Sandbox Reserved 1600: Difference between revisions

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=Introduction=

<scene name='83/838655/Bdoxidase_structure_full/4'>Cytochrome bd oxidase</scene> is an integral membrane protein that catalyzes the reduction of oxygen to water using quinol as the reducing substrate.<ref name=”Giuffrè”>PMID:24486503</ref>. The full reaction is O₂ + 4H+ + 4e- → 2H₂O. The reaction is electrogenic but it is not coupled to a proton pump. Instead, bd oxidase utilizes internal water molecules to provide the four protons needed and an external ubiquinol molecule for the four electrons needed <ref name = ”Safarian”>PMID:31604309</ref>.

<scene name='83/838655/Bdoxidase_structure_full/4'>Cytochrome bd oxidase</scene> is an integral membrane protein that catalyzes the reduction of oxygen to water using quinol as the reducing substrate <ref name=”Giuffrè”>PMID:24486503</ref>. The full reaction is O₂ + 4H+ + 4e- → 2H₂O. The reaction is electrogenic but it is not coupled to a proton pump. Instead, bd oxidase utilizes internal water molecules to provide the four protons needed and an external ubiquinol molecule for the four electrons needed <ref name = ”Safarian”>PMID:31604309</ref>.

There are two main types of respiratory cytochrome oxidases: the heme/copper oxidases, and the heme-only cytochrome bd quinol oxidase, which is what bd oxidase falls under. <ref name=”Das”>PMID:15743950</ref> Heme-only cytochrome bd quinol oxidases are associated with microaerobic dioxygen respiration, and they have a high affinity for oxygen.

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==Potential Oxygen Entry Site==

<scene name='83/838655/Bd_oxidase_heme_d/1'>Heme D</scene> is the hypothesized spot for the <scene name='83/832926/Potential_oxygen_entry_site/1'>oxygen</scene> to enter the protein. Heme D (~~seen~~ in green) is directly connected to the protein surface on CydA and contains a solvent accessible substrate channel. This channel and accessibility allow for oxygen to easily bind to Heme D and eventually be reduced to two ~~water~~ molecules. This process requires a proton and electron source, both described in the later sections.

<scene name='83/838655/Bd_oxidase_heme_d/1'>Heme D</scene> is the hypothesized spot for the <scene name='83/832926/Potential_oxygen_entry_site/1'>oxygen</scene> to enter the protein. Heme D (shown in green) is directly connected to the protein surface on CydA and contains a solvent accessible substrate channel. This channel and accessibility allow for oxygen to easily bind to Heme D and eventually be reduced to two H₂O molecules. This process requires a proton and electron source, both described in the later sections.

==Electron Source==

Sandbox Reserved 1600: Difference between revisions

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@@ Line 4: / Line 4: @@
 <StructureSection  load='5DOQ'  size='350'  frame='true' side='right' caption='bd oxidase 5DOQ' scene='83/838655/Bdoxidase_structure_full/3'>
 =Introduction=
-<scene name='83/838655/Bdoxidase_structure_full/4'>Cytochrome bd oxidase</scene> is an integral membrane protein that catalyzes the reduction of oxygen to water using quinol as the reducing substrate.<ref name=”Giuffrè”>PMID:24486503</ref>. The full reaction is O₂ + 4H<sup>+</sup> + 4e<sup>-</sup> → 2H₂O. The reaction is electrogenic but it is not coupled to a proton pump. Instead, bd oxidase utilizes internal water molecules to provide the four protons needed and an external ubiquinol molecule for the four electrons needed <ref name = ”Safarian”>PMID:31604309</ref>.
+<scene name='83/838655/Bdoxidase_structure_full/4'>Cytochrome bd oxidase</scene> is an integral membrane protein that catalyzes the reduction of oxygen to water using quinol as the reducing substrate <ref name=”Giuffrè”>PMID:24486503</ref>. The full reaction is O₂ + 4H<sup>+</sup> + 4e<sup>-</sup> → 2H₂O. The reaction is electrogenic but it is not coupled to a proton pump. Instead, bd oxidase utilizes internal water molecules to provide the four protons needed and an external ubiquinol molecule for the four electrons needed <ref name = ”Safarian”>PMID:31604309</ref>.
 There are two main types of respiratory cytochrome oxidases: the heme/copper oxidases, and the heme-only cytochrome bd quinol oxidase, which is what bd oxidase falls under. <ref name=”Das”>PMID:15743950</ref> Heme-only cytochrome bd quinol oxidases are associated with microaerobic dioxygen respiration, and they have a high affinity for oxygen.
@@ Line 30: / Line 31: @@
 ==Potential Oxygen Entry Site==
-<scene name='83/838655/Bd_oxidase_heme_d/1'>Heme D</scene> is the hypothesized spot for the <scene name='83/832926/Potential_oxygen_entry_site/1'>oxygen</scene> to enter the protein. Heme D (seen in green) is directly connected to the protein surface on CydA and contains a solvent accessible substrate channel. This channel and accessibility allow for oxygen to easily bind to Heme D and eventually be reduced to two water molecules. This process requires a proton and electron source, both described in the later sections.
+<scene name='83/838655/Bd_oxidase_heme_d/1'>Heme D</scene> is the hypothesized spot for the <scene name='83/832926/Potential_oxygen_entry_site/1'>oxygen</scene> to enter the protein. Heme D (shown in <font color='green'><b>green</b></font>) is directly connected to the protein surface on CydA and contains a solvent accessible substrate channel. This channel and accessibility allow for oxygen to easily bind to Heme D and eventually be reduced to two H₂O molecules. This process requires a proton and electron source, both described in the later sections.
 ==Electron Source==