Open AccessWhy is catalase so fast?
Author(s) -
Lionel R. Milgrom
Publication year - 2021
Publication title -
international journal of high dilution research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.129
H-Index - 9
ISSN - 1982-6206
DOI - 10.51910/ijhdr.v15i4.865
Subject(s) - catalase , disproportionation , hydrogen peroxide , enzyme , chemistry , molecule , hydrogen molecule , biochemistry , aqueous solution , biophysics , catalysis , biology , organic chemistry
ded network of hydrogen-bonded water and H2O2 molecules, stretching out far beyond the enzymes’ active sites, into the cell's internal aqueous medium. As catalases function, they provide coherent oxidative ‘pulses’, which rapidly spread throughout the H-bonded network, effectively ‘unzipping’ H2O2 molecules as far as they extend from the enzyme.
Result/discussion: This 'memory-of-water'-like mechanism predicts catalase H2O2 disproportionation should occur outside the enzyme. An experimental protocol is proposed to test this prediction. If successful, it would suggest a) holistic re-appraisal of the conventional mechanistic framework of enzyme kinetics is required, and b) should encourage more research into understanding the biochemical effects of CAM therapies.
Keywords: Holistic biochemistry; catalase enzymes; hydrogen peroxide disproportionation; hydrogen-bonded networks; memory of water.