Oxyl and hydroxyl radical transfer in mitochondrial amidoxime reducing component-catalyzed nitrite reduction.
J Am Chem Soc
; 137(16): 5276-9, 2015 Apr 29.
Article
in En
| MEDLINE
| ID: mdl-25897643
ABSTRACT
A combination of electron paramagnetic resonance (EPR) spectroscopy and computational approaches has provided insight into the nature of the reaction coordinate for the one-electron reduction of nitrite by the mitochondrial amidoxime reducing component (mARC) enzyme. The results show that a paramagnetic Mo(V) species is generated when reduced enzyme is exposed to nitrite, and an analysis of the resulting EPR hyperfine parameters confirms that mARC is remarkably similar to the low-pH form of sulfite oxidase. Two mechanisms for nitrite reduction have been considered. The first shows a modest reaction barrier of 14 kcal/mol for the formation of ·NO from unprotonated nitrite substrate. In marked contrast, protonation of the substrate oxygen proximal to Mo in the Mo(IV)-O-N-O substrate-bound species results in barrierless conversion to products. A fragment orbital analysis reveals a high degree of Mo-O(H)-N-O covalency that provides a π-orbital pathway for one-electron transfer to the substrate and defines orbital constraints on the Mo-substrate geometry for productive catalysis in mARC and other pyranopterin molybdenum enzymes that catalyze this one-electron transformation.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Oxidoreductases
/
Arabidopsis
/
Hydroxyl Radical
/
Arabidopsis Proteins
/
Mitochondria
/
Nitrites
Language:
En
Journal:
J Am Chem Soc
Year:
2015
Document type:
Article
Affiliation country:
United States