Sandbox Reserved 1625: Difference between revisions

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[[Image:proton graadient.jpg|300 px|left|thumb|Figure 2: Overall schematic representation of the reductive cycle of cytochrome bd oxidase. <ref name= "Giuffre">PMID: 24486503</ref>; In this cycle, molecular oxygen is reduced into water using the quinol as a reducing substrate. The three hemes essential to the electron transfer are located near the periplasmic space. Heme b558 is involved in quinol oxidation and heme d serves as the site where O2 binds and becomes reduced to H2O.]]

This page will ~~be specifically focusing~~ on the structure and overall function of the ~~6RX4~~ ''bd'' oxidase in [https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli'']. ~~6RX4~~ is a part of the long(L) quinol-binding domain subfamily ~~that~~ terminal oxidases ~~are classified into~~. The L-subfamily of ''bd'' oxidases are responsible for the survival of acute infectious diseases such as ''E. coli'' and [http://www.example.com ~~salmonella~~]. The 6RX4's three <scene name='83/832931/Heme/4'>heme</scene> groups, its periplasmically exposed <scene name='83/832924/Q_loop/3'>Q-loop</scene>, and <scene name='83/832942/Four_subunits_labelled_6rx4/2'>four protein subunits</scene> will be of primary focus when ~~identifying~~ the ~~relationship between~~ structure ~~and function~~.

This page will focus on the structure and overall function of the ''bd'' oxidase in [https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli'']. This ''bd'' oxidase is part of the long(L) quinol-binding domain subfamily of terminal oxidases. The L-subfamily of ''bd'' oxidases are responsible for the survival of acute infectious diseases such as ''E. coli'' and [http://www.example.com ''Salmonella'']. The 6RX4's three <scene name='83/832931/Heme/4'>heme</scene> groups, its periplasmically exposed <scene name='83/832924/Q_loop/3'>Q-loop</scene>, and <scene name='83/832942/Four_subunits_labelled_6rx4/2'>four protein subunits</scene> will be the primary focus when explaining how the structure of ''bd'' oxidase allows it to catalyze the reduction of molecular oxygen into water.

==Structure==

=== Subunits ===

Sandbox Reserved 1625: Difference between revisions

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@@ Line 8: / Line 8: @@
 [[Image:proton graadient.jpg|300 px|left|thumb|Figure 2: Overall schematic representation of the reductive cycle of cytochrome bd oxidase. <ref name= "Giuffre">PMID: 24486503</ref>; In this cycle, molecular oxygen is reduced  into water using the quinol as a reducing substrate. The three hemes essential to the electron transfer are located near the periplasmic space. Heme b<sub>558</sub> is involved in quinol oxidation and heme d serves as the site where O<sub>2</sub> binds and becomes reduced to H<sub>2</sub>O.]]
-This page will be specifically focusing on the structure and overall function of the 6RX4 ''bd'' oxidase in [https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli'']. 6RX4 is a part of the long(L) quinol-binding domain subfamily that terminal oxidases are classified into. The L-subfamily of ''bd'' oxidases are responsible for the survival of acute infectious diseases such as ''E. coli'' and [http://www.example.com salmonella]. The 6RX4's three <scene name='83/832931/Heme/4'>heme</scene> groups, its periplasmically exposed <scene name='83/832924/Q_loop/3'>Q-loop</scene>, and <scene name='83/832942/Four_subunits_labelled_6rx4/2'>four protein subunits</scene> will be of primary focus when identifying the relationship between structure and function.
+This page will focus on the structure and overall function of the ''bd'' oxidase in [https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli'']. This ''bd'' oxidase is part of the long(L) quinol-binding domain subfamily of terminal oxidases. The L-subfamily of ''bd'' oxidases are responsible for the survival of acute infectious diseases such as ''E. coli'' and [http://www.example.com ''Salmonella'']. The 6RX4's three <scene name='83/832931/Heme/4'>heme</scene> groups, its periplasmically exposed <scene name='83/832924/Q_loop/3'>Q-loop</scene>, and <scene name='83/832942/Four_subunits_labelled_6rx4/2'>four protein subunits</scene> will be the primary focus when explaining how the structure of ''bd'' oxidase allows it to catalyze the reduction of molecular oxygen into water.
 ==Structure==
 === Subunits ===