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5 results for “Proton conductivity”
An unusual amino acid substitution within hummingbird cytochrome c oxidase alters a key proton-conducting channel
<p>Hummingbirds in flight exhibit the highest metabolic rate of all vertebrates. The bioenergetic requirements associated with sustained hovering flight raise the possibility of unique amino acid substitutions that would enhance aerobic metabolism. Here, we have identified a non-conservative substitution within the mitochondria-encoded cytochrome <i>c</i> oxidase subunit I (COI) that is fixed within hummingbirds, yet exceedingly rare among other vertebrates. This unusual change is also rare among metazoans, but can be identified in several clades with diverse life histories. We performed atomistic molecular dynamics simulations using bovine and hummingbird COI models, thereby bypassing experimental limitations imposed by the inability to modify mtDNA in a site-specific manner. Intriguingly, our findings suggest that COI amino acid position 153 (bovine numbering system) provides control over the hydration and activity of a key proton channel in COX. We discuss potential phenotypic outcomes linked to this intriguing alteration encoded by the hummingbird mitochondrial genome.</p>
An unusual amino acid substitution within hummingbird cytochrome c oxidase alters a key proton-conducting channel
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Dissected Antiporter Modules Establish Minimal Proton-Conduction Elements in the Respiratory Complex I
<ul> <li>Snapshots from MD simulations (see SI table 4 for reference)</li> </ul>
Electrophysiological recordings and a liposome-based assay showing the absence of chloride and proton conduction in TTYH proteins
<p>The Tweety homologues (TTYHs) are members of a conserved family of eukaryotic membrane proteins that are abundant in the brain. The three human paralogs were assigned to function as anion channels that are either activated by Ca<sup>2+</sup> or cell swelling. To uncover their unknown architecture and its relationship to function, we have determined the structures of human TTYH1–3 by cryo-electron microscopy. All structures display equivalent features of a dimeric membrane protein that contains five transmembrane segments and an extended extracellular domain. As none of the proteins shows features reminiscent of an anion channel, we revisited functional experiments and did not find any indication of ion conduction. Instead, we find density in an extended hydrophobic pocket contained in the extracellular domain that emerges from the lipid bilayer, which suggests a role of TTYH proteins in the interaction with lipid-like compounds residing in the membrane.</p>
Electrophysiological recordings and a liposome-based assay showing the absence of chloride and proton conduction in TTYH proteins
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