Sandbox Reserved 1605
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
=== H and O channels === | === H and O channels === | ||
| - | The hydrogen and oxygen channels are essential for | + | The hydrogen and oxygen channels are essential for H<sup>+</sup> and O<sub>2</sub> molecules to reach the active site of bd oxidase. A proton motive force generated by the oxidase<ref name= "Safarian">PMID:27126043</ref> allows protons from the cytoplasm flow through a water-filled hydrophilic channel entering at D119<sup>A</sup> and moving past K57<sup>A</sup>, K109<sup>B</sup>, D105<sup>B</sup>, Y379<sup>B</sup>, and D58<sup>B</sup> <ref name="Theßeling">PMID:31723136</ref> where they can be transferred to the active site. |
=== Hemes === | === Hemes === | ||
== Applications == | == Applications == | ||
Revision as of 02:23, 24 March 2020
| This Sandbox is Reserved from Jan 13 through September 1, 2020 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1598 through Sandbox Reserved 1627. |
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Bd oxidase in Escherichia coli
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References
- ↑ 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
- ↑ Thesseling A, Rasmussen T, Burschel S, Wohlwend D, Kagi J, Muller R, Bottcher B, Friedrich T. Homologous bd oxidases share the same architecture but differ in mechanism. Nat Commun. 2019 Nov 13;10(1):5138. doi: 10.1038/s41467-019-13122-4. PMID:31723136 doi:http://dx.doi.org/10.1038/s41467-019-13122-4
Student Contributors
- Grace Bassler
- Emily Neal
- Marisa Villarreal
