WFRF:(Rasmusson I)
Sökning: WFRF:(Rasmusson I) > Oxidation and reduc...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03748naa a2200397 4500 | |
| 001 | oai:lup.lub.lu.se:d9bed102-dd08-43ac-93cf-5e1b9493084e | |
| 003 | SwePub | |
| 008 | 160401s2004 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://lup.lub.lu.se/record/2770912 URI |
| 024 | 7 | a https://doi.org/10.1042/BJ200319692 DOI |
| 040 | a (SwePub)lu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Johansson, Fredrik Iu Lund University,Lunds universitet,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science4 aut0 (Swepub:lu)cob-fdj |
| 245 | 1 0 | a Oxidation and reduction of pyridine nucleotides in alamethicin-permeabilized plant mitochondria |
| 264 | 1 | c 2004 |
| 520 | a The inner mitochondrial membrane is selectively permeable, which limits the transport of solutes and metabolites across the membrane. This constitutes a problem when intramitochondrial enzymes are studied. The channel-forming antibiotic AlaM (alamethicin) was used as a potentially less invasive method to permearbilize mitochondria and study the highly branched electron-transport chain in potato tuber (Solanum tuberosum) and pea leaf (Pisum sativum) mitochondria. We show that AlaM permeabilized the inner membrane of plant mitochondria to NAD(P)H, allowing the quantification of internal NAD(P)H dehydrogenarses as well as matrix enzymes in situ. AlaM was found to inhibit the electron-tran sport chain at the external Ca2+-dependent rotenone-insensitive NADH dehydrogenase and around complexes III and IV. Nevertheless, under optimal conditions, especially complex I-mediated NADH oxidation in AlaM-treated mitochondria was much higher than what has been previously measured by other techniques. Our results also show a difference in substrate specificities for complex I in mitochondria as compared with inside-out submitochondrial particles. AlaM facilitated the passage of cofactors to and from the mitochondrial matrix and allowed the determination of NAD(+) requirements of malate oxidation in situ. In summary, we conclude that AlaM provides the best method for quantifying NADH dehydrogenase activities and that AlaM will prove to be an important method to study enzymes under conditions that resemble their native environment not only in plant mitochondria but also in other membrane-enclosed compartments, such as intact cells, chloroplasts and peroxisomes. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
| 653 | a complex 1 | |
| 653 | a alamethicin | |
| 653 | a NADH dehydrogenase | |
| 653 | a electron-transport chain | |
| 653 | a permeabilization | |
| 653 | a plant mitochondria | |
| 700 | 1 | a Michalecka, Agnieszkau Lund University,Lunds universitet,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science4 aut0 (Swepub:lu)fysb-ami |
| 700 | 1 | a Moller, IM4 aut |
| 700 | 1 | a Rasmusson, Allanu Lund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science4 aut0 (Swepub:lu)fysb-ara |
| 710 | 2 | a Biologiska institutionenb Naturvetenskapliga fakulteten4 org |
| 773 | 0 | t Biochemical Journalg 380:1, s. 193-202q 380:1<193-202x 0264-6021 |
| 856 | 4 | u http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1224159&blobtype=pdfy FULLTEXT |
| 856 | 4 | u http://dx.doi.org/10.1042/BJ20031969y FULLTEXT |
| 856 | 4 8 | u https://lup.lub.lu.se/record/277091 |
| 856 | 4 8 | u https://doi.org/10.1042/BJ20031969 |
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