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 properties that help shuttle the protons from the intracellular side of the protein to <scene name='83/838655/Bd_oxidase_heme_b_595/2'>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>, shown in purple 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>, shown in green in Figure 4.

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/2'>Heme D</scene>, where the actual reduction occurs. The 2H₂O molecules are then expelled, ~~as seen~~ in red 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 at their respective hemes, the protons and electrons are shuttled to <scene name='83/838655/Bd_oxidase_heme_d/2'>Heme D</scene>, where the actual reduction occurs. The 2H₂O molecules are then expelled from <scene name='83/838655/Bd_oxidase_heme_d/2'>Heme D</scene>, shown in red 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'' =

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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 properties that help shuttle the protons from the intracellular side of the protein to <scene name='83/838655/Bd_oxidase_heme_b_595/2'>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>, 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>, shown in <font color='green'><b>green</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 <scene name='83/838655/Bd_oxidase_heme_d/2'>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].
+When all of these elements of the reduction aggregate in the active site at their respective hemes, the protons and electrons are shuttled to <scene name='83/838655/Bd_oxidase_heme_d/2'>Heme D</scene>, where the actual reduction occurs. The 2H₂O molecules are then expelled from <scene name='83/838655/Bd_oxidase_heme_d/2'>Heme D</scene>, shown 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'' =

Sandbox Reserved 1600: Difference between revisions

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