Nitric Oxide Synthase: Difference between revisions

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===Zinc===
===Zinc===


In order for NOS to be active it has to dimerize and bind H<sub>4</sub>B. The dimer is structurally sabilized by a <applet load='2g6h' size='300' frame='true' align='right' caption=Zinc' /><scene name='Nitric_oxide_synthase/Zink/4'>zinc ion</scene>.
<applet load='2g6h' size='300' frame='true' align='right' caption=Zinc' />
In order for NOS to be active it has to dimerize and bind H<sub>4</sub>B. The dimer is structurally sabilized by a <scene name='Nitric_oxide_synthase/Zink/4'>zinc ion</scene>.
which is situated at the oxygenase domain interface of the dimer<ref name="penta"/>.  The zinc ion is tetrahedrally coordinated by four cysteins (two from each monomer - Cys109 and Cys104). The zinc ion is found at a 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 (cysteines) form a disulfide bond connecting the two subunits<ref>PMID: 10562539</ref>.
which is situated at the oxygenase domain interface of the dimer<ref name="penta"/>.  The zinc ion is tetrahedrally coordinated by four cysteins (two from each monomer - Cys109 and Cys104). The zinc ion is found at a 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 (cysteines) form a disulfide bond connecting the two subunits<ref>PMID: 10562539</ref>.