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   <subfield code="a">Intra- and Inter-Complex Cross-Linking of Subunits in the Quinol Oxidase Super-Complex from Thermophilic Bacillus PS3</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Takeshi Tanaka, Masatomo Inoue, Junshi Sakamoto, Nobuhito Sone]</subfield>
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   <subfield code="a">Gram-positive thermophilic Bacilli contain quinol-cytochrome c reductase and cyto-chrome c oxidase as two major respiratory complexes of the electron transfer chain, and these enzymes can be extracted with mild detergents as an associated quinol oxidase super-complex.The reductase is composed of three subunits; cytochrome b8 cytochrome c1, and FeS protein, whereas cytochrome c oxidase consists of four subunits numbered 1 through 4. In order to clarify the interactions between the subunits, the super-complex isolated from Bacillus PS3 was cross-linked with three bifunctional cross-linkers; disuccinimidyl tartrate, 3,3′-dithiobis(succinimidylpropionate), and ethylene glycolbis(sulfosuccinimi-dylsuccinate). The most prominent cross-linking was observed for the combination of subunit 1 plus 2 in cytochrome c oxidase, and for that of cytochrome b8 plus cytochrome C1 in the reductase. In addition to these intra-complex cross-linkings, inter-complex linking was observed for the combination of cytochrome b8 plus subunit 1 with ethylene glycolbis-(sulfosuccinimidylsuccinate), and for the combinations of cytochrome b8 plus subunit 1 and cytochrome fit, plus subunit 2 with 3,3 -dithiobis(succinimidylpropionate). Incubation in the presence of Triton X-100, which was confirmed to cleave the two enzyme complexes, selectively reduced the inter-complex cross-linking, suggesting that the chemical cross-linking reflect the spatial arrangement of subunits in the super-complex.</subfield>
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   <subfield code="a">chemical cross-linker</subfield>
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   <subfield code="a">intrinsic membrane protein</subfield>
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   <subfield code="t">The Journal of Biochemistry</subfield>
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