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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.
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.
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[[Image:proton graadient.jpg|300 px|left|thumb|Figure 1: Overall schematic representation of cytochrome bd; General display of the reduction of molecular oxygen into water [https://reader.elsevier.com/reader/sd/pii/S0005272814000267?token=7EBD28607F562A4542A155260BB6B714F7098C72BBD88FB97B262942997FD11F8F90D09B5CE4E119693D5B5EDB06C1DB.]]]
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[[Image:proton graadient.jpg|300 px|left|thumb|Figure 1: Overall schematic representation of cytochrome bd; General display of the reduction of molecular oxygen into water [https://doi.org/10.1016/j.bbabio.2014.01.016.]]]
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Revision as of 03:09, 24 March 2020

bd Oxidase, 5DOQ

Marisa Villarreal/Sandbox 1.

bd Oxidase, 5DOQ

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References

[2]. [1].

  1. 1.0 1.1 Safarian S, Rajendran C, Muller H, Preu J, Langer JD, Ovchinnikov S, Hirose T, Kusumoto T, Sakamoto J, Michel H. Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases. Science. 2016 Apr 29;352(6285):583-6. doi: 10.1126/science.aaf2477. PMID:27126043 doi:http://dx.doi.org/10.1126/science.aaf2477
  2. 2.0 2.1 Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677

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Marisa Villarreal

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