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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
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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
2021-01-03 10:10:37
@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}},
  doi          = {{10.1016/0014-5793(88)80757-9}},
  volume       = {{232}},
  year         = {{1988}},
}