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	<scene name='83/832931/Full/2'>test1</scene>		<scene name='83/832931/Full/2'>test1</scene>
-	<scene name='83/832931/Heme/1'>hemes</scene>	+	<scene name='83/832931/Heme/2'>hemes</scene>
	== Function ==		== Function ==

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Revision as of 01:04, 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.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Bd oxidase in Escherichia coli

spinqualitylabelsall models E. coli bd oxidase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image test</scene’> Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights 4.1 H and O channels 4.2 Hemes 5 Applications Function Disease Relevance Structural highlights H and O channels The hydrogen and oxygen channels are essential for hydrogen and oxygen molecules to reach the active site of bd oxidase. A proton motive force generated by the bd oxidase[1] allows protons from the cytoplasm flow through a water-filled hydrophilic channel entering at D119A and moving past K57A, K109B, D105B, Y379B, and D58B [2] where they can be transferred to the active site. Hemes Applications This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

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. ↑ 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