Sandbox Reserved 1625: Difference between revisions

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[[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.]]

The overall mechanism of bd oxidases involves an exergonic reduction reaction of molecular oxygen into water (Figure 1). During this reaction, a proton gradient is generated in order to assist in the conservation of energy. Unlike other terminal oxidases, bd oxidases do not use a proton pump. Instead, bd oxidases use a form of vectorial chemistry that releases protons from the quinol oxidation into the positive, periplasmic side of the membrane. Protons that are required for the water formation are then consumed from the negative, cytoplasmic side of the membrane, thus creating the previously mentioned proton gradient.

The overall mechanism of bd oxidases involves an exergonic reduction reaction of molecular oxygen into water (Figure 1). During this reaction, a proton gradient is generated in order to assist in the conservation of energy. <ref name="Belevich">PMID: 17690093</ref> Unlike other terminal oxidases, bd oxidases do not use a proton pump. Instead, bd oxidases use a form of vectorial chemistry that releases protons from the quinol oxidation into the positive, periplasmic side of the membrane. Protons that are required for the water formation are then consumed from the negative, cytoplasmic side of the membrane, thus creating the previously mentioned proton gradient.

This page will be specifically focusing on the structure and overall function of the 6RX4 bd oxidase. 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 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.

Sandbox Reserved 1625: Difference between revisions

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@@ Line 9: / Line 9: @@
 [[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.]]
-The overall mechanism of bd oxidases involves an exergonic reduction reaction of molecular oxygen into water (Figure 1). During this reaction, a proton gradient is generated in order to assist in the conservation of energy. Unlike other terminal oxidases, bd oxidases do not use a proton pump. Instead, bd oxidases use a form of vectorial chemistry that releases protons from the quinol oxidation into the positive, periplasmic side of the membrane. Protons that are required for the water formation are then consumed from the negative, cytoplasmic side of the membrane, thus creating the previously mentioned proton gradient.
+The overall mechanism of bd oxidases involves an exergonic reduction reaction of molecular oxygen into water (Figure 1). During this reaction, a proton gradient is generated in order to assist in the conservation of energy. <ref name="Belevich">PMID: 17690093</ref> Unlike other terminal oxidases, bd oxidases do not use a proton pump. Instead, bd oxidases use a form of vectorial chemistry that releases protons from the quinol oxidation into the positive, periplasmic side of the membrane. Protons that are required for the water formation are then consumed from the negative, cytoplasmic side of the membrane, thus creating the previously mentioned proton gradient.
 This page will be specifically focusing on the structure and overall function of the 6RX4 bd oxidase. 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 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.