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The protein inhibitor of neuronal nitric oxide synthase (PIN): characterization of its action on pure nitric oxide synthases
Author(s) -
Hemmens Benjamin,
Woschitz Silvia,
Pitters Eva,
Klösch Burkhardt,
Völker Christof,
Schmidt Kurt,
Mayer Bernd
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00704-2
Subject(s) - nitric oxide synthase , neuronal nitric oxide synthase , nitric oxide , enzyme , chemistry , atp synthase , isozyme , biochemistry , reductase , arginine , biophysics , biology , amino acid , organic chemistry
Neuronal NO synthase (nNOS) was discovered recently to interact specifically with the protein PIN (protein inhibitor of nNOS) [Jaffrey, S.R. and Snyder, S.H. (1996) Science 274, 774–777]. We have studied the effects on pure NOS enzymes of the same GST‐tagged PIN used in the original paper. Unexpectedly, all NOS isoenzymes were inhibited. The IC 50 for nNOS was 18±6 μM GST‐PIN with 63 nM nNOS after 30 min at 37°C. Uncoupled NADPH oxidation was inhibited similarly, whereas cytochrome c reductase activity, the K M for l ‐arginine, and dimerization were unaffected. We reconsider the physiological role of PIN in the light of these results.