Sandbox Reserved 1625: Difference between revisions
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[[Image:Transmem1.png|300 px|right|thumb|'''Figure 2''. Cartoon model of cytochrome bd-oxidase in ''E. coli''. Dashed lines represent borders of cytoplasmic and extracellular regions.]] | [[Image:Transmem1.png|300 px|right|thumb|'''Figure 2''. Cartoon model of cytochrome bd-oxidase in ''E. coli''. Dashed lines represent borders of cytoplasmic and extracellular regions.]] | ||
bd Oxidase is a type of quinol-dependent terminal oxidase found exclusively in prokaryotes.<ref name="Safarian">PMID: 27126043</ref> With a very high oxygen affinity, bd oxidases play a vital role in the oxidative phosphorylation pathway in both gram-positive and gram-negative bacteria. bd oxidases responsibility in the oxidative phosphorylation pathway allows the protein to also assist as a key survival factor in the bacterial stress response against antibacterial drugs. <ref name="Safarian, Hahn, Mills">PMID: 31604309</ref> The <scene name='83/832931/Full/4'>cytochrome ''bd'' oxidase</scene> allows bacteria to be resistant to hypoxia, cyanide, nitric oxide, and H<sub>2</sub>O<sub>2</sub><ref name="Harikishore">PMID: 31939065</ref> | bd Oxidase is a type of quinol-dependent terminal oxidase found exclusively in prokaryotes.<ref name="Safarian">PMID: 27126043</ref> With a very high oxygen affinity, bd oxidases play a vital role in the oxidative phosphorylation pathway in both gram-positive and gram-negative bacteria. bd oxidases responsibility in the oxidative phosphorylation pathway allows the protein to also assist as a key survival factor in the bacterial stress response against antibacterial drugs. <ref name="Safarian, Hahn, Mills">PMID: 31604309</ref> The <scene name='83/832931/Full/4'>cytochrome ''bd'' oxidase</scene> allows bacteria to be resistant to hypoxia, cyanide, nitric oxide, and H<sub>2</sub>O<sub>2</sub><ref name="Harikishore">PMID: 31939065</ref> Given this knowledge, bd oxidases have become an area of scientific research worth pursuing as they could serve as an ideal target for antimicrobial drug development. <ref name="Boot">PMID: 28878275</ref> | ||
Given this knowledge, bd oxidases have become an area of scientific research worth pursuing as they could serve as an ideal target for antimicrobial drug development. | |||
[[Image:proton graadient.jpg|300 px|left|thumb|Figure 1: Overall schematic representation of cytochrome bd. <ref name= "Giuffre">PMID: 24486503</ref>; General display of the reduction of molecular oxygen into water using the quinol as a reducing substrate. The three hemes are located near the periplasmic space, meaning that the membrane potential is generated mainly from proton transfer from the cytoplasm towards the active site on the opposite site of the membrane. Heme''b558'' is involved in quinol oxidation and Heme''d'' serves as the site where O2 binds and becomes reduced to H2O.]] | [[Image:proton graadient.jpg|300 px|left|thumb|Figure 1: Overall schematic representation of cytochrome bd. <ref name= "Giuffre">PMID: 24486503</ref>; General display of the reduction of molecular oxygen into water using the quinol as a reducing substrate. The three hemes are located near the periplasmic space, meaning that the membrane potential is generated mainly from proton transfer from the cytoplasm towards the active site on the opposite site of the membrane. Heme''b558'' is involved in quinol oxidation and Heme''d'' serves as the site where O2 binds and becomes reduced to H2O.]] | ||
