physical Inorganic Chemistry, 39–74. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470602577.ch2.

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Warshel, A. "Simulations of Proton Transfer and Hydride Transfer Reactions in Proteins." In Molecular Aspects of Biotechnology: Computational Models and Theories, 175–91. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2538-3_8.

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Conference papers on the topic "Proton transfer reactions"

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Siwick, Bradley J., and Huib J. Bakker. "The Role of Water in Intermolecular Proton Transfer Reactions." In International Conference on Ultrafast Phenomena. Washington, D.C.: OSA, 2006. http://dx.doi.org/10.1364/up.2006.tuf3.

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Kumar, P. Rajesh, and Bernardine Renaldo Wong. "Analytical Proton Transfer Amplitude for Heavy Ion Induced Nuclear Reactions." In MALAYSIA ANNUAL PHYSICS CONFERENCE 2010 (PERFIK-2010). AIP, 2011. http://dx.doi.org/10.1063/1.3573702.

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FOLMER, D. E., E. S. WISNIEWSKI, and A. W. CASTLEMAN. "THE EFFECTS OF WATER SOLVATION OF DOUBLE PROTON TRANSFER REACTIONS." In Proceedings of the International Symposium. WORLD SCIENTIFIC, 2000. http://dx.doi.org/10.1142/9789812793805_0063.

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Douhal, Abderrazzak, Mikel Sanz, María Ángeles Carranza, Juan Ángel Organero, and Laura Tormo. "Femtochemistry of Intramolecular Charge and Proton Transfer Reactions in Solution." In MODERN TRENDS IN PHYSICS RESEARCH: First International Conference on Modern Trends in Physics Research; MTPR-04. American Institute of Physics, 2005. http://dx.doi.org/10.1063/1.1896490.

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Grabowska, A. "Proton transfer reactions prepared by the hydrogen bonds in electronically excited polyatomic molecules." In Ultrafast reaction dynamics and solvent effects. AIP, 1994. http://dx.doi.org/10.1063/1.45385.

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Borgis, D. "Theory and simulation of proton transfer reactions along weak and strong H bonds in solution." In Ultrafast reaction dynamics and solvent effects. AIP, 1994. http://dx.doi.org/10.1063/1.45382.

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Winghart, Marc-Oliver, Peng Han, Zhuang-Yan Zhang, Rolf Mitzner, Mattis Fondell, Ehud Pines, Michael Odelius, Philippe Wernet, and Erik T. J. Nibbering. "Ultrafast Electronic Structural Dynamics of Water-Mediated Photoacid-Base Proton Transfer Reactions." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 2022. http://dx.doi.org/10.1364/up.2022.th4a.6.

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We determine how the transient electronic structure changes of imidazole base upon proton transfer from a naphthol photoacid in aqueous solution can be locally monitored with ultrafast nitrogen K-edge spectroscopy.
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Löhmannsröben, Hans-Gerd, Toralf Beitz, and Robert Laudien. "Kinetic investigations of proton transfer and complex formation reactions by laser ion mobility spectrometry." In Optics East 2006, edited by Tuan Vo-Dinh, Robert A. Lieberman, and Günter Gauglitz. SPIE, 2006. http://dx.doi.org/10.1117/12.685370.

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Ayyad, Y., J. Lee, A. Tamii, N. Aoi, H. Fujita, Y. Fujita, E. Ganioglu, et al. "Investigating Neutron-Proton Pairing insd-Shell Nuclei via (p,3He) and (3He,p) Transfer Reactions." In Proceedings of the Conference on Advances in Radioactive Isotope Science (ARIS2014). Journal of the Physical Society of Japan, 2015. http://dx.doi.org/10.7566/jpscp.6.030039.

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Kato, Nobuhiko. "Theoretical study on the effect of solvent and intermolecular fluctuations in proton transfer reactions: General theory." In SLOW DYNAMICS IN COMPLEX SYSTEMS: 3rd International Symposium on Slow Dynamics in Complex Systems. AIP, 2004. http://dx.doi.org/10.1063/1.1764291.

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Reports on the topic "Proton transfer reactions"

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Schwartz, Benjamin Joel. Femtosecond dynamics of fundamental reaction processes in liquids: Proton transfer, geminate recombination, isomerization and vibrational relaxation. Office of Scientific and Technical Information (OSTI), November 1992. http://dx.doi.org/10.2172/10131752.

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Schwartz, B. J. Femtosecond dynamics of fundamental reaction processes in liquids: Proton transfer, geminate recombination, isomerization and vibrational relaxation. [Spiropyrans]. Office of Scientific and Technical Information (OSTI), November 1992. http://dx.doi.org/10.2172/6666275.

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Barefoot, Susan F., Bonita A. Glatz, Nathan Gollop, and Thomas A. Hughes. Bacteriocin Markers for Propionibacteria Gene Transfer Systems. United States Department of Agriculture, June 2000. http://dx.doi.org/10.32747/2000.7573993.bard.

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The antibotulinal baceriocins, propionicin PLG-1 and jenseniin G., were the first to be identified, purified and characterized for the dairy propionibaceria and are produced by Propionibacterium thoenii P127 and P. thoenii/jensenii P126, respectively. Objectives of this project were to (a) produce polyclonal antibodies for detection, comparison and monitoring of propionicin PLG-1; (b) identify, clone and characterize the propionicin PLG-1 (plg-1) and jenseniin G (jnG) genes; and (3) develop gene transfer systems for dairy propionibacteria using them as models. Polyclonal antibodies for detection, comparison and monitoring of propionicin PLG-1 were produced in rabbits. Anti-PLG-1 antiserum had high titers (256,000 to 512,000), neutralized PLG-1 activity, and detected purified PLG-1 at 0.10 mg/ml (indirect ELISA) and 0.033 mg/ml (competitive indirect ELISA). Thirty-nine of 158 strains (most P. thoenii or P. jensenii) yielded cross-reacting material; four strains of P. thoenii, including two previously unidentified bacteriocin producers, showed biological activity. Eight propionicin-negative P127 mutants produced neither ELISA response nor biological activity. Western blot analyses of supernates detected a PLG-1 band at 9.1 kDa and two additional protein bands with apparent molecular weights of 16.2 and 27.5 kDa. PLG-1 polyclonal antibodies were used for detection of jenseniin G. PLG-1 antibodies neutralized jenseniin G activity and detected a jenseniin G-sized, 3.5 kDa peptide. Preliminary immunoprecipitation of crude preparations with PLG-1 antibodies yielded three proteins including an active 3-4 kDa band. Propionicin PLG-1 antibodies were used to screen a P. jensenii/thoenii P126 genomic expression library. Complete sequencing of a cloned insert identified by PLG-1 antibodies revealed a putative response regulator, transport protein, transmembrane protein and an open reading frame (ORF) potentially encoding jenseniin G. PCR cloning of the putative plg-1 gene yielded a 1,100 bp fragment with a 355 bp ORF encoding 118 amino acids; the deduced N-terminus was similar to the known PLG-1 N-terminus. The 118 amino acid sequence deduced from the putative plg-1 gene was larger than PLG-1 possibly due to post-translational processing. The product of the putative plg-1 gene had a calculated molecular weight of 12.8 kDa, a pI of 11.7, 14 negatively charged residues (Asp+Glu) and 24 positively charged residues (Arg+Lys). The putative plg-1 gene was expressed as an inducible fusion protein with a six-histidine residue tag. Metal affinity chromatography of the fused protein yielded a homogeneous product. The fused purified protein sequence matched the deduced putative plg-1 gene sequence. The data preliminarily suggest that both the plg-1 and jnG genes have been identified and cloned. Demonstrating that antibodies can be produced for propionicin PLG-1 and that those antibodies can be used to detect, monitor and compare activity throughout growth and purification was an important step towards monitoring PLG-1 concentrations in food systems. The unexpected but fortunate cross-reactivity of PLG-1 antibodies with jenseniin G led to selective recovery of jenseniin G by immunoprecipitation. Further refinement of this separation technique could lead to powerful affinity methods for rapid, specific separation of the two bacteriocins and thus facilitate their availability for industrial or pharmaceutical uses. Preliminary identification of genes encoding the two dairy propionibacteria bacteriocins must be confirmed; further analysis will provide means for understanding how they work, for increasing their production and for manipulating the peptides to increase their target species. Further development of these systems would contribute to basic knowledge about dairy propionibacteria and has potential for improving other industrially significant characteristics.
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4

Ohad, Itzhak, and Himadri Pakrasi. Role of Cytochrome B559 in Photoinhibition. United States Department of Agriculture, December 1995. http://dx.doi.org/10.32747/1995.7613031.bard.

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The aim of this research project was to obtain information on the role of the cytochrome b559 in the function of Photosystem-II (PSII) with special emphasis on the light induced photo inactivation of PSII and turnover of the photochemical reaction center II protein subunit RCII-D1. The major goals of this project were: 1) Isolation and sequencing of the Chlamydomonas chloroplast psbE and psbF genes encoding the cytochrome b559 a and b subunits respectively; 2) Generation of site directed mutants and testing the effect of such mutation on the function of PSII under various light conditions; 3) To obtain further information on the mechanism of the light induced degradation and replacement of the PSII core proteins. This information shall serve as a basis for the understanding of the role of the cytochrome b559 in the process of photoinhibition and recovery of photosynthetic activity as well as during low light induced turnover of the D1 protein. Unlike in other organisms in which the psbE and psbF genes encoding the a and b subunits of cytochrome b559, are part of an operon which also includes the psbL and psbJ genes, in Chlamydomonas these genes are transcribed from different regions of the chloroplast chromosome. The charge distribution of the derived amino-acid sequences of psbE and psbF gene products differs from that of the corresponding genes in other organisms as far as the rule of "positive charge in" is concerned relative to the process of the polypeptide insertion in the thylakoid membrane. However, the sum of the charges of both subunits corresponds to the above rule possibly indicating co-insertion of both subunits in the process of cytochrome b559 assembly. A plasmid designed for the introduction of site-specific mutations into the psbF gene of C. reinhardtii. was constructed. The vector consists of a DNA fragment from the chromosome of C. reinhardtii which spans the region of the psbF gene, upstream of which the spectinomycin-resistance-conferring aadA cassette was inserted. This vector was successfully used to transform wild type C. reinhardtii cells. The spectinomycin resistant strain thus obtained can grow autotrophically and does not show significant changes as compared to the wild-type strain in PSII activity. The following mutations have been introduced in the psbF gene: H23M; H23Y; W19L and W19. The replacement of H23 involved in the heme binding to M and Y was meant to permit heme binding but eventually alter some or all of the electron transport properties of the mutated cytochrome. Tryptophane W19, a strictly conserved residue, is proximal to the heme and may interact with the tetrapyrole ring. Therefore its replacement may effect the heme properties. A change to tyrosine may have a lesser affect on the potential or electron transfer rate while a replacement of W19 by leucine is meant to introduce a more prominent disturbance in these parameters. Two of the mutants, FW19L and FH23M have segregated already and are homoplasmic. The rest are still grown under selection conditions until complete segregation will be obtained. All mutants contain assembled and functional PSII exhibiting an increased sensitivity of PSII to the light. Work is still in progress for the detailed characterization of the mutants PSII properties. A tobacco mutant, S6, obtained by Maliga and coworkers harboring the F26S mutation in the b subunit was made available to us and was characterized. Measurements of PSII charge separation and recombination, polypeptide content and electron flow indicates that this mutation indeed results in light sensitivity. Presently further work is in progress in the detailed characterization of the properties of all the above mutants. Information was obtained demonstrating that photoinactivation of PSII in vivo initiates a series of progressive changes in the properties of RCII which result in an irreversible modification of the RCII-D1 protein leading to its degradation and replacement. The cleavage process of the modified RCII-D1 protein is regulated by the occupancy of the QB site of RCII by plastoquinone. Newly synthesized D1 protein is not accumulated in a stable form unless integrated in reassembled RCII. Thus the degradation of the irreversibly modified RCII-D1 protein is essential for the recovery process. The light induced degradation of the RCII-D1 protein is rapid in mutants lacking the pD1 processing protease such as in the LF-1 mutant of the unicellular alga Scenedesmus obliquus. In this case the Mn binding site of PSII is abolished, the water oxidation process is inhibited and harmful cation radicals are formed following light induced electron flow in PSII. In such mutants photo-inactivation of PSII is rapid, it is not protected by ligands binding at the QB site and the degradation of the inactivated RCII-D1 occurs rapidly also in the dark. Furthermore the degraded D1 protein can be replaced in the dark in absence of light driven redox controlled reactions. The replacement of the RCII-D1 protein involves the de novo synthesis of the precursor protein, pD1, and its processing at the C-terminus end by an unknown processing protease. In the frame of this work, a gene previously isolated and sequenced by Dr. Pakrasi's group has been identified as encoding the RCII-pD1 C-terminus processing protease in the cyanobacterium Synechocystis sp. PCC 6803. The deduced sequence of the ctpA protein shows significant similarity to the bovine, human and insect interphotoreceptor retinoid-binding proteins. Results obtained using C. reinhardtii cells exposes to low light or series of single turnover light flashes have been also obtained indicating that the process of RCII-D1 protein turnover under non-photoinactivating conditions (low light) may be related to charge recombination in RCII due to back electron flow from the semiquinone QB- to the oxidised S2,3 states of the Mn cluster involved in the water oxidation process.
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