Sandbox Reserved 1716: Difference between revisions

<scene name='90/904321/Iii/1'>Step III</scene> is within this partially oxidized state and free Cys43 forms a bond with Cys 51. Cys51 kicks its electrons to Cys132, and Cys 132 forms a disulfide bond with Cys135. Cys135 then reduces the epoxide ring on Vitamin K Epoxide after donating its electrons. The epoxide ring opens and reforms Vitamin K Quinone (Fig.3).  

<scene name='90/904321/Iv/1'>Step IV</scene> is the last step of this cycle. A bond between Cys43 and Cys51 causes an electron transfer to Cys132. In its reduced form Cys132 will attack Cys135, and the extra electrons are kicked to Vitamin K Epoxide. This opens the epoxide ring on Vitamin K Epoxide so that it may be reformed into Vitamin K Quinone. Vitamin K Quinone is released from Vitamin K Epoxide Reductase. VKOR is in a fully oxidized open conformation. This process is repeated over and over unless interrupted by inhibitors known as Vitamin K Antagonists or VKAs.  Vitamin K Quinone will exit the central binding pocket and the open conformation will form. VKOR is in its fully oxidized state after donating its electrons to Vitamin K Epoxide. This is when the luminal helix will be visible. The cycle then repeats at Step I to keep reducing Vitamin K Epoxide to Vitamin K Quinone. <ref name="Liu"/>