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Almarsson, O., Sinha, A., Gopinath, E. and Bruice, T.C. (1993) Mechanism of One-Electron Oxidation of NAD(P)H and Function of NADPH Bound to Catalase. Journal of the American Chemical Society, 115, 7093-7102.
https://doi.org/10.1021/ja00069a005

has been cited by the following article:

• TITLE: Remote Control of Bovine Catalase Activity with Specific Frequencies of Human and Bovine Catalase with and without Bound NADP+

  AUTHORS: Thibaud Etienne d’Oultremont

  KEYWORDS: Remote Control, Catalase, Frequency, Rate Promoting Vibration (RPV), NADP

  JOURNAL NAME: Advances in Enzyme Research, Vol.12 No.2, June 23, 2024

  ABSTRACT: Remote control enzyme technology is widely used today through resonance. In this study, we showed that the use of frequencies of the catalase enzyme itself to increase enzymatic rate is successful not only in test tubes but also remotely. The present study also suggests that, under optimal temperature, the use of bovine catalase frequency (the specific frequency of that enzyme) has a superior rate promoting vibration than the human catalase frequency, and so increases very significantly the chemical rate of bovine catalase (about 120% at 40˚C). It also suggests that bovine catalase subjected to bovine and human frequencies with catalase bound NADP+ experienced more resonance weight towards NADP+ and so were more slowly reduced back to catalase bound NADPH, increasing compound II formation rate, and slowing down the catalase activity rate.