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J. Biol. Chem., Vol. 275, Issue 48, 37524-37532, December 1, 2000
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From the We now show that NO serves as a substrate
for multiple members of the mammalian peroxidase superfamily under
physiological conditions. Myeloperoxidase (MPO), eosinophil peroxidase,
and lactoperoxidase all catalytically consumed NO in the presence of
the co-substrate hydrogen peroxide
(H2O2). Near identical rates of NO
consumption by the peroxidases were observed in the presence versus absence of plasma levels of Cl
Nitric Oxide Is a Physiological Substrate for Mammalian
Peroxidases*
§ and¶
**
Department of Cell Biology and
¶ Department of Cardiology, Cleveland Clinic Foundation,
Cleveland, Ohio 44195 and the Chemistry Department, Cleveland
State University, Cleveland, Ohio 44115
.
Although rates of NO consumption in buffer were accelerated in the
presence of a superoxide-generating system, subsequent addition of
catalytic levels of a model peroxidase, MPO, to NO-containing solutions
resulted in the rapid acceleration of NO consumption. The interaction
between NO and compounds I and II of MPO were further investigated
during steady-state catalysis by stopped-flow kinetics. NO dramatically
influenced the build-up, duration, and decay of steady-state levels of
compound II, the rate-limiting intermediate in the classic peroxidase
cycle, in both the presence and absence of Cl.
Collectively, these results suggest that peroxidases may function as a
catalytic sink for NO at sites of inflammation, influencing its
bioavailability. They also support the potential existence of a complex
and interdependent relationship between NO levels and the modulation of
steady-state catalysis by peroxidases in vivo.
*
This work was supported in part by the American Heart
Association and by National Institutes of Health Grants HL62526 and HL61878.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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M. J. Coffey, R. Natarajan, P. H. Chumley, B. Coles, P.-R. Thimmalapura, M. Nowell, H. Kuhn, M. J. Lewis, B. A. Freeman, and V. B. O'Donnell Catalytic consumption of nitric oxide by 12/15- lipoxygenase: Inhibition of monocyte soluble guanylate cyclase activation PNAS, July 3, 2001; 98(14): 8006 - 8011. [Abstract] [Full Text] [PDF]
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