Proteolysis of Paracoccus denitrificans cytochrome oxidase by trypsin and chymotrypsin.
Paracoccus oxidase containing only two subunits was subjected to proteolysis by trypsin and chymotrypsin. Both subunits of the purified enzyme were cleaved at only a few sites and enzymatic activity was not inhibited. The cleavage sites were identified by protein sequencing. Subunit I was cleaved near the amino-terminus and subunit II in the loop connecting the two predicted trans-membrane helices. In native membrane fragments, but not in intact spheroplasts, this loop was accessible to both proteases. These results provide experimental evidence for the folding of subunit II in the membrane.
Finel
M
M
Department of Medical Chemistry, University of Helsinki, Finland.
D002918:Chymotrypsin / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000378:metabolism*; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000378:metabolism; D010230:Paracoccus / Q000201:enzymology*; D010449:Peptide Mapping; D011487:Protein Conformation; D012995:Solubility; D014357:Trypsin / Q000378:metabolism*
D046911:Macromolecular Substances; D008565:Membrane Proteins; D003576:Electron Transport Complex IV; D002918:Chymotrypsin; D014357:Trypsin