Nitric Oxide Synthase: Difference between revisions

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===Zinc===
===Zinc===
In order for Nos to be active it has to dimerize. The two monomers are held together by a single structural zinc ion which is situated at the interface. It is coordinated to the S atom of two cysteins in each monomer (cys110 and cys115. Hydrogenbonding further supports the binding of two monomers.<ref>PMID: 10074942</ref>
In order for Nos to be active it has to dimerize and bind H4B. The two monomers are held together by a single structural zinc ion which is situated at the interface of the dimer.<ref>PMID: 10074942</ref>  The zinc ion is tetrahedrally coordinated and has four cysteins bound as ligands (two from each monomer - Cys109 and Cys104). Further, it is found that zinc binds together the oxygenase domains of the monomers. The zinc ion is found at region which connects the N-terminal hook and the subunit core. The coordination of zinc arranges the N-terminal hooks so that they interact with their own subunit. However, when there is no zinc ion present, two of the thiolate ligands form a disulfide bond connecting the two subunits<ref>PMID: 10562539</ref>.


== The Reductase Domain of NOS ==
== The Reductase Domain of NOS ==