Structural homologies between the amino acid sequence of Clostridium pasteurianum MoFe protein and the DNA sequences of nifD and K genes of phylogenetically diverse bacteria

FEBS Letters

Nakano, Tohru²  Hase, Toshiharu²  Wakabayashi, Sadao²  Matsubara, Hiroshi²  Zumft, Walter G.¹ 

[1] Lehrstuhl für Mikrobiologie, Universität Karlsruhe, Kaiserstrasse 12, D-7500 Karlsruhe 1, FRG;Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan

关键词: Amino acid sequence;    Nitrogenase;    MoFe protein;    Sequence homology;    Clostridium;    N-;    amino-: C-;    carboxyl-: Cm-;    S-carboxymethyl-: HPLC;    high performance liquid chromatography;    TLC;    thin-layer chromatography;   

DOI  :  10.1016/0014-5793(84)80040-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The complete amino acid sequence of the larger (α-) subunit and about 70% of the total sequence of the smaller (β-) subunit of the MoFe protein from Clostridium pasteurianum was determined by analyses of peptides derived from BrCN cleavage and by digestions with trypsin, staphylococcal protease and lysylendo-peptidase of the separated subunits. The α-subunit has 529 amino acid residues, giving an M _r value of 58 774. This is the first complete sequence for the α-subunit of an isolated MoFe protein. In comparing the sequences of both subunits to those from other sources, 5 out of 9 cysteines in the α-subunit and 3 out of 6 in the β-subunit are invariant, thus suggesting a function as ligands to FeS and MoFeS clusters in the MoFe protein. All of these cysteines are located in the amino terminal halves of both subunits.

【 授权许可】

Unknown