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Ligands to the 2Fe iron-sulfur center in succinate dehydrogenase

Aevarsson, A and Hederstedt, Lars LU (1988) In FEBS Letters 232(2). p.298-302
Abstract
Membrane-bound succinate oxidoreductases are flavoenzymes containing one each of a 2Fe, a 3Fe and a 4Fe iron-sulfur center. Amino acid sequence homologies indicate that all three centers are located in the Ip (B) subunit. From polypeptide and gene analysis of Bacillus subtillis succinate dehydrogenase-defective mutants combined with earlier EPR spectroscopic data, we show that four conserved cysteine residues in the first half of Ip are the ligands to the [2Fe-2S] center. These four residues have previously been predicted to be the ligands. Our results also suggest that the N-terminal part of B. subtilis Ip constitutes a domain which can incorporate separately the 2Fe center and interact with Fp, the flavin-containing subunit of the... (More)
Membrane-bound succinate oxidoreductases are flavoenzymes containing one each of a 2Fe, a 3Fe and a 4Fe iron-sulfur center. Amino acid sequence homologies indicate that all three centers are located in the Ip (B) subunit. From polypeptide and gene analysis of Bacillus subtillis succinate dehydrogenase-defective mutants combined with earlier EPR spectroscopic data, we show that four conserved cysteine residues in the first half of Ip are the ligands to the [2Fe-2S] center. These four residues have previously been predicted to be the ligands. Our results also suggest that the N-terminal part of B. subtilis Ip constitutes a domain which can incorporate separately the 2Fe center and interact with Fp, the flavin-containing subunit of the dehydrogenase.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEBS Letters
volume
232
issue
2
pages
298 - 302
publisher
Wiley-Blackwell
external identifiers
  • scopus:0024295186
ISSN
1873-3468
DOI
10.1016/0014-5793(88)80757-9
language
English
LU publication?
yes
id
ddc9c890-9ff7-4429-b451-9ee5e5d8c494
date added to LUP
2017-07-18 10:55:10
date last changed
2017-09-07 16:20:29
@article{ddc9c890-9ff7-4429-b451-9ee5e5d8c494,
  abstract     = {Membrane-bound succinate oxidoreductases are flavoenzymes containing one each of a 2Fe, a 3Fe and a 4Fe iron-sulfur center. Amino acid sequence homologies indicate that all three centers are located in the Ip (B) subunit. From polypeptide and gene analysis of Bacillus subtillis succinate dehydrogenase-defective mutants combined with earlier EPR spectroscopic data, we show that four conserved cysteine residues in the first half of Ip are the ligands to the [2Fe-2S] center. These four residues have previously been predicted to be the ligands. Our results also suggest that the N-terminal part of B. subtilis Ip constitutes a domain which can incorporate separately the 2Fe center and interact with Fp, the flavin-containing subunit of the dehydrogenase.<br/>},
  author       = {Aevarsson, A and Hederstedt, Lars},
  issn         = {1873-3468},
  language     = {eng},
  number       = {2},
  pages        = {298--302},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Ligands to the 2Fe iron-sulfur center in succinate dehydrogenase},
  url          = {http://dx.doi.org/10.1016/0014-5793(88)80757-9},
  volume       = {232},
  year         = {1988},
}