Localization and Function of the Membrane-bound Riboflavin in the Na+-translocating NADH:Quinone Oxidoreductase (Na+-NQR) from Vibrio cholerae

被引：35

作者：

Casutt, Marco S. ^{[3
]}

Huber, Tamara ^{[1
]}

Brunisholz, Rene ^{[2
]}

Tao, Minli ^{[1
]}

Fritz, Guenter ^{[3
]}

Steuber, Julia ^{[1
]}

机构：

[1] Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland

[2] Funct Genom Ctr Zurich, CH-8057 Zurich, Switzerland

[3] Univ Freiburg, Dept Neuropathol, D-79106 Freiburg, Germany

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2010年 / 285卷 / 35期

基金：

瑞士国家科学基金会;

关键词：

NADH-QUINONE OXIDOREDUCTASE; MULTIPLE SEQUENCE ALIGNMENT; PUMPING NADH; DETERGENT BINDING; NADHUBIQUINONE OXIDOREDUCTASE; UBIQUINONE OXIDOREDUCTASE; PROTEIN STRUCTURE; CRYSTAL-STRUCTURE; PROSTHETIC GROUPS; ESCHERICHIA-COLI;

D O I：

10.1074/jbc.M109.071126

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The sodium ion-translocating NADH: quinone oxidoreductase (Na+-NQR) from the human pathogen Vibrio cholerae is a respiratory membrane protein complex that couples the oxidation of NADH to the transport of Na+ across the bacterial membrane. The Na+-NQR comprises the six subunits NqrABCDEF, but the stoichiometry and arrangement of these subunits are unknown. Redox-active cofactors are FAD and a 2Fe-2S cluster on NqrF, covalently attached FMNs on NqrB and NqrC, and riboflavin and ubiquinone-8 with unknown localization in the complex. By analyzing the cofactor content and NADH oxidation activity of subcomplexes of the Na+-NQR lacking individual subunits, the riboflavin cofactor was unequivocally assigned to the membrane-bound NqrB subunit. Quantitative analysis of the N-terminal amino acids of the holo-complex revealed that NqrB is present in a single copy in the holo-complex. It is concluded that the hydrophobic NqrB harbors one riboflavin in addition to its covalently attached FMN. The catalytic role of two flavins in subunit NqrB during the reduction of ubiquinone to ubiquinol by the Na+-NQR is discussed.

引用

页码：27088 / 27099

页数：12

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