The structure of porin from Paracoccus denitrificans at 3.1 Å resolution
✍ Scribed by A. Hirsch; J. Breed; K. Saxena; O-M.H. Richter; B. Ludwig; K. Diederichs; W. Welte
- Book ID
- 117107277
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 744 KB
- Volume
- 404
- Category
- Article
- ISSN
- 0014-5793
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## Abstract Porins from outer membrane of Gram‐negative bacteria have a highly stable structure. Our previous studies on porin from __Paracoccus denitrificans__ showed that the outer membrane protein porin is extremely stable toward heat, pH, and chemical denaturants. The major question we have add
Electron transfer (ET) between the large membrane-integral redox complexes in the terminal part of the respiratory chain is mediated either by a soluble__c__-type cytochrome, as in mitochondria, or by a membrane-anchored cytochrome__c__, as described for the ET chain of the bacterium__Paracoccus den