Evidence that cytochrome b is the antimycin-binding component of the yeast mitochondrial cytochrome bc1 complex

Roberts, Henry; Smith, Stuart; Marzuki, Sangkot; Linnane, Anthony W.

doi:10.1016/0003-9861(80)90368-9

Cited by 43 publications

(18 citation statements)

References 30 publications

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“…1A) and in mitochondria isolated from AA-treated cells (Fig. 3) and is due to the ability of AA to block electron transfer between Cyt b and cl in complex III (Cyt c reductase) of the mETC (20,23). It should be noted that AA also inhibits cyclic electron transport in chloroplasts by binding to a b-type Cyt (22), but this is not an important consideration in these heterotrophic suspension cells.…”

Section: Discussionmentioning

confidence: 99%

“…AA is a specific inhibitor that blocks electron transfer between Cyt b and cl in the CP (20,23). In Euglena gracilis, addition of AA induced CN-resistant respiration within 5 h (2-4).…”

mentioning

confidence: 99%

“…Also, interpretation of the data is hampered because KCN is known to inhibit many enzymes of metabolism (29). Nevertheless, inhibition of the CP by a specific respiratory inhibitor may be a useful tool to study mechanisms of induction of AP capacity in plants.AA is a specific inhibitor that blocks electron transfer between Cyt b and cl in the CP (20,23). In Euglena gracilis, addition of AA induced CN-resistant respiration within 5 h (2-4).…”

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confidence: 99%

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Coordinate Regulation of Cytochrome and Alternative Pathway Respiration in Tobacco

Vanlerberghe

McIntosh²

1992

Plant Physiol.

103

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In suspension cells of NT1 tobacco (Nicotiana tabacum L. cv bright yellow), inhibition of the cytochrome pathway of respiration with antimycin A induced a large increase in the capacity of the alternative pathway over a period of approximately 12 h, as confirmed in both whole cells and isolated mitochondria. The increase in alternative pathway capacity required de novo RNA Mitochondrial electron transport in plants may proceed through either the CP2 or the AP (6,12,14). Transfer of electrons from NADH through the CP is coupled at three sites to the translocation of protons from the matrix to the intermembrane space. Reentry of protons to the matrix through complex V (mitochondrial ATP synthetase) results in the production of ATP. In this case, carbon oxidation in respiration is coupled to the production of ATP, and in many instances respiration rate is tightly regulated by the availability of ADP (i.e. adenylate control) (8, 12). Transfer of electrons through the AP bypasses two of the three sites of proton translocation. Under these conditions, carbon oxidation is not as tightly coupled to the production of ATP, and it is expected that respiration rate would not be as strictly regulated by the availability of ADP (8,12 It seems imperative that plants be able to regulate in a coordinate fashion the partitioning of electrons between the CP and the AP to meet changing metabolic requirements. Two important factors to be regulated will be, first, the capacity of each pathway to transfer electrons, and second, the degree to which that capacity is used (i.e. the degree of engagement of the pathway). The degree of engagement of the AP is dependent upon the redox poise of the ubiquinone pool (9) and, to some extent, upon the substrates being oxidized by the mitochondria (7).Although many studies indicate that plants are capable of altering the capacity of the AP (6, 14), little is known about the mechanisms by which this occurs. Some studies show that inhibition of the CP with respiratory inhibitors increases AP respiration. For example, treatment of rice roots with low concentrations of KCN or NaN3 for 6 h resulted in increased CN-resistant respiration, although it was not shown whether this CN-resistant respiration was sensitive to SHAM (11). In pea roots, a CN-resistant and SHAM-sensitive component of respiration was induced after several hours of KCN treatment (28). From the above reports, it is not clear whether the KCN treatment increased the capacity or simply the engagement of the AP. Also, interpretation of the data is hampered because KCN is known to inhibit many enzymes of metabolism (29). Nevertheless, inhibition of the CP by a specific respiratory inhibitor may be a useful tool to study mechanisms of induction of AP capacity in plants.AA is a specific inhibitor that blocks electron transfer between Cyt b and cl in the CP (20,23). In Euglena gracilis, addition of AA induced CN-resistant respiration within 5 h (2-4). A similar induction was seen in the yeast Hansenula anomala (17) and led to the ide...

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Section: Discussionmentioning

confidence: 99%

“…AA is a specific inhibitor that blocks electron transfer between Cyt b and cl in the CP (20,23). In Euglena gracilis, addition of AA induced CN-resistant respiration within 5 h (2-4).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

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Coordinate Regulation of Cytochrome and Alternative Pathway Respiration in Tobacco

Vanlerberghe

McIntosh²

1992

Plant Physiol.

103

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“…Its a band maximum is shifted by 2 nm towards the higher wavelengths by antimycin. These results strongly suggest a direct action of this inhibitor on the bMo species, which would be similar to its action in yeast (29).…”

Section: Resultsmentioning

confidence: 52%

Optical and Potentiometric Study of the b- and c-Type Cytochromes in Mushroom Agaricus bisporus Lge Mitochondria

Denis

Gallinet

1981

Plant Physiol.

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Agaricus bisporus Lge. mushroom belongs to the Basidiomycete species and lies in the evolution tree between lower mushrooms, Ascomycete species (like yeast, Neurospora crassa), and higher plant organisms. This variety of mushroom is, therefore, of particular interest when looking at some evolution effects on oxidation metabolisms or on the structure and function of the respiratory chain in the mitochondrial membrane. Results concerning the number and the role of the Cyt b in the mitochondrial respiratory chain depend on the investigated organisms, and it should be of some help to shed some light in that direction.It is generally accepted that there are only two b-type Cyt in complex III of the mammalian mitochondrial respiratory chain (28,33), although a larger number of components have been described optically or potentiometrically (35). Dual wavelength difference spectrometry has brought evidence for three spectral forms of b-type Cyt in higher plants (24,27). However, more Permanent address:

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“…No direct evidence is presently available which definitively identifies the antimycin-binding components of the bc, complex. However a recent study of Roberts et al [19] on the binding of antimycin to mitochondrial particles of antimycin-resistant and cytochrome-b-deficient yeast strains, furnishes new support to previous indirect evidence [23] that an antimycin-binding site is located on the apocytochrome b coded by mitochondrial DNA. This paper confirms that the absence of cytochrome h in Box strains is accompanied by the loss of the high-affinity binding of antimycin A .…”

Section: Interaction Bet Ween Diuron and Cytochrome Bmentioning

confidence: 68%

Modification of the Spectral Properties of Cytochrome b in Mutants of Saccharomyces cerevisiae Resistant to 3‐(3,4‐Dichlorophenyl)‐1,1‐dimethylurea

Briquet

Goffeau

1981

European Journal of Biochemistry

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The effects of five inhibitors of the cytochrome bc1 complex: 3‐(3.4‐dichlorophenyl)‐1,1‐dimethylurea (diuron), 2‐n‐heptyl‐4‐hydroxyqttinoline‐N‐oxide (HpHOQnO), antimycin A, funiculosin and mucidin were measured in submitochondrial particles of strains of the yeast Saccharomyces cerevisiae belonging to two classes of diuronresistant mutants Diu 1 and Diu 2 which are modified in different exons of the split mitochondrial gene of cytochrome b. The oxidation of NADH and of cytochronic b‐561 exhibits a similar resistance to diuron and HpHOQnO in Diu I and Diu2 mutants. No extra reduction of cytochrome b‐561 and cytochrome b‐565 is observed in the presence of diuron and HpHOQnO. Both Diu 1 and Diu 2 mutants exhibit the red shift of cytochrome b‐561 induced by concentrations of HpHOQnO 2‐3‐times higher than those required in the parental strain. The spectral and respiratory effects of antimycin A, funiculosin and mucidin are generally similar in the diuron‐resistant mutants and in their parental strains. However a cross‐resistance between diuron and antimycin A is indicated in one Diu 2 mutant. From the combined genetic and biochemical data it is concluded that the interaction of diuron and HpHOQnO with cytochrome b is mediated by at least two specific amino acids located apart in tile central region of tile apocytochrome b peptide coded by mitochondrial DNA. These two amino acids control tightly the extra reduction of cytochromes b‐565 and b‐561 as well as tile flow of electrons through the bc1 complex. However the binding of HpHOQnO required for the expression of the red shift of cytochrome b‐561 is only slightly affected by the diu‐l and diu‐2 mutations.

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Evidence that cytochrome b is the antimycin-binding component of the yeast mitochondrial cytochrome bc1 complex

Cited by 43 publications

References 30 publications

Coordinate Regulation of Cytochrome and Alternative Pathway Respiration in Tobacco

Coordinate Regulation of Cytochrome and Alternative Pathway Respiration in Tobacco

Optical and Potentiometric Study of the b- and c-Type Cytochromes in Mushroom Agaricus bisporus Lge Mitochondria

Modification of the Spectral Properties of Cytochrome b in Mutants of Saccharomyces cerevisiae Resistant to 3‐(3,4‐Dichlorophenyl)‐1,1‐dimethylurea

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