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Cu2+ and zn2+ inhibit nitric-oxide synthase through an interaction with the reductase domain

Academic Article
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Overview

authors

  • Perry, J. M.
  • Zhao, Y. D.
  • Marletta, Michael

publication date

  • May 2000

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Cu(2+) and Zn(2+) inhibit all of the NADPH-dependent reactions catalyzed by neuronal nitric-oxide synthase (nNOS) including ferricytochrome c reduction, NADPH oxidation, and citrulline formation. Cu(2+) and Zn(2+) also inhibit ferricytochrome c reduction by the independent reductase domain. Zn(2+) affects all activities of the full-length nNOS and the reductase domain to the same extent (estimated IC(50) values from 9 to 31 microm), suggesting Zn(2+) occupation of a single site in the reductase domain. Citrulline formation and NADPH oxidation by the full-length nNOS and ferricytochrome c reduction by the reductase domain are affected similarly by Cu(2+), with estimated IC(50) values ranging from 6 to 33 microm. However, Cu(2+) inhibits ferricytochrome c reduction by the full-length nNOS 2 orders of magnitude more potently, with an estimated IC(50) value of 0.12 microm. These data suggest the possibility that Cu(2+) may interact with nNOS at two sites, one composed exclusively of the reductase domain (which is perhaps also involved in Zn(2+)-mediated inhibition), and another that includes components of both domains. Occupation of the second (higher affinity) site could then promote the selective inhibition of ferricytochrome c reduction in full-length nNOS. Neither the inhibition by Cu(2+) nor that by Zn(2+) is dependent on calmodulin.

subject areas

  • Calmodulin
  • Copper
  • Cytochrome c Group
  • Enzyme Inhibitors
  • NADP
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type I
  • Oxidation-Reduction
  • Oxidoreductases
  • Superoxide Dismutase
  • Zinc
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.275.19.14070

PubMed ID

  • 10799481
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Additional Document Info

start page

  • 14070

end page

  • 14076

volume

  • 275

issue

  • 19

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