Non-thermal effects of microwaves on proteins: thermophilic enzymes as model system.
Abstract
Two thermophilic and thermostable enzymes, isolated from Sulfolobus solfataricus, S-adenosylhomocysteine hydrolase and 5'-methylthioadenosine phosphorylase, were exposed to 10.4 GHz microwave radiation in order to discriminate between thermal and non-thermal microwave effects. The exposure causes a non-thermal, irreversible and time-dependent inactivation of both enzymes; the inactivation rate is related to the energy absorbed and is independent of the enzyme concentration. The influence of salts on enzyme inactivation has also been investigated. Conformational changes of S-adenosylhomocysteine hydrolase, detected by fluorescence and circular dichroism techniques, suggest that microwaves induce protein structural rearrangements not related to temperature.
AI evidence extraction
Main findings
Two thermophilic enzymes (S-adenosylhomocysteine hydrolase and 5'-methylthioadenosine phosphorylase) exposed to 10.4 GHz microwave radiation showed non-thermal, irreversible, time-dependent inactivation. The inactivation rate was related to absorbed energy and independent of enzyme concentration; conformational changes detected by fluorescence and circular dichroism suggested microwave-induced structural rearrangements not related to temperature.
Outcomes measured
- enzyme activity/inactivation
- protein conformational/structural changes (fluorescence, circular dichroism)
- influence of salts on inactivation
Limitations
- No exposure duration reported in abstract
- No SAR or dosimetry details reported in abstract beyond 'energy absorbed'
- In vitro enzyme model; relevance to whole organisms/humans not addressed in abstract
- Sample size/replicates not reported in abstract
Suggested hubs
-
mechanisms-non-thermal
(0.86) Reports non-thermal microwave effects on protein structure and enzyme activity.
View raw extracted JSON
{
"study_type": "in_vitro",
"exposure": {
"band": "microwave",
"source": null,
"frequency_mhz": 10400,
"sar_wkg": null,
"duration": null
},
"population": null,
"sample_size": null,
"outcomes": [
"enzyme activity/inactivation",
"protein conformational/structural changes (fluorescence, circular dichroism)",
"influence of salts on inactivation"
],
"main_findings": "Two thermophilic enzymes (S-adenosylhomocysteine hydrolase and 5'-methylthioadenosine phosphorylase) exposed to 10.4 GHz microwave radiation showed non-thermal, irreversible, time-dependent inactivation. The inactivation rate was related to absorbed energy and independent of enzyme concentration; conformational changes detected by fluorescence and circular dichroism suggested microwave-induced structural rearrangements not related to temperature.",
"effect_direction": "harm",
"limitations": [
"No exposure duration reported in abstract",
"No SAR or dosimetry details reported in abstract beyond 'energy absorbed'",
"In vitro enzyme model; relevance to whole organisms/humans not addressed in abstract",
"Sample size/replicates not reported in abstract"
],
"evidence_strength": "low",
"confidence": 0.7399999999999999911182158029987476766109466552734375,
"peer_reviewed_likely": "yes",
"keywords": [
"microwave radiation",
"10.4 GHz",
"non-thermal effects",
"thermophilic enzymes",
"Sulfolobus solfataricus",
"S-adenosylhomocysteine hydrolase",
"5'-methylthioadenosine phosphorylase",
"enzyme inactivation",
"protein conformational change",
"circular dichroism",
"fluorescence"
],
"suggested_hubs": [
{
"slug": "mechanisms-non-thermal",
"weight": 0.85999999999999998667732370449812151491641998291015625,
"reason": "Reports non-thermal microwave effects on protein structure and enzyme activity."
}
]
}
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