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Structural characterization of nitrimyoglobin.

L L Bondoc1, R Timkovich

  • 1Department of Chemistry, University of Alabama, Tuscaloosa 35487-0336.

The Journal of Biological Chemistry
|April 15, 1989
PubMed
Summary
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Nitrimyoglobin, a modified form of myoglobin, was synthesized with high yield. This new pigment retains myoglobin

Area of Science:

  • Biochemistry
  • Spectroscopy
  • Protein Chemistry

Background:

  • Myoglobin is a vital protein for oxygen transport.
  • Metmyoglobin is an oxidized form of myoglobin.
  • Nitrite reactions with proteins can lead to novel derivatives.

Purpose of the Study:

  • To synthesize and characterize nitrimyoglobin, a novel derivative of metmyoglobin.
  • To investigate the structural and functional properties of nitrimyoglobin.
  • To determine the site and specificity of the chemical modification.

Main Methods:

  • 1H and 15N Nuclear Magnetic Resonance (NMR) spectroscopy.
  • UV-visible spectroscopy.
  • Ligand binding assays (O2).
  • Heme extraction and porphyrin characterization.

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Main Results:

  • Nitrimyoglobin formed in >94% yield with high structural similarity to myoglobin.
  • Spectroscopic data confirmed a single nitro group addition at a specific heme position.
  • Nitrimyoglobin exhibited reversible O2 binding similar to myoglobin.
  • The modified heme structure was identified as 3-(trans-2-nitrovinyl)-2,7,12,18-tetramethyl-8-vinylporphyrin-13,17-dipropionic acid.

Conclusions:

  • Nitrimyoglobin is a stable, well-defined protein derivative.
  • The modification is regiospecific, occurring at the heme's 2-vinyl group.
  • Nitrimyoglobin retains key functional properties of myoglobin, including O2 binding.