BRENDA - Enzyme Database

X-ray absorption spectroscopic analysis of reductive [2Fe-2S] cluster degradation in hyperthermophilic archaeal succinate:caldariellaquinone oxidoreductase subunits

Li, Z.; Shokes, J.E.; Kounosu, A.; Imai, T.; Iwasaki, T.; Scott, R.A.; Biochemistry 42, 15003-15008 (2003)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
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
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
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
-
1.3.5.1
Sulfurisphaera tokodaii
-
-
-
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
-
1.3.5.1
Sulfurisphaera tokodaii 7
-
-
-
Cloned(Commentary) (protein specific)
EC Number
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
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