Recent progress in the Na+-translocating NADH-quinone reductase from the marine Vibrio alginolyticus

被引:83
作者
Hayashi, M [1 ]
Nakayama, Y [1 ]
Unemoto, T [1 ]
机构
[1] Chiba Univ, Fac Pharmaceut Sci, Lab Membrane Biochem, Inage Ku, Chiba 2638522, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2001年 / 1505卷 / 01期
关键词
Na+ pump; NADH-quinone reductase; respiratory chain; flavin cofactor; marine bacterium; Vibrio alginolyticus;
D O I
10.1016/S0005-2728(00)00275-9
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 respiratory chain of Cram-negative marine and halophilic bacteria has a Na+-dependent NADH-quinone reductase that functions as a primary Na+ pump. The Na+-translocating NADH-quinone reductase (NQR) from the marine Vibrio alginolyticus is composed of six structural genes (nqrA to nqrF). The NqrF subunit has non-covalently bound FAD. There are conflicting results on the existence of other flavin cofactors. Recent studies revealed that the NqrB and NqrC subunits have a covalently bound flavin, possibly FMN, which is attached to a specified threonine residue. A novel antibiotic, korormicin, was found to specifically inhibit the NQR complex. From the homology search of the nqr operon, it was found that the Na+-pumping NQR complex is widely distributed among Gram-negative pathogenic bacteria. (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:37 / 44
页数:8
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