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Relevant bibliographies by topics / Proton transfer reactions

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Journal articles

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"

1

Mijatović, Tea, Suzana Szilner, Lorenzo Corradi, 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

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2

Brzezinski, Peter, Joachim Reimann, and Pia Ädelroth. "Molecular architecture of the proton diode of cytochrome c oxidase." Biochemical Society Transactions 36, no. 6 (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.

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3

Pavošević, Fabijan, Sharon Hammes-Schiffer, Angel Rubio, and Johannes Flick. "Cavity-Modulated Proton Transfer Reactions." Journal of the American Chemical Society 144, no. 11 (2022): 4995–5002. http://dx.doi.org/10.1021/jacs.1c13201.

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4

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

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5

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

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6

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

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7

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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8

Kapral, Raymond, Styliani Consta, and Daniel Laria. "1996 Polanyi Award Lecture Proton reactions in clusters." Canadian Journal of Chemistry 75, no. 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

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9

Schmickler, Wolfgang. "The transfer coefficient in proton transfer reactions." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 284, no. 2 (1990): 269–77. http://dx.doi.org/10.1016/0022-0728(90)85037-6.

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10

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 (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 mech

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