PRIMARY STRUCTURES OF 2 SUBUNITS OF NADH-UBIQUINONE REDUCTASE FROM NEUROSPORA-CRASSA CONCERNED WITH NADH-OXIDATION - RELATIONSHIP TO A SOLUBLE NAD-REDUCING HYDROGENASE OF ALCALIGENES-EUTROPHUS

被引:51
作者
PREIS, D
WEIDNER, U
CONZEN, C
AZEVEDO, JE
NEHLS, U
ROHLEN, D
VANDERPAS, J
SACKMANN, U
SCHNEIDER, R
WERNER, S
WEISS, H
机构
[1] UNIV DUSSELDORF,INST BIOCHEM,UNIV STR 1,W-4000 DUSSELDORF 1,GERMANY
[2] UNIV MUNICH,INST PHYSIOL CHEM,W-8000 MUNICH 2,GERMANY
关键词
NADH UBIQUINONE REDUCTASE; COMPLEX-I; NAD(H)-BINDING SITE; FMN-BINDING SITE; IRON-SULFUR CLUSTER; (NEUROSPORA-CRASSA);
D O I
10.1016/0167-4781(91)90049-R
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 primary structures of the nuclear-encoded 51 kDa and 78 kDa subunits of the respiratory chain NADH: ubiquinone reductase (complex I) from Neurospora crassa mitochondria were determined by sequencing cDNA and the N-terminus of the mature proteins. Both subunits are related to the soluble NAD-reducing hydrogenase of the bacterium Alcaligenes eutrophus. Sequence comparison between these subunits, the corresponding subunits of the bovine complex I and the bacterial NAD-reducing hydrogenase further confirms the binding sites of NAD(H), FMN and three iron-sulfur clusters.
引用
收藏
页码:133 / 138
页数:6
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