2019
DOI: 10.1155/2019/7608512
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The Registration of a Biomaser-Like Effect in an Enzyme System with an RTM Sensor

Abstract: The concentration dependence of a microwave frequency radiation from a solution of a functioning enzyme system (ES) (with the example of cytochrome P450 BM3 (CYP102A1) system during lauric acid (LA) hydroxylation) has been studied with a radiothermometric sensor. Registration of the radiation from the enzyme solution has been performed in the frequency range from 3.4 to 4.2 GHz at the enzyme concentrations from 10−10 М to 10−6 М. It has been demonstrated that the catalysis of LA hydroxylation in a reconstitute… Show more

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Cited by 8 publications
(7 citation statements)
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“…The problem of the effect of microwave radiation on enzymes is of great interest. Particularly, this concerns the power range at the level of background radiation (~10 −12 W/cm 2 ), at which the radiation in enzyme systems is registered 29 and pathological changes in human are detected 30 . The impact of microwave radiation on proteins is determined by both the radiation power and the exposure time.…”
Section: Discussionmentioning
confidence: 99%
“…The problem of the effect of microwave radiation on enzymes is of great interest. Particularly, this concerns the power range at the level of background radiation (~10 −12 W/cm 2 ), at which the radiation in enzyme systems is registered 29 and pathological changes in human are detected 30 . The impact of microwave radiation on proteins is determined by both the radiation power and the exposure time.…”
Section: Discussionmentioning
confidence: 99%
“…This effect could be explained using biomaser hypothesis. Also, the synchronized pulsed radiation could indicate the generation of qubits in a biological system [34]. The similar 0.5 C microwave emission increase in passive mode and 2 C in excitation mode was observed in a solution of horseradish peroxidase (HRP).…”
Section: In Vitro Applicationsmentioning
confidence: 77%
“…Microwave emission has been observed as well -in the process of hydroxylation of enzyme CYP102 A1 [34]. The 0.5-2 C increase within 10-20 s in multi-pulse mode follows the addition of cosubstrate NADPH (0.2 mM) to the system containing lauric acid (0.5 mM), and enzyme 10 À10 to 10 À8 M. A single-pulse mode (synchronized pulse radiation) at 10 À6 M concentration of enzyme was observed.…”
Section: In Vitro Applicationsmentioning
confidence: 99%
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