Transmembrane orientation and topology of the NADH:quinone oxidoreductase putative quinone binding subunit NuoH.
Transmembrane orientation and topology of the NADH:quinone oxidoreductase putative quinone binding subunit NuoH.
复制标题
NADH:醌氧化还原酶推定醌结合亚基 NuoH 的跨膜方向和拓扑。
DOI:
10.1016/s0005-2728(00)00265-6
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发表时间:
2001
期刊:
影响因子:
--
通讯作者:
C. Hägerhäll
中科院分区:
文献类型:
--
作者:
Robert S. Roth;C. Hägerhäll
NADH:quinone oxidoreductase, or Complex I, is a multi-subunit membrane-bound enzyme in the respiratory chain of many pro- and eukaryotes. The enzyme catalyzes the oxidation of NADH and donates electrons to the quinone pool, coupled to proton translocation across the membrane, but the mechanism of energy transduction is not understood. In bacteria the enzyme consists of 14 subunits, seven membrane spanning and seven protruding from the membrane. The hydrophobic NuoH (NQO8, ND1, NAD1, NdhA) subunit is seemingly involved in quinone binding. A homologous, structurally and most likely functionally similar subunit is also found in F420H2oxidoreductases and in complex membrane-bound hydrogenases. We have made theoretical analyses of NuoH and NuoH-like polypeptides and experimentally analyzed the transmembrane topology of the NuoH subunit from Rhodobacter capsulatus by constructing and analyzing alkaline phosphatase fusion proteins. This demonstrated that the NuoH polypeptide has eight transmembrane segments, and four highly conserved hydrophilic sequence motifs facing the inside, bacterial cytoplasm. The N-terminal and C-terminal ends are located on the outside of the membrane. A topology model of NuoH based on these results is presented, and implications from the model are discussed.
DOI:
--
发表时间:
1991
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Yun,CH;VanDoren,SR;Crofts,AR;Gennis,RB
通讯作者:
Gennis,RB
DOI:
10.1111/j.1432-1033.1994.tb19985.x
发表时间:
1994-01-15
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
作者:
FRIEDRICH, T;VANHEEK, P;WEISS, H
通讯作者:
WEISS, H
影响因子:
56.9
作者:
LAWRENCE, CE;ALTSCHUL, SF;WOOTTON, JC
通讯作者:
WOOTTON, JC