Electron-transfer complexes of Ascaris suum muscle mitochondria. III. Composition and fumarate reductase activity of complex II

Kita, Kiyoshi; Takamiya, Shinzaburo; Furushima, Rieko; Ma, Yongtao; Suzuki, Hiroshi; Ozawa, Takayuki; Okumura, Hiroshi

doi:10.1016/0005-2728(88)90210-1

Cited by 65 publications

(23 citation statements)

References 40 publications

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“…Complex II was purified from Ascaris mitochondria as described by Takamiya et al [3][4][5]. Purified complex II was treated with 20% (w/v) sodium dodecyl sulfate (SDS) and then subjected to gel chromatography on a Biogel P-60 (<400) column equilibrated with 2°70 (w/v) SDS [16].…”

Section: Purification Of the Fp Subunit From Ascaris Complex Hmentioning

confidence: 99%

“…We have isolated complex II from muscle mitochondria of adult worms of Ascaris [3][4][5][6], inhabitants of the host's small intestine where the oxygen 'supply is limited. Ascaris complex II, unlike its mammalian counterparts, functions physiologically as the terminal oxidase in the NADH-fumarate reductase system, an anaerobic respiratory chain [3,5].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Ascaris complex II, unlike its mammalian counterparts, functions physiologically as the terminal oxidase in the NADH-fumarate reductase system, an anaerobic respiratory chain [3,5]. Indeed, Ascaris complex II exhibits high fumarate reductase (FRD) activity over succinate-ubiquinone oxidoreductase (SDH) activity (SDH/FRD = 0.05) [5]. It is a major component of Ascaris mitochondria (8o70 of mitochondrial protein) [7] and is composed of the following four subunits: a flavoprotein (Fp) subunit containing a flavin (Mr= 68 kDa), an Ip subunit associated with iron-sulfur centers (Mr = 26 kDa) and two hydrophobic, heme bcontaining polypeptides called CybL and Cybs (Mr = 15 and 13.5 kDa, respectively) [3,5].…”

Section: Introductionmentioning

confidence: 99%

“…Indeed, Ascaris complex II exhibits high fumarate reductase (FRD) activity over succinate-ubiquinone oxidoreductase (SDH) activity (SDH/FRD = 0.05) [5]. It is a major component of Ascaris mitochondria (8o70 of mitochondrial protein) [7] and is composed of the following four subunits: a flavoprotein (Fp) subunit containing a flavin (Mr= 68 kDa), an Ip subunit associated with iron-sulfur centers (Mr = 26 kDa) and two hydrophobic, heme bcontaining polypeptides called CybL and Cybs (Mr = 15 and 13.5 kDa, respectively) [3,5]. In the case of bacteria, the genes of complex II have been cloned and sequenced from Escherichia coil (sdh and frd) [8][9][10], Bacillus subtilis (sdh ) [11,12] and Proteus vulgaris (frd) [13].…”

Section: Introductionmentioning

confidence: 99%

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Structural studies on three flavin‐interacting regions of the flavoprotein subunit of complex II in Ascaris suum mitochondria

et al. 1990

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The flavoprotein (Fp) subunit of mitochondrial complex II contains covalently bound FAD as a prosthetic group. In this study, the primary structure of the flavin-bound tryptic peptide from the Fp subunit of Ascaris complex II was determined and found to be highly similar to those of the corresponding flavin-binding regions of bovine heart and bacterial Fp subunits. Furthermore, the Ascaris Fp subunit was shown to contain two regions exhibiting striking sequence similarity to the segments that have been predicted to interact noncovalently with the AMP moiety of FAD in bacterial Fp subunits. The conservation of these two regions also in the mitochondrial Fp subunit suggests their functional importance.

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Section: Purification Of the Fp Subunit From Ascaris Complex Hmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Structural studies on three flavin‐interacting regions of the flavoprotein subunit of complex II in Ascaris suum mitochondria

et al. 1990

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Succinate:Quinone Oxidoreductases

Lancaster

2004

Handbook of Metalloproteins

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Succinate:quinone oxidoreductases encompass the succinate:quinone reductase (SQR) enzymes of aerobic respiration (respiratory complex II) and the quinol:fumarate reductase (QFR) enzymes of anaerobic respiration. These enzymes couple the two‐electron oxidation of succinate to fumarate to the two‐electron reduction of quinone to hydroquinone (quinol), and also catalyse the reverse reaction, the reduction of fumarate by quinol. Members of the superfamily are composed of two hydrophilic subunits, a large flavoprotein subunit A and a smaller subunit B containing three iron–sulfur centers, and one large subunit C or two small subunits C and D hydrophobic polypeptides that are integral membrane proteins and bind two, one, or no heme b groups. On the basis of the available crystal structures of members of the superfamily, structural and functional aspects of succinate:quinone oxidoreductases are comprehensively discussed.

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Succinate:Quinone Oxidoreductases

Lancaster

2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Electron-transfer complexes of Ascaris suum muscle mitochondria. III. Composition and fumarate reductase activity of complex II

Cited by 65 publications

References 40 publications

Structural studies on three flavin‐interacting regions of the flavoprotein subunit of complex II in Ascaris suum mitochondria

Structural studies on three flavin‐interacting regions of the flavoprotein subunit of complex II in Ascaris suum mitochondria

Succinate:Quinone Oxidoreductases

Succinate:Quinone Oxidoreductases

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