Sandbox Reserved 1600: Difference between revisions

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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.

Cytochrome bd oxidase plays a key role in protecting [https://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], more specifically [https://en.wikipedia.org/wiki/Heterotroph heterotrophs], from high [https://en.wikipedia.org/wiki/Oxidative_stress oxidative stress] (ie. preventing free radicals in intracellular space in prokaryotes).<ref name=”Jünemann”>PMID:9332500</ref> Other organisms, like humans, have mechanisms that do the same thing but are more intricate due to the organism’s higher levels of complexity.

Cytochrome bd oxidase plays a key role in protecting [https://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], more specifically [https://en.wikipedia.org/wiki/Heterotroph heterotrophs], from high [https://en.wikipedia.org/wiki/Oxidative_stress oxidative stress] (ie. preventing free radicals in intracellular space in [https://en.wikipedia.org/wiki/Prokaryote, prokaryotes]).<ref name=”Jünemann”>PMID:9332500</ref> Other organisms, like humans, have mechanisms that do the same thing but are more intricate due to the organism’s higher levels of complexity.

The ''Geobacillus thermodenitrificans'' is a facultative aerobic thermophilic bacterium that utilizes the bd oxidase mechanism. The oxygen enters the enzyme through the selective <scene name='83/832926/Potential_oxygen_entry_site/1'>oxygen entry site</scene> that funnels the extracellular oxygen to <scene name='83/838655/Bd_oxidase_heme_d/2'>Heme D</scene> in the active site. The electrons for the reaction are provided by ubiquinone molecule bound to the <scene name='83/838655/Bdoxidase_q_loop/2'>Q loop</scene>. The protons for the reaction are provided by one of two <scene name='83/838655/Bdoxidase_proton_pathways/1'>potential proton pathways</scene>, either the <scene name='83/838655/Bdoxidase_cyda_pathway/6'>CydA pathway</scene>or <scene name='83/838655/Bdoxidase_cydb_pathway/3'>CydB pathway</scene>. Both of the proton pathways utilize the intracellular water molecules for the proton source, and shuttle them to <scene name='83/838655/Bd_oxidase_heme_b_595/2'>Heme B595</scene>.

Sandbox Reserved 1600: Difference between revisions

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 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.
-Cytochrome bd oxidase plays a key role in protecting [https://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], more specifically [https://en.wikipedia.org/wiki/Heterotroph heterotrophs], from high [https://en.wikipedia.org/wiki/Oxidative_stress oxidative stress] (ie. preventing free radicals in intracellular space in prokaryotes).<ref name=”Jünemann”>PMID:9332500</ref> Other organisms, like humans, have mechanisms that do the same thing but are more intricate due to the organism’s higher levels of complexity.
+Cytochrome bd oxidase plays a key role in protecting [https://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], more specifically [https://en.wikipedia.org/wiki/Heterotroph heterotrophs], from high [https://en.wikipedia.org/wiki/Oxidative_stress oxidative stress] (ie. preventing free radicals in intracellular space in [https://en.wikipedia.org/wiki/Prokaryote, prokaryotes]).<ref name=”Jünemann”>PMID:9332500</ref> Other organisms, like humans, have mechanisms that do the same thing but are more intricate due to the organism’s higher levels of complexity.
 The ''Geobacillus thermodenitrificans'' is a facultative aerobic thermophilic bacterium that utilizes the bd oxidase mechanism. The oxygen enters the enzyme through the selective <scene name='83/832926/Potential_oxygen_entry_site/1'>oxygen entry site</scene> that funnels the extracellular oxygen to <scene name='83/838655/Bd_oxidase_heme_d/2'>Heme D</scene> in the active site. The electrons for the reaction are provided by ubiquinone molecule bound to the <scene name='83/838655/Bdoxidase_q_loop/2'>Q loop</scene>. The protons for the reaction are provided by one of two <scene name='83/838655/Bdoxidase_proton_pathways/1'>potential proton pathways</scene>, either the <scene name='83/838655/Bdoxidase_cyda_pathway/6'>CydA pathway</scene>or <scene name='83/838655/Bdoxidase_cydb_pathway/3'>CydB pathway</scene>. Both of the proton pathways utilize the intracellular water molecules for the proton source, and shuttle them to <scene name='83/838655/Bd_oxidase_heme_b_595/2'>Heme B595</scene>.