Non-thermal effects of microwaves on proteins: thermophilic enzymes as model system.

FEBS letters · 1997 · Harm · Low evidence

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HarmLow evidencePaper 6337

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 an…

Study snapshot

PublicationFEBS letters · 1997
Study typein_vitro
Reported directionHarm
Evidence ratingLow

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.

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AI evidence extraction

Structured fields below were generated from the paper’s abstract and metadata to make the evidence easier to inspect. Automated extraction may be incomplete or incorrect; verify important details against the original paper.

Study typein_vitro
Effect directionharm
PopulationNot supplied
Sample sizeNot supplied
Exposuremicrowave · 10400 MHz
Evidence strengthLowConfidence: 74% · Peer reviewed: yes

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
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": 0.74,
  "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": 0.86,
      "reason": "Reports non-thermal microwave effects on protein structure and enzyme activity."
    }
  ]
}
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AI-extracted fields are generated from the abstract and metadata and may be incomplete or incorrect. This material is for informational purposes and is not medical advice.

Identifiers and source

DOI: 10.1016/s0014-5793(96)01505-0
PubMed: 9037175

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