Comparative aspects of quinol-cytochrome c/plastocyanin oxidoreductases

Hauska, Günter; Hurt, Eduard C.; Gabellini, Nadia; Lockau, Wolfgang

doi:10.1016/0304-4173(83)90002-2

Cited by 397 publications

(174 citation statements)

References 251 publications

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“…Also, the topology of the Fe/S protein (and of cytochrome cl) appears to be the same in both cases: the Fe/S protein is on the opposite side of the F,-ATPase, i.e., facing the intermembrane space in mitochondria and facing the thylakoid lumen in photosynthetic bacteria. As judged from all available data, the function, topology, and structure of the Fe/S proteins in the mitochondrial bc, complex, the bacterial bc, complex, and the chloroplast bef complex are directly comparable (Hauska et al, 1983).…”

Section: Discussionmentioning

confidence: 97%

“…A striking homology of the Fe/S protein of this prokaryote to the Neurospora Fe/S protein has been observed. The function of the R. sphaeroides Fe/S protein is directly comparable to that of the mitochondrial Fe/S protein, since it is part of a bc, complex and transfers electrons to cytochrome cl (Trumpower, 1981;Hauska et al, 1983). The Ft. sphaeroides and mitochondrial cytochromes cl display a remarkable homology.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

Hartl

Schmidt

Wächter

et al. 1986

Cell

322

214

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

Hartl

Schmidt

Wächter

et al. 1986

Cell

322

214

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“…The use of electron transport inhibitors, such as antimycin A and myxothiazol, has provided us with strong evidence for the existence of a 'Qcycle' type of electron transfer pathways in the mitochondrial and bacterial cytochrome ba-cl complexes [5]. On the other hand, our understanding of the cytochrome be-f complex in higher plants is comparatively meager.…”

Section: Introductionmentioning

confidence: 99%

“…This is found in both the mitochondrial-type complexes (cf. [5]) and in the b6-f complex from spinach (un-published). The inhibitors DBMIB, DNP-INT and UHDBT have all been shown to interact with the Rieske Fe-S protein in the bc-f complex [8].…”

Section: Introductionmentioning

confidence: 99%

The effects of quinone analogues on cytochrome b₆ reduction and oxidation in a reconstituted system

Lam

1984

FEBS Letters

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The reconstituted system containing Photosystem I, plastocyanin and the cytochrome kfcomplex is used to study the effects of various quinone analogues on the redox behavior of cytochrome be. The effects of DBMIB, DNP-INT and HQNO are compared in an attempt to discern the modes of action of these quinone analogues. Both DBMIB and DNP-INT are potent inhibitors of the plastocyanin reductase activity of the isolated cytochrome complex. However, while DBMIB abolished the oxidant-induced reduction of cytochrome b6, DNP-INT only inhibited about 25% of the net reduction. On the other hand, HQNO does not show any significant inhibition of plastocyanin reductase activity of the isolated cytochrome complex at concentrations up to 20pM. An enhancement of the net amount of cytochrome be reduced is observed in the presence of HQNO. Both DNP-INT and HQNO inhibited the dark oxidation rate of cytochrome be. The possible identity of the oxidant for cytochrome b6 is discussed. Plastoquinone is concluded to be the most likely candidate. DNP-INT is concluded to have at least two sites of inhibition in the cytochrome complex. The implications of these findings on quinone functions in the cytochrome b6-f complex are discussed.

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“…The cytochrome bc~ complexes of mitochondria contain 9-11 polypeptides [1], while the counterpart complexes which have been purified from prokaryotes typically contain many fewer subunits [2]. For example, the complexes from Paracoecus denitrificans [3] and Rhodospirillum rubrum [4,5] contain only three electron transfer proteins, cytochrome bo cytochrome cl and Rieske iron-sulfur protein.…”

Section: Introductionmentioning

confidence: 99%

Deletion of subunit 9 of the Saccharomyces cerevisiae cytochrome bc₁ complex specifically impairs electron transfer at the ubiquinol oxidase site (center P) in the bc₁ complex

1992

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Deletion of QcRg, the nuclear gene encoding subunit 9 of the mitochondrial cytoehromc bc, complex in Saccharono,ces cerevisiae, results in inactivation of the bc~ complex and inabillity of the yeast to grow on non-fermentable carbon sources. The loss of bet complex activity is due to loss of electron transfer activity at the ubiquinol oxidase site (center P) in the complex. Electron transfer at the abiquinone reductas¢ site (center N), is unaffected by the lo~s of subunit 9, but the extent of ¢ytochrome b reduction is diminished. This is the first instance in which a supernumerary polypeptide, lacking a redox prosthetic group, laas been shown to be required for an electron transfer reaction within the cytoehrome bc~ complex.

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Comparative aspects of quinol-cytochrome c/plastocyanin oxidoreductases

Cited by 397 publications

References 251 publications

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

The effects of quinone analogues on cytochrome b₆ reduction and oxidation in a reconstituted system

Deletion of subunit 9 of the Saccharomyces cerevisiae cytochrome bc₁ complex specifically impairs electron transfer at the ubiquinol oxidase site (center P) in the bc₁ complex

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Comparative aspects of quinol-cytochrome c/plastocyanin oxidoreductases

Cited by 397 publications

References 251 publications

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

The effects of quinone analogues on cytochrome b6 reduction and oxidation in a reconstituted system

Deletion of subunit 9 of the Saccharomyces cerevisiae cytochrome bc1 complex specifically impairs electron transfer at the ubiquinol oxidase site (center P) in the bc1 complex

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Product

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About

The effects of quinone analogues on cytochrome b₆ reduction and oxidation in a reconstituted system

Deletion of subunit 9 of the Saccharomyces cerevisiae cytochrome bc₁ complex specifically impairs electron transfer at the ubiquinol oxidase site (center P) in the bc₁ complex