Characterisation of the last Fe-S cluster-binding subunit of Neurospora crassa complex I

被引：7

作者：

Sousa, R

Barquera, B

Duarte, M

Finel, M

Videira, A ^{[1
]}

机构：

[1] Univ Porto, Inst Ciencias Biomed Abel Salazar, P-4100 Porto, Portugal

[2] Univ Helsinki, Dept Chem, Inst Biomed, SF-00100 Helsinki, Finland

[3] Univ Porto, Unidade Multidisiplinar Invest Biomed, P-4100 Porto, Portugal

[4] Univ Porto, Inst Mol & Celular Biol, P-4150 Porto, Portugal

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 1999年 / 1411卷 / 01期

基金：

芬兰科学院;

关键词：

mitochondrion; NADH dehydrogenase; complex I; iron-sulfur protein; cDNA; (Neurospora crassa);

D O I：

10.1016/S0005-2728(99)00014-6

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：

We have cloned cDNAs encoding the last iron-sulphur protein of complex I from Neurospora crassa. The cDNA sequence contains an open reading frame that codes for a precursor polypeptide of 226 amino acid residues with a molecular mass of 24 972 Da. Our results indicate that the mature protein belongs probably to the peripheral arm of complex I and is rather unstable when not assembled into the enzyme. The protein is highly homologous to the PSST subunit of bovine complex I, the most likely candidate to bind iron-sulphur cluster N-2. All the amino acid residues proposed to bind such a cluster are conserved in the fungal protein. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：142 / 146

页数：5

共 28 条

[1] Bovine-heart NADH:ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups [J].