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Nitric oxide generation from heme/copper assembly mediated nitrite reductase activity.

Shabnam Hematian1, Maxime A Siegler, Kenneth D Karlin

  • 1Department of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|January 17, 2014
PubMed
Summary

This study investigates how heme and copper complexes convert nitrite to nitric oxide (NO). Different binding modes of nitrite to copper affect reaction rates, with heme acting as the electron source but not limiting the overall speed.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Chemical Biology

Background:

  • Nitric oxide (NO) is a crucial signaling molecule and vasodilator.
  • Nitrite (NO2-) recycling generates NO, especially under hypoxic or ischemic conditions.
  • The heme a 3/CuB active site of cytochrome c oxidase converts nitrite to NO.

Purpose of the Study:

  • To further investigate the nitrite reductase chemistry of heme/copper assemblies.
  • To explore the influence of different nitrite binding modes to copper on reaction kinetics.
  • To assess the role of the ferrous heme center's reducing ability in nitrite conversion.

Main Methods:

  • Synthesized copper(II)-nitrito complexes with varying ligands and nitrite coordination modes (O,O'-bidentate, O-unidentate).
  • Utilized two tetraarylporphyrinate-iron(II) complexes with electron-donating or electron-withdrawing substituents.
  • Analyzed kinetic behavior and proposed reaction mechanisms for heme/copper heterobinuclear structures.

Main Results:

  • Different modes of nitrite coordination to copper(II) resulted in distinct kinetic behaviors.
  • Ferrous heme consistently served as the reducing agent for nitrite to NO conversion.
  • The reducing strength of the heme center did not significantly impact the overall reaction rate.

Conclusions:

  • The coordination geometry of nitrite to copper influences the kinetics of NO generation.
  • Heme/copper heterobinuclear structures are key to understanding this nitrite reductase activity.
  • Reaction mechanisms involving these complexes provide insights into biological NO synthesis.