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Title:

Thermodynamic analysis of L-arginine and N omega-hydroxy-L-arginine binding to nitric oxide synthase.

Document type:
Journal Article; Research Support, Non-U.S. Gov't
Author(s):
Zakariassen, H; Cederkvist, FH; Harbitz, E; Shimizu, T; Lange, R; Mayer, B; Gorren, AC; Andersson, KK; Sørlie, M
Abstract:
Isothermal titration calorimetry has been used to determine thermodynamic parameters of substrate binding to the oxygenase domain of neuronal nitric oxide synthase (nNOS(oxy)) in the presence of the cofactor tetrahydrobiopterin. The intermediate N(omega)-hydroxy-L-arginine (NHA) has a larger affinity than L-Arginine (L-Arg) for nNOS(oxy), with K(d)=0.4+/-0.1 microM and 1.7+/-0.3 microM at 25 degrees C, respectively. nNOS(oxy) binds NHA and L-Arg with DeltaH -4.1+/-0.2 and -1.0+/-0.1 kcal/mol and...     »
Journal title abbreviation:
Biochim Biophys Acta
Year:
2008
Journal volume:
1784
Journal issue:
5
Pages contribution:
806-10
Language:
eng
Fulltext / DOI:
doi:10.1016/j.bbapap.2008.02.016
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/18371313
Print-ISSN:
0006-3002
TUM Institution:
Klinik für Herz- und Gefäßchirurgie (Prof. Lange)
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