This model was taken from the Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51. This model shows kinetic binding of L-Arginine to neuronal nitric oxide synthase. Model shows the substrate (L-Arginine) binding to nNOS in a two-step reversible fashion. First there is rapid binding equilibrium between Im-nNOS and L-Arginine to form an intermediate that contains bound imidazole and L-Arginine. This is followed by a slower conformational change in the Im-enzyme-substrate complex that is associated with release of bound imidazole and generation of a modified enzyme-substrate complex which is detected due to spectral change. Replicates Figure 4 panel) This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2011 The BioModels.net Team. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not.. To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.
Release of Imidazole from complex of L-Arginine and Imidazole bound rat brain neuronal Nitric Oxide Synthase. Abu-Soud HM et al. Biochemistry. 1999 21;38(38):12446-51.
Binding of L-Arginine to Imidazole bound rat brain neuronal Nitric Oxide Synthase. Kd = 0.5mM = 500uM Abu-Soud HM et al. Biochemistry. 1999 21;38(38):12446-51.