Introduction
bd Oxidase is a type of quinol-dependent terminal oxidase found exclusively in prokaryotes. 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. 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.
![Figure 1: Overall schematic representation of cytochrome bd [1]; 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. Hemeb558 is involved in quinol oxidation and Hemed serves as the site where O2 binds and becomes reduced to H2O.](/wiki/images/thumb/e/e6/Proton_graadient.jpg/300px-Proton_graadient.jpg)
Figure 1: Overall schematic representation of cytochrome bd
[1]; 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.
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 groups, its periplasmically exposed , and will be of primary focus when identifying the relationship between structure and function.
Function
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Disease
Relevance
Structural highlights
![Figure 1: Overall schematic representation of cytochrome bd [1]; 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. Hemeb558 is involved in quinol oxidation and Hemed serves as the site where O2 binds and becomes reduced to H2O.](/wiki/index.php/Image:Proton_graadient.jpg)
