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Structural studies on three flavin‐interacting regions of the flavoprotein subunit of complex II in Ascaris suum mitochondria
Author(s) -
Furushima Rieko,
Kita Kiyoshi,
Takamiya Shinzaburo,
Konishi Kiyoshi,
Aoki Takashi,
Oya Hiroshi
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81405-d
Subject(s) - flavoprotein , flavin group , protein subunit , ascaris suum , biochemistry , moiety , cofactor , chemistry , ascaris , biology , stereochemistry , enzyme , zoology , helminths , gene
The flavoprotein (Fp) subunit of mitochondrial complex II contains covalently bound FAD as a prosthetic group. In this study, the primary structure of the flavin‐bound tryptic peptide from the Fp subunit of Ascaris complex II was determined and found to be highly similar to those of the corresponding flavin‐binding regions of bovine heart and bacterial Fp subunits. Furthermore, the Ascaris Fp subunit was shown to contain two regions exhibiting striking sequence similarity to the segments that have been predicted to interact noncovalently with the AMP moiety of FAD in bacterial Fp subunits. The conservation of these two regions also in themitochondrial Fp subunit suggests their functional importance.