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Rapid Generation of Amyloid from Native Proteins In vitro
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Nitrite catalyzes ferriheme protein reductive nitrosylation.

Bernadette O Fernandez1, Peter C Ford

  • 1Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, USA.

Journal of the American Chemical Society
|August 28, 2003
PubMed
Summary

Nitrite ions catalyze the reduction of methemoglobin and metmyoglobin. This reaction mechanism involves outer sphere reduction and the formation of dinitrogen trioxide, potentially modifying proteins.

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Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Bioinorganic Chemistry

Background:

  • Methemoglobin and metmyoglobin are iron-containing proteins crucial for oxygen transport.
  • Nitrite ion (NO2-) and nitric oxide (NO) play significant roles in biological systems.
  • Understanding the redox chemistry of heme proteins is vital for elucidating their function.

Purpose of the Study:

  • To investigate the catalytic role of nitrite ion in the reduction of methemoglobin and metmyoglobin.
  • To elucidate the mechanism of nitrite-catalyzed reduction of ferriheme proteins.
  • To explore the potential implications of reaction intermediates on protein structure.

Main Methods:

  • Spectrophotometric monitoring of ferriheme protein reduction.
  • Kinetic analysis of catalysis rate constants.
  • Comparison of protein and model system reduction potentials.

Main Results:

  • Nitrite ion was found to catalyze the NO reduction of methemoglobin and metmyoglobin at pH 7.0.
  • Catalysis rate constants correlated with FeIII/II reduction potentials of ferric nitrosyl complexes.
  • A mechanism involving outer sphere reduction of the FeIII(NO) center by NO2- was proposed.

Conclusions:

  • The proposed mechanism explains the observed catalytic activity of nitrite.
  • The formation of dinitrogen trioxide (N2O3) as a reaction intermediate was inferred.
  • N2O3 may lead to unintended protein modifications due to its strong nitrosating ability.