onr:"swepub:oai:DiVA.org:su-144709"
Sökning: onr:"swepub:oai:DiVA.org:su-144709" > Single Proteoliposo...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03727naa a2200505 4500 | |
| 001 | oai:DiVA.org:su-144709 | |
| 003 | SwePub | |
| 008 | 170720s2017 | |||||||||||000 ||eng| | |
| 009 | oai:research.chalmers.se:49489755-c27f-4b65-8b85-e3b45401276b | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1447092 URI |
| 024 | 7 | a https://doi.org/10.1002/ijch.2016001382 DOI |
| 024 | 7 | a https://research.chalmers.se/publication/2498552 URI |
| 040 | a (SwePub)sud (SwePub)cth | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Berg, Johanu Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University4 aut0 (Swepub:su)joberg |
| 245 | 1 0 | a Single Proteoliposomes with E.coli Quinol Oxidase :b Proton Pumping without Transmembrane Leaks |
| 264 | c 2017-02-10 | |
| 264 | 1 | b Wiley,c 2017 |
| 338 | a print2 rdacarrier | |
| 520 | a Respiratory oxidases are transmembrane enzymes that catalyze the reduction of dioxygen to water in the final step of aerobic respiration. This process is linked to proton pumping across the membrane. Here, we developed a method to study the catalytic turnover of the quinol oxidase, cytochromebo(3) from E.coli at single-molecule level. Liposomes with reconstituted cytochromebo(3) were loaded with a pH-sensitive dye and changes in the dye fluorescence, associated with proton transfer and pumping, were monitored as a function of time. The single-molecule approach allowed us to determine the orientation of cytochromebo(3) in the membrane; in approximate to 70% of the protein-containing liposomes protons were released to the outside. Upon addition of substrate we observed the buildup of a pH (in the presence of the K+ ionophore valinomycin), which was stable over at least approximate to 800s. No rapid changes in pH (proton leaks) were observed during steady state proton pumping, which indicates that the free energy stored in the electrochemical gradient in E.coli is not dissipated or regulated through stochastic transmembrane proton leaks, as suggested from an earlier study (Li etal. J. Am. Chem. Soc. (2015) 137, 16055-16063). | |
| 650 | 7 | a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng |
| 650 | 7 | a NATURVETENSKAPx Fysikx Annan fysik0 (SwePub)103992 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Physical Sciencesx Other Physics Topics0 (SwePub)103992 hsv//eng |
| 650 | 7 | a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng |
| 653 | a proton translocation | |
| 653 | a single molecule | |
| 653 | a proton pump | |
| 653 | a electron transfer | |
| 653 | a membrane protein | |
| 653 | a Biochemistry | |
| 653 | a biokemi | |
| 700 | 1 | a Block, Stephan,d 1978u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)blocks |
| 700 | 1 | a Höök, Fredrik,d 1966u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)fredrikh |
| 700 | 1 | a Brzezinski, Peteru Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University4 aut0 (Swepub:su)brzez |
| 710 | 2 | a Stockholms universitetb Institutionen för biokemi och biofysik4 org |
| 773 | 0 | t Israel Journal of Chemistryd : Wileyg 57:5, s. 437-445q 57:5<437-445x 0021-2148 |
| 856 | 4 | u http://dx.doi.org/10.1002/ijch.201600138y FULLTEXT |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-144709 |
| 856 | 4 8 | u https://doi.org/10.1002/ijch.201600138 |
| 856 | 4 8 | u https://research.chalmers.se/publication/249855 |
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