Structural studies on three flavin‐interacting regions of the flavoprotein subunit of complex II in Ascaris suum mitochondria

FEBS Letters

Takamiya, Shinzaburo¹  Konishi, Kiyoshi¹  Furushima, Rieko¹  Oya, Hiroshi¹  Kita, Kiyoshi¹  Aoki, Takashi¹ 

[1] Department of Parasitology, Juntendo University, School of Medicine, Bunkyo-ku, Tokyo 113, Japan

关键词: Complex II;    Flavoprotein;    Flavin-binding domain;    Fumarate reductase;    Anaerobic respiration;    (Ascaris);   

DOI  :  10.1016/0014-5793(90)81405-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown