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The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...
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ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
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Oxidation of aldehydes and ketones results in the formation of carboxylic acids. Aldehydes, bearing hydrogen next to the carbonyl group, are easily oxidized compared to ketones. This is because an aldehydic proton can easily be abstracted during oxidation.
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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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Proton transfer in oxidized adenosine self-aggregates.

Amedeo Capobianco1, Tonino Caruso, Maurizio Celentano

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This study investigates the electrochemical oxidation of adenosine using UV-vis and IR spectroscopy. Findings reveal a proton transfer process in oxidized adenosine, supported by theoretical computations.

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Area of Science:

  • Electrochemistry
  • Spectroscopy
  • Computational Chemistry

Background:

  • Adenosine is a fundamental nucleoside with diverse biological roles.
  • Understanding its electrochemical behavior is crucial for various applications.
  • Derivatization allows for tailored investigation of adenosine properties.

Purpose of the Study:

  • To investigate the electrochemical oxidation of derivatized adenosine.
  • To characterize the transient species formed during oxidation using spectroscopic methods.
  • To elucidate the mechanism of proton transfer in oxidized adenosine complexes.

Main Methods:

  • Potentiostatic oxidation of derivatized adenosine in dichloromethane.
  • In situ UV-vis and IR spectroscopy using an optically transparent thin layer electrode.
  • Theoretical computations (e.g., DFT) to model reaction intermediates and predict spectroscopic signals.

Main Results:

  • Observed broad Zundel-like absorption in oxidized adenosine spectra (2800-3600 cm⁻¹).
  • Spectroscopic evidence indicates an ongoing proton transfer process.
  • Theoretical calculations confirm favored proton transfer in oxidized 1:1 self-association complexes.

Conclusions:

  • Electrochemical oxidation of adenosine induces a significant proton transfer.
  • Spectroscopic and computational data provide a comprehensive understanding of the oxidation mechanism.
  • The study successfully assigns transient spectroscopic signals to specific oxidized adenosine species.