Sandbox Reserved 1600: Difference between revisions

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The protons that are required in the pathway are not provided by a pump, but rather via intracellular water. The <scene name='83/838655/Bdoxidase_proton_pathways/1'>potential proton pathways</scene> utilize amino acids with charges that help shuttle the protons from the intracellular side of the protein to <scene name='83/838655/Bd_oxidase_heme_b_595/1'>Heme B595</scene>. in the active site. The <scene name='83/838655/Bdoxidase_cyda_pathway_glu108/1'>CydA pathway</scene> passes through the <scene name='83/838655/Bdoxidase_cyda_subunit/2'>CydA subunit</scene>, and is shown in <font color='purple'><b>purple</b></font> in Figure 4. The <scene name='83/838655/Bdoxidase_cydb_pathway/3'>CydB pathway</scene> proceeds through the <scene name='83/838655/Bdoxidase_cydb_subunit/2'>CydB subunit</scene>, and is shown in <font color='green'><b>green</b></font> in Figure 4.
The protons that are required in the pathway are not provided by a pump, but rather via intracellular water. The <scene name='83/838655/Bdoxidase_proton_pathways/1'>potential proton pathways</scene> utilize amino acids with charges that help shuttle the protons from the intracellular side of the protein to <scene name='83/838655/Bd_oxidase_heme_b_595/1'>Heme B595</scene>. in the active site. The <scene name='83/838655/Bdoxidase_cyda_pathway_glu108/1'>CydA pathway</scene> passes through the <scene name='83/838655/Bdoxidase_cyda_subunit/2'>CydA subunit</scene>, and is shown in <font color='purple'><b>purple</b></font> in Figure 4. The <scene name='83/838655/Bdoxidase_cydb_pathway/3'>CydB pathway</scene> proceeds through the <scene name='83/838655/Bdoxidase_cydb_subunit/2'>CydB subunit</scene>, and is shown in <font color='green'><b>green</b></font> in Figure 4.


As shown above, the electrons required for the reduction mechanism come from a ubiquinol molecule (Fig. 2) that simultaneously binds to the <scene name='83/838655/Bdoxidase_q_loop/2'>Q loop</scene> and gets oxidized giving 4e<sup>-</sup> to Heme B558.  Once at Heme B558 the 4e<sup>-</sup> will be shuttled directly to Heme D to be used in the reduction of O₂. The electron pathway is depicted in <font color='blue'><b>blue</b></font> in Figure 4.
As shown above, the electrons required for the reduction mechanism come from a ubiquinol molecule (Fig. 2) that simultaneously binds to the <scene name='83/838655/Bdoxidase_q_loop/2'>Q loop</scene> and gets oxidized giving 4e<sup>-</sup> to Heme B558.  Once at Heme B558 the 4e<sup>-</sup> will be shuttled directly to <scene name='83/838655/Bd_oxidase_heme_d/1'>Heme D</scene> to be used in the reduction of O₂. The electron pathway is depicted in <font color='blue'><b>blue</b></font> in Figure 4.


When all of these elements of the reduction aggregate in the active site, the protons and electrons are shuttled to Heme D, where the actual reduction occurs. The 2H₂O molecules are then expelled, as seen in <font color='red'><b>red</b></font> in Figure 4. The shuttling of these electrons and protons also helps assist with the electric chemical potential in the [https://en.wikipedia.org/wiki/Cell_membrane cellular membrane].
When all of these elements of the reduction aggregate in the active site, the protons and electrons are shuttled to <scene name='83/838655/Bd_oxidase_heme_d/1'>Heme D</scene>, where the actual reduction occurs. The 2H₂O molecules are then expelled, as seen in <font color='red'><b>red</b></font> in Figure 4. The shuttling of these electrons and protons also helps assist with the electric chemical potential in the [https://en.wikipedia.org/wiki/Cell_membrane cellular membrane].


= Structure Similarity to bd oxidase found in ''E. coli'' =
= Structure Similarity to bd oxidase found in ''E. coli'' =