Open AccessStructurally identical porin in lithoauto‐ and organoheterotrophically grown Rhodobacter capsulatus cells
Author(s) -
Waldmann Ulrich,
Robledano Mafalda,
Weckesser Jürgen,
Schulz Georg
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07798.x
Subject(s) - rhodobacter , porin , biochemistry , amino acid , crystallization , isoelectric focusing , peptide sequence , isoelectric point , chemistry , biology , stereochemistry , bacterial outer membrane , gene , escherichia coli , enzyme , organic chemistry , mutant
The porin from lithoautotrophically grown Rhodobacter capsulatus 37b4 cells migrated identically to porin from organoheterotrophic cells on SDS‐PAGE. Moreover, it behaved comparably in isoelectric focusing, and it was also EDTA‐sensitive. Furthermore, the porins of the two growth conditions were essentially identical in amino acid composition and N‐terminal amino acid sequence. A final proof for structural identity could be obtained by crystallization and structural analysis showing identity in all non‐hydrogen atoms.