Ligands to the 2Fe iron-sulfur center in succinate dehydrogenase
(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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Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/ddc9c890-9ff7-4429-b451-9ee5e5d8c494
- author
- Aevarsson, A and Hederstedt, Lars LU
- organization
- publishing date
- 1988
- 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}}, }