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Modeling low-pH hemoproteins.

L A Andersson1, M Mylrajan, E P Sullivan

  • 1Department of Chemical and Biological Sciences, Oregon Graduate Center, Beaverton 97006-1999.

The Journal of Biological Chemistry
|November 15, 1989
PubMed
Summary
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A novel spectral signature for a proposed low-pH heme intermediate was identified using resonance Raman spectroscopy. This finding helps verify the existence and function of this key biological molecule.

Area of Science:

  • Biochemistry
  • Spectroscopy
  • Bioinorganic Chemistry

Background:

  • A tetracoordinate ferrous heme intermediate is hypothesized at low pH (<3.0) in hemoproteins.
  • This intermediate is thought to form via proximal histidine N(epsilon) protonation and Fe-N(epsilon) bond cleavage.

Purpose of the Study:

  • To establish a distinct spectral signature for the proposed low-pH tetracoordinate heme species.
  • To provide a method for verifying the existence and functional significance of this intermediate.

Main Methods:

  • Soret excitation resonance Raman spectroscopy was employed.
  • Crystallographically defined tetracoordinate iron(II)-octaethylporphyrin (Fe.OEP) was studied.
  • Spectra were compared to other ferrous and ferric heme complexes.

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Main Results:

  • High-frequency resonance Raman spectral features (>900 cm-1) of Fe.OEP were distinct from other ferrous heme coordination states.
  • These features align with frequencies typically observed for low-spin hexacoordinate ferric porphyrins.
  • Little macrocycle effect was observed on Raman frequencies above 900 cm-1.

Conclusions:

  • A testable spectral signature for the proposed tetracoordinate ferrous heme intermediate has been established.
  • This signature can be used to verify the presence and investigate the function of this low-pH biological intermediate.