Electron transport and energy conservation in the archaebacterium<i>Sulfolobus acidocaldarius</i>

Schäfer, Günter; Anemüller, Stefal; Moll, Ralf; Meyer, W.; Lübben, Mathias

doi:10.1111/j.1574-6968.1990.tb04106.x

Cited by 44 publications

(17 citation statements)

References 37 publications

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“…6). The observed temperature optimum for succinate -PMS-C121nd oxidoreductase at 81 "C corresponds to the reported optimum growth temperature of Sulfolobus [31]. Evaluation of primary data in Arrhenius plot analysis (Fig.…”

Section: Enzymatic Propertiessupporting

confidence: 65%

“…This indicated that redox reactions catalysed by SDH are rate-limited by the applied electron acceptor as has also been reported for soluble heart muscle SDH [46]. c) However, added caldariella quinone, the physiologically acting electron mediator in Suljolobus membranes [31], was only slowly reduced as compared to water-soluble dyes. This may reflect an unfavourable accessibility of the quinone binding site since caldariella quinone had to be added in Triton X-100 dispersed form.…”

Section: Enzymatic Propertiesmentioning

confidence: 81%

“…Therefore reduction of C1,Ind directly by a prosthetic group or a tightly bound caldariella quinone might be concluded. Though caldariella quinone is likely to serve as a central pool for reducing equivalents in the respiratory chain of Sulfolobus [31], the low activities of the isolated SDH complex with the detergent-dispersed quinone as an electron acceptor was surprising. Besides deprivation of lipids (see Results), the loss of other essential compounds may be a likely reason.…”

Section: Discussionmentioning

confidence: 99%

“…Caldariella quinone reduction was recorded by dual-wavelength spectroscopy (Sigma ZWS I1 spectrophotometer) at 351 nm minus 341 nm [31] using a differential absorption coefficient A& of 1778 M-' cm-'. Tests were performed in 88 mM KH2P04, 29 mM disodium succinate, 0.18% (massivol.)…”

Section: Analytical Proceduresmentioning

confidence: 99%

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

Moll

Schäfer

1991

European Journal of Biochemistry

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A succinate dehydrogenase complex was isolated in a three-step purification from plasma membranes of the thermoacidophilic archaebacterium Suljolobus acidocaldarius. It consists of four subunits : a, 66 kDa ; b, 3 1 kDa; c, 28 kDa and d, 12.8 kDa. In the 141-kDa native protein, the four subunits are present in an equimolar stoichiometry. The complex contains acid-non-extractable flavin, iron and acid-labile sulphide. Maximal succinate dehydrogenase activities were recorded at pH 6.5, which coincides with the internal pH of Suljolobus cells. The temperature optimum of 8 1 "C defines the Sulfolobus succinate dehydrogenase as a thermophilic enzyme complex. The K , for succinate was found to be 1.42 mM (55°C). Similar to the mitochondrial soluble succinate dehydrogenase, this enzyme is capable of transferring electrons to artifical electron acceptors, for instance phenazine methosulfate, N,N,N',N'-tetramethyl-p-phenylenediamine and ferricyanide. In contrast to the mitochondrial succinate dehydrogenase, the archaebacterial enzyme reduces 1,4-dichloroindophen01 also in the absence of phenazine methosulfate. Caldariella quinone, the physiological electron mediator in the Sulfolobus respiratory chain, was only slowly reduced under adjusted conditions. The succinate -phenazine methosulfate-(l,4-dichloroindopheno1) oxidoreductase of the isolated complex was strongly inhibited by tetrachlorobenzoquinone. In plasma membranes the complex reduces molecular oxygen in a cyanide-sensitive reaction. Polyclonal Suljolobus anti-a antibodies crossreacted with 66 -67-kDa polypeptides from membranes of Therrnoplasma acidophiliurn, Sulfolohus solfataricus and beef heart submitochondrial particles.Succinate dehydrogenase (SDH) complexes have been isolated and characterized from beef heart mitochondria [l, 21 and from eubacteria, like the Gram-positive Bacillus subtilis [3], the Gram-negative Escherichia coli Paracoccus denifr$cans [lo] and others [ll -131. The water-soluble form of mitochondrial SDH, representing the peripheral part of a larger membrane-spanning complex, is composed of a 70-kDa polypeptide, the flavoprotein and a 27-kDa polypeptide, the iron-sulfur protein subunit. While the flavoprotein carries covalently bound 8-a-N(3)-histidyl-FAD, it was suggested that the iron-sulfur protein contains three FeS clusters : the Correspondence to G. Schafer, Institut fur Biochemie, Medizinische Universitat zu Lubeck, Ratzeburger Allee 160, W-2400 Lubeck 1 , Federal Republic of Germany Abbreviations. PMS, phenazine methosulfate; C121nd, 1,4-dichloroindophenol; Qca', caldariella quinone; Qo, 2,3-dimethoxy-5-methyl-1,4-benzoquinone; QI, ubiquinone-1 ; Qhr ubiquinone-6, PhMeSo2F, phenylmethylsulphonyl fluoride; Chapso, 3-[(3-cholamidopropyI)-dimethylammonio]-2-hydroxy-l-propanesulfonic acid; SB 12, N-dodecyl-N,N-dimethylammonio-3-propanesulfonic acid; Ph(NMe)2, N,N,N',N'-tetramethyl-p-phenylenediamine; SDH, succinate dehydrogenase.Enzymes. Succinate dehydrogenase (EC 1.3.99.1); cytochrome ua3 (EC 1.9.3.1); ATPase or ATP synthase (EC 3.6...

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Section: Enzymatic Propertiessupporting

confidence: 65%

Section: Enzymatic Propertiesmentioning

confidence: 81%

Section: Discussionmentioning

confidence: 99%

Section: Analytical Proceduresmentioning

confidence: 99%

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

Moll

Schäfer

1991

European Journal of Biochemistry

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“…Two terminal oxidases have been identified in its plasma membrane (8,45,46) and genetically characterized (13,29). Both are sharing an unusual complexity compared with other procaryotic cytochrome c or quinol oxidases (for a review see Refs.…”

Section: Discussionmentioning

confidence: 99%

The Archaeal SoxABCD Complex Is a Proton Pump in Sulfolobus acidocaldarius

Gleißner

Kaiser

Antonopoulos

et al. 1997

Journal of Biological Chemistry

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The thermoacidophilic archaeon Sulfolobus acidocaldarius expresses a very unusual quinol oxidase, which contains four heme a redox centers and one copper atom. The enzyme was solubilized with dodecyl maltoside and purified to homogeneity by a combination of hydrophobic interaction and anion exchange chromatography. The oxidase complex consists of four polypeptide subunits with apparent molecular masses of 64, 39, 27, and 14 kDa that are encoded by the soxABCD operon (Lü bben, M., Kolmerer, B., and Saraste, M. (1992) EMBO J. 11, 805-812). The optical spectra and redox potentials of the SoxABCD complex have been characterized, and the absorption coefficients of the contributing cytochromes a 587 and aa 3 were determined. The EPR spectra indicate the presence of three low spin and one high spin heme species, the latter associated with the binuclear heme Cu B site. Standard midpoint potentials of the cytochrome a 587 heme centers were determined as ؉210 and ؉270 mV, respectively. The maximum turnover of the complex (1300 s ؊1 at 65°C) was found to be about three times greater than that of the previously studied isolated cytochrome aa 3 subunit alone (Gleissner, ؉ /e ؊ ratio >1 was determined, identifying the SoxABCD complex as a proton-pumping quinol oxidase. According to structural analysis, the cytochrome aa 3 moiety of the complex does not contain the signature of a H ؉ pumping channel as identified in Rhodobacter sphaeroides or Paracoccus denitrificans. Therefore, for H ؉ translocation, a mechanism different from that in typical heme-copper oxidases of the aa 3 or bo 3 type is discussed.M

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How can Archaea Cope with Extreme Acidity?

Schäfer

2007

Novartis Foundation Symposium 221 ‐ Bacterial Responses to pH

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Electron transport and energy conservation in the archaebacteriumSulfolobus acidocaldarius

Cited by 44 publications

References 37 publications

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

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

The Archaeal SoxABCD Complex Is a Proton Pump in Sulfolobus acidocaldarius

How can Archaea Cope with Extreme Acidity?

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