Purification and characterisation of an archaebacterial succinate dehydrogenase complex from the plasma membrane of the thermoacidophile <i>Sulfolobus acidocaldarius</i>

Moll, Ralf; Schäfer, Günter

doi:10.1111/j.1432-1033.1991.tb16319.x

Cited by 49 publications

(43 citation statements)

References 54 publications

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“…As succinate and NADH are almost equally capable of reducing the Rieske-type protein, it can be assumed that the physiological reductant within the membrane is caldariellaquinone, the putative electron acceptor of both NADH-and succinate dehydrogenases [3,4]. These results would be compatible with a simple linear electron transport system like that found in mitochondria.…”

Section: Febs Letterssupporting

confidence: 78%

“…The signal at g = 4.3 indicates the presence of low symmetry nonheme iron. In the g = 2 region, an intense resonance with a g-value of 2.08, presumably due to copper and further signals at g -2, presumably due to the S3-center of the succinate-dehydrogenase [4] and to radicals are also observed. The resonances at g = 1.89 and g -1.73 have g-values very close to those of Riesketype iron-sulfur clusters from various sources [l].…”

Section: Resultsmentioning

confidence: 97%

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Evidence for a Rieske‐type FeS center in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

et al. 1993

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A high-potential iron-sulfur cluster with characteristics similar to a Rieske-type center was detected in the plasma membrane of Sulfolobus acidoculdurius by EPR spectroscopy. In the reduced form this center has g-values of g, = 2.031, gr = 1.890 and g, = 1.725 (gav = 1.88, rhombicity = 0.37) and its reduction potential at pH 7.4 was determined to be +325 + IO mV. The archaebacterial cluster exhibits some unique properties, in comparison to eubacterial and eukaryotic Rieske-type centers. First, the reduction potential is pH-dependent in the range from pH 6.7 to 8.2. Second, the typical inhibitor of Rieske FeS centers, DBMIB, had no effect on the g-values of this cluster. The center is reducible by both NADH and succinate in the presence of cyanide, an inhibitor of the terminal oxidases. The possible role of a Rieske-type center in an organism lacking any c-type cytochromes is discussed.

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Section: Febs Letterssupporting

confidence: 78%

Section: Resultsmentioning

confidence: 97%

Evidence for a Rieske‐type FeS center in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

et al. 1993

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“…S. acidocaldarius DSM 639 was grown aerobically at 75 to 80°C and pH 2.5 as described previously (40). Cells used for enzyme purification were harvested in the late logarithmic growth phase at an absorbance at 546 nm of 1.5 to 1.7; cells used for DNA or RNA extraction were harvested at an absorbance at 546 nm of 0.8 to 1.0.…”

Section: Methodsmentioning

confidence: 99%

“…The Sdh complex was isolated from plasma membranes of sonicated cells of S. acidocaldarius by solubilization with Chapso and subsequent hydroxyapatite and DEAE chromatography as described previously (40).…”

Section: Methodsmentioning

confidence: 99%

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A succinate dehydrogenase with novel structure and properties from the hyperthermophilic archaeon Sulfolobus acidocaldarius: genetic and biophysical characterization

1997

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The sdh operon of Sulfolobus acidocaldarius DSM 639 is composed of four genes coding for the 63.1-kDa flavoprotein (SdhA), the 36.5-kDa iron-sulfur protein (SdhB), and the 32.1-kDa SdhC and 14.1-kDa SdhD subunits. The four structural genes of the sdhABCD operon are transcribed into one polycistronic mRNA of 4.2 kb, and the transcription start was determined by the primer extension method to correspond with the first base of the ATG start codon of the sdhA gene. The S. acidocaldarius SdhA and SdhB subunits show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane ␣-helical regions present in all other succinate:quinone reductases (SQRs) and quinol:ifumarate reductases (QFRs) so far examined. Moreover, the SdhC subunit reveals remarkable 30% sequence similarity to the heterodisulfide reductase B subunit of Methanobacterium thermoautotrophicum and Methanococcus jannaschii, containing all 10 conserved cysteine residues. Electron paramagnetic resonance (EPR) spectroscopic studies of the purified enzyme as well as of membranes revealed the presence of typical S1 [2Fe2S] and S2 [4Fe4S] clusters, congruent with the deduced amino acid sequences. In contrast, EPR signals for a typical S3 [3Fe4S] cluster were not detected. However, EPR data together with sequence information implicate the existence of a second [4Fe4S] cluster in S. acidocaldarius rather than a typical [3Fe4S] cluster. These results and the fact that the S. acidocaldarius succinate dehydrogenase complex reveals only poor activity with caldariella quinone clearly suggest a unique structure for the SQR of S. acidocaldarius, possibly involving an electron transport pathway from the enzyme complex into the respiratory chain different from those for known SQRs and QFRs.Succinate:quinone reductase (SQR), a membrane-bound enzyme complex and component of the respiratory chain (complex II) of all aerobic organisms, catalyzes the oxidation of succinate to fumarate in the tricarboxylic acid cycle and transfers the electrons directly to quinones in the membrane. The reverse reaction, the reduction of fumarate, which is the last step in fumarate respiration of anaerobic or facultative anaerobic organisms, is catalyzed by quinol:fumarate reductase (QFR). The two enzyme complexes are very similar with regard to composition of subunits, prosthetic groups, and probably structure (2, 24). SQRs and QFRs are composed of three or four subunits of which the largest protein is a flavoprotein (M r of 65,000 to 79,000) carrying covalently bound 8-␣-N(3)-histidyl-flavin adenine dinucleotide (FAD). An iron-sulfur protein (M r of 25,000 to 37,000) together with this flavoprotein subunit represents the peripheral part of the enzyme complex. The iron-sulfur protein is suggested to contain three different types of iron-sulfur clusters, each equimolar with FAD. Magnetic circular dichroism and electron paramagnetic resonance...

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An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes.

Lübben¹,

Kolmerer²,

Saraste³

1992

The EMBO Journal

131

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The operon coding for a respiratory quinol oxidase was cloned from thermoacidophilic archaebacterium Sulfolobus acidocaldarius. It contains three genes, soxA, soxB and soxC. The first two genes code for proteins related to the cytochrome c oxidase subunits II and I, respectively. soxC encodes a protein homologous to cytochrome b, which is a subunit of the mitochondrial and bacterial cytochrome c reductases and the chloroplast cytochrome b6f complex. soxA is preceded by a promoter and the genes are cotranscribed into a 4 kb mRNA. Their protein products form a complex which has been partially purified and has quinol oxidase activity. The reduced minus oxidized absorption spectrum of the complex has two maxima at 586 and 606 nm. The latter is typical of cytochrome c oxidase. The complex contains four haems A. Two haems belong to the ‘cytochrome oxidase’ part of the complex and two are probably bound to be apocytochrome b (SoxC) and responsible for the 586 nm absorption peak. The homology between the sox gene products and their mitochondrial counterparts suggests that energy conservation coupled to the quinol oxidation catalysed either by the Sulfolobus oxidase or two mitochondrial respiratory enzymes may have a similar mechanism.

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Purification and characterisation of an archaebacterial succinate dehydrogenase complex from the plasma membrane of the thermoacidophile Sulfolobus acidocaldarius

Cited by 49 publications

References 54 publications

Evidence for a Rieske‐type FeS center in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

Evidence for a Rieske‐type FeS center in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

A succinate dehydrogenase with novel structure and properties from the hyperthermophilic archaeon Sulfolobus acidocaldarius: genetic and biophysical characterization

An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes.

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