Sandbox 5: Difference between revisions
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<table style="background-color:yellow"><tr><td>'''This sandbox will be used for a student project at University of Copenhagen from April until the 1st of July 2009. Please don't edit the page until then.'''</td></tr></table> | <table style="background-color:yellow"><tr><td>'''This sandbox will be used for a student project at University of Copenhagen from April until the 1st of July 2009. Please don't edit the page until then.'''</td></tr></table> | ||
== An Overview == | |||
An overview of the NOS homodimer is given below. All cofactors are included and the electron transfer pathway which takes place in NOS is indicated. | |||
[[Image:Example.jpg]] | |||
The NOS homodimer is composed of two types of domains: a oxygenase domain and a reductase domain. Each subunit is held together by a Zinc ion, which is bound by the amino acid Cystein present in the oxygenase. Binding of the domains is caused by CaM. The reductase domain supplies electrons for the NOS reaction which takes place in the oxygenase domain. The reductase domain contains two redox-active prothetic groups, FAD and FMN. NADPH binds to the domain and passes on an electron to FAD which passes the electron on to FMN. FMN is a Flavin mononucleotide. FMN passes the electron on to the Heme in the oxygenase domain on the opposite subunit. The oxygenase domain contains BH4 (5,6,7,8-tetrahydrobiopterin)and the already mentioned Heme ion (Fe(III)). These two are also redox active groups.BH4 is required by NOS in order to produce NO and not H2O2. Besides Heme and BH4, the oxygenase domain binds the substrate L-arginine which takes part in the NO synthase reaction (see below). | |||