NADPH‐sulfite reductase flavoprotein from Escherichia coli: Contribution to the flavin content and subunit interaction

FEBS Letters

Covès, Jacques¹  Eschenbrenner, Michel¹  Fontecave, Marc¹ 

[1] Laboratoire d'Etudes Dynamiques et Structurales de la Sélectivité, Unité de Recherche Associée au Centre National de la Recherche Scientifique no. 332, Université Joseph Fourier, BP 53, 38041 Grenoble Cédex 9, France

关键词: Sulfite reductase;    Flavoprotein;    Flavin;    Quaternary structure;    Escherichia coli;   

DOI  :  10.1016/0014-5793(95)01081-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The flavoprotein component (SiR-FP) of the sulfite reductase of E. coli is an octamer of the 66 kDa α subunit. It was shown to be cleaved in two peptide fragments. The 23 kDa fragment has been purified as a polymer of 8–10 subunits. It corresponds to the N-terminal part of the native protein and was shown to contain essentially FMN as cofactor. The 43 kDa fragment is monomeric. It contains exclusively FAD and remains able to catalyze efficiently NADPH-dependent reductions. One can conclude that each α-chain of SiR-FP is composed of two distinct domains, one binding FAD and the other FMN and that the FMN-binding domains cooperate for a head-to-head subunit interaction.

【 授权许可】

Unknown