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PORPHYRIN COMPOUNDS DERIVED FROM BACTERIA.

F M Stone1, C B Coulter

  • 1Department of Bacteriology, College of Physicians and Surgeons, Columbia University, New York.

The Journal of General Physiology
|October 30, 2009
PubMed
Summary
This summary is machine-generated.

This study identifies a novel complex porphyrin in bacteria like B. phosphorescens and C. diphtheriae, distinct from cytochrome c. This porphyrin, potentially containing copper, may relate to bacterial toxin production.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Spectroscopy

Background:

  • Bacterial pigments share similarities with known heme compounds like cytochrome c.
  • Previous research indicated the presence of porphyrin-like substances in bacterial extracts, but their direct isolation from bacteria was challenging.

Purpose of the Study:

  • To characterize the pigment found in bacterial extracts of B. phosphorescens, yeast, and C. diphtheriae.
  • To investigate the nature and origin of a complex porphyrin observed in bacterial extracts and its potential relationship with toxin production.

Main Methods:

  • Spectroscopic analysis of pigments from bacterial extracts (B. phosphorescens, yeast, C. diphtheriae) using methods like freezing-thawing and alkaline extraction.
  • Chemical treatment of extracts with acetic acid to identify components.
  • Extraction of complex porphyrin from whole bacteria and culture filtrates using acetic acid-ether.
  • Microspectroscopic examination of diphtheria bacilli treated with glacial acetic acid.

Main Results:

  • Bacterial extracts contain pigments resembling cytochrome c and alpha-hematin, with distinct spectral bands.
  • A complex porphyrin, labile and yielding coproporphyrin and its copper compound upon disintegration, was successfully isolated directly from bacteria.
  • The complex porphyrin's spectral properties (bands at 575-574 nm and 539-535 nm) were characterized.
  • Copper was detected in extracts from washed bacteria, suggesting cellular uptake and potential incorporation into the porphyrin structure.
  • Treatment of C. diphtheriae with acetic acid caused cytochrome bands to fade, replaced by complex porphyrin bands.

Conclusions:

  • The isolated complex porphyrin is a distinct compound present within bacterial cells, not merely a degradation product.
  • This porphyrin may represent a cellular form of copper incorporation.
  • The presence and liberation of this porphyrin compound correlate with toxin production in C. diphtheriae, differentiating it from nonpathogenic strains.