Nitric Oxide Synthase: Difference between revisions

Line 81:

===Zinc===

In order for ~~Nos~~ to be active it has to dimerize and bind H<sub>4</sub>B. The ~~two monomers are held together~~ by a ~~single structural~~ <applet load='2g6h' size='300' frame='true' align='right' caption='Zinc' /><scene name='Nitric_oxide_synthase/Zink/2'>zinc ion</scene>

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/3'>zinc ion</scene>.

which is situated at the interface of the dimer<ref name="penta"/>. 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 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

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>.

ligands (cysteines) form a disulfide bond connecting the two subunits<ref>PMID: 10562539</ref>.

Nitric Oxide Synthase: Difference between revisions

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@@ Line 81: / Line 81: @@
 ===Zinc===
-In order for Nos to be active it has to dimerize and bind H<sub>4</sub>B. The two monomers are held together by a single structural <applet load='2g6h' size='300' frame='true' align='right' caption='Zinc' /><scene name='Nitric_oxide_synthase/Zink/2'>zinc ion</scene>
+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/3'>zinc ion</scene>.
-which is situated at the interface of the dimer<ref name="penta"/>.  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 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
+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>.
-ligands (cysteines) form a disulfide bond connecting the two subunits<ref>PMID: 10562539</ref>.