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Literature summary extracted from

  • Li, Z.; Shokes, J.E.; Kounosu, A.; Imai, T.; Iwasaki, T.; Scott, R.A.
    X-ray absorption spectroscopic analysis of reductive [2Fe-2S] cluster degradation in hyperthermophilic archaeal succinate:caldariellaquinone oxidoreductase subunits (2003), Biochemistry, 42, 15003-15008.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.5.1 SdhC and the N-terminal domain fragment of SdhB of respiratory complex II are overproduced in Escherichia coli Sulfurisphaera tokodaii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.5.1 iron-sulfur centre K-edge X-ray absorption spectroscopy is used to monitor the structural changes of their Fe sites in the irreversible [2Fe-2S] cluster degradation process. Regardless of the differences in the cluster-ligating cysteine motifs and the XAS-detectable [2Fe-2S]2+ cluster environments, a complete reductive breakdown of the [2Fe-2S] clusters results in the appearance of a new Fourier transform peak at about 3.3 A with a concomitant loss of the Fe-Fe interaction at ca. 2.7 A for both proteins. The results suggest that a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de novo biosynthesis and/or regulation of iron-binding enzymes in the cellular system Sulfurisphaera tokodaii
1.3.5.1 [2Fe-2S]-center the [2Fe-2S] cluster in SdhB-N and center C in SdhC are two succinate reducible high-potential centers detected in the archaeal succinate:caldariellaquinone oxidoreductase complex that differ in their arrangements of the cluster-binding cysteine motifs and the local cluster surroundings. a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de noVo biosynthesis and/or regulation of iron-binding enzymes in the cellular system Sulfurisphaera tokodaii

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Sulfurisphaera tokodaii
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1.3.5.1 Sulfurisphaera tokodaii F9VN10 and Q9C4L8 and F9VN12 and F9VN13 F9VN10: subunit sdhA, Q9C4L8: subunit sdhB, F9VN12: subunit sdhC, F9VN13: subunit sdhD
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1.3.5.1 Sulfurisphaera tokodaii 7
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1.3.5.1 Sulfurisphaera tokodaii 7 F9VN10 and Q9C4L8 and F9VN12 and F9VN13 F9VN10: subunit sdhA, Q9C4L8: subunit sdhB, F9VN12: subunit sdhC, F9VN13: subunit sdhD
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Synonyms

EC Number Synonyms Comment Organism
1.3.5.1 succinate dehydrogenase (caldariellaquinone)
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 Sulfurisphaera tokodaii
1.3.5.1 succinate:caldariellaquinone oxidoreductase
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 Sulfurisphaera tokodaii