IR exciton activation mechanism of ethanol oxidation by human alcohol dehydrogenase (ADH) 1A enzyme

Article Biochemistry & Molecular Biology

Contrary to consensus, oxidation of ethanol by human alcohol dehydrogenase (ADH) 1A is activated by ATP

Igor Khmelinskii et al.

Summary: New research finds that the enzymatic oxidation of ethanol is significantly accelerated by ADH1A alcohol dehydrogenase in the presence of ATP, by up to 20 times. This challenges the previous understanding of the role of ATP in ADH enzyme function and calls for a thorough revision of existing literature on ADH enzyme properties.

BIOCHIMIE (2022)

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Article Chemistry, Physical

Energy transfer along Muller cell intermediate filaments isolated from porcine retina: II. Excitons at 2500 cm-1 produced by ADH1A upon hydrolysis of one ATP molecule

Igor Khmelinskii et al.

Summary: The study found that the energy transfer of IR excitons in MC IFs is independent of ATP concentration. The emission spectra of IR excitons arriving to the other side of the capillary matrix varied depending on the exciton generation method. The results support new ideas on ATP energy transfer along protein filaments in vivo.

CHEMICAL PHYSICS LETTERS (2021)

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Article Spectroscopy

Energy transfer along Muller cell intermediate filaments isolated from porcine retina: I. Excitons produced by ADH1A dimers upon simultaneous hydrolysis of two ATP molecules

Igor Khmelinskii et al.

Summary: The study investigated the propagation of IR excitons in Muller cell intermediate filaments filled with a capillary matrix, generated by IR radiation or enzymatic ATP hydrolysis. The emission spectra of excitons depended on the generation method, with ATP-hydrolyzed excitons requiring energy contribution of two ATP molecules simultaneously. The results suggest that ATP-liberated energy could be transmitted along natural polypeptide nanofibers within and between live cells.

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY (2021)

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Article Physics, Fluids & Plasmas

Reaction coupling in ADH1A alcohol dehydrogenase enzyme by exciplex formation with adenosine diphosphate moderated by low-energy electronic excited states

Igor Khmelinskii et al.

Summary: Two commonly accepted theories about enzymes were revisited. The first states that ATP-stored energy is only released when the substrate is in place, and the second states that ATP-released energy moves along the enzyme molecule in the form of molecular vibrations. However, experimental evidence suggests that energy released upon ATP hydrolysis moves in the form of excited-state electrons, refuting these theories.

PHYSICAL REVIEW E (2021)

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Article Chemistry, Physical