scholarly journals Separate binding sites for antimycin and mucidin in the respiratory chain of the bacterium Paracoccus denitrificans and their occurrence in other denitrificans bacteria

1988 ◽  
Vol 252 (3) ◽  
pp. 905-908 ◽  
Author(s):  
I Kucera ◽  
R Hedbávný ◽  
V Dadák
Keyword(s):  
Respiratory Chain ◽  
Binding Sites ◽  
Paracoccus Denitrificans ◽  
Pseudomonas Stutzeri ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Q Cycle ◽  
Cytochromes C ◽  
Fluorimetric Titration

By means of the method of fluorimetric titration it has been shown that mucidin does not affect the attachment of antimycin to membranes from anaerobically grown Paracoccus denitrificans. The fluorimetric titration with antimycin can be used in the determination of the amount of the cytochrome bc1 complex in the membrane. In cells inhibited with antimycin, the oxidation of cytochromes c was accompanied by the reduction of cytochrome b; in the presence of mucidin this effect did not take place. The results, which indicated a difference in binding sites, were interpreted in terms of the Q-cycle [Mitchell (1976) J. Theor. Biol. 62, 327-367; Trumpower (1981) Biochim. Biophys. Acta 639, 129-155]. Comparable sensitivity towards antimycin and mucidin was shown by other typical denitrifying bacteria: Pseudomonas stutzeri and Alcaligenes xylosoidans, subspecies denitrificans.

scholarly journals Respiratory chain supercomplexes associate with the cysteine desulfurase complex of the iron–sulfur cluster assembly machinery

2018 ◽  
Vol 29 (7) ◽  
pp. 776-785 ◽  
Author(s):  
Lena Böttinger ◽  
Christoph U. Mårtensson ◽  
Jiyao Song ◽  
Nicole Zufall ◽  
Nils Wiedemann ◽  
...  
Keyword(s):  
Respiratory Chain ◽  
Complex Iii ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Respiratory Chain Complexes ◽  
Cysteine Desulfurase ◽  
Complex Iv ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur ◽  
Chain Complexes

Mitochondria are the powerhouses of eukaryotic cells. The activity of the respiratory chain complexes generates a proton gradient across the inner membrane, which is used by the F1FO-ATP synthase to produce ATP for cellular metabolism. In baker’s yeast, Saccharomyces cerevisiae, the cytochrome bc1 complex (complex III) and cytochrome c oxidase (complex IV) associate in respiratory chain supercomplexes. Iron–sulfur clusters (ISC) form reactive centers of respiratory chain complexes. The assembly of ISC occurs in the mitochondrial matrix and is essential for cell viability. The cysteine desulfurase Nfs1 provides sulfur for ISC assembly and forms with partner proteins the ISC-biogenesis desulfurase complex (ISD complex). Here, we report an unexpected interaction of the active ISD complex with the cytochrome bc1 complex and cytochrome c oxidase. The individual deletion of complex III or complex IV blocks the association of the ISD complex with respiratory chain components. We conclude that the ISD complex binds selectively to respiratory chain supercomplexes. We propose that this molecular link contributes to coordination of iron–sulfur cluster formation with respiratory activity.

Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe-2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans

1998 ◽  
Vol 255 (1) ◽  
pp. 100-106 ◽  
Author(s):  
Thomas Schroter ◽  
Oliver M. Hatzfeld ◽  
Sabine Gemeinhardt ◽  
Marcus Korn ◽  
Thorsten Friedrich ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Mutational Analysis ◽  
Paracoccus Denitrificans ◽  
Cytochrome Bc1 ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex

scholarly journals Characterization of mutations in crucial residues around the Qo binding site of the cytochrome bc1 complex from Paracoccus denitrificans

FEBS Journal ◽  
2008 ◽  
Vol 275 (19) ◽  
pp. 4773-4785 ◽  
Author(s):  
Thomas Kleinschroth ◽  
Oliver Anderka ◽  
Michaela Ritter ◽  
Andreas Stocker ◽  
Thomas A. Link ◽  
...  
Keyword(s):  
Binding Site ◽  
Paracoccus Denitrificans ◽  
Cytochrome Bc1 ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex

scholarly journals The nature of the stimulation of the respiratory chain of rat liver mitochondria by glucagon pretreatment of animals

1982 ◽  
Vol 204 (1) ◽  
pp. 37-47 ◽  
Author(s):  
A P Halestrap
Keyword(s):  
Respiratory Chain ◽  
Electron Flow ◽  
Liver Mitochondria ◽  
Complex Iii ◽  
Secondary Site ◽  
Rat Liver Mitochondria ◽  
Succinate Oxidation ◽  
Q Cycle ◽  
Cytochromes C ◽  
Stimulation Of

1. Studies on the cytochrome spectra of liver mitochondria from control and glucagon-treated rats in State 4, State 3 and in the presence of uncoupler are reported. 2. The stimulation of electron flow between cytochromes c1 and c observed previously [Halestrap (1978) Biochem. J. 172, 399-405] was shown to be an artefact of Ca2+-induced swelling of mitochondria. 3. When precautions were taken to prevent such swelling, glucagon treatment was shown to enhance the reduction of cytochromes c, c1 and b558 in both State 3 and uncoupled conditions with either succinate or glutamate + malate as substrate. An increase in the reduction of cytochromes b562 and b566 was also seen in some, but not all, experiments. 4. In State 4 with succinate but not glutamate + malate as substrate, cytochromes c, c1, b558, b562 and b566 showed increased reduction. 5. Glucagon stimulated oxidation of duroquinol and palmitoylcarnitine by intact mitochondria and of NADH by disrupted mitochondria. 6. No effect of glucagon on succinate dehydrogenase activity or the temperature-dependence of succinate oxidation could be detected. 7. Glucagon enhanced the inhibition of the respiratory chain by colletotrichin, but not antimycin or 8-heptyl-4-hydroxyquinoline N-oxide. 8. These results are interpreted in terms of a primary stimulation by glucagon of the ‘Q cycle’ [Mitchell (1976) J. Theor. Biol. 62, 827-367] within Complex III (ubiquinol:cytochrome c oxidoreductase) and a secondary site of action involving stimulation of electron flow into Complex III from the ubiquinone pool. 9. Ageing of mitochondria, hyperosmotic treatment or addition of 20 mM-benzyl alcohol opposed the effects of glucagon treatment on cytochrome spectra and colletotrichin inhibition of respiration. 10. These results support the hypothesis that glucagon exerts its effects on the mitochondria by perturbing the membrane structure.

scholarly journals The cellular location and specificity of bacterial cytochrome c peroxidases

1990 ◽  
Vol 271 (3) ◽  
pp. 707-712 ◽  
Author(s):  
C F Goodhew ◽  
I B Wilson ◽  
D J Hunter ◽  
G W Pettigrew
Keyword(s):  
Cytochrome C ◽  
Paracoccus Denitrificans ◽  
Pseudomonas Stutzeri ◽  
Cytochrome C Peroxidase ◽  
Total Activity ◽  
Gram Negative Bacteria ◽  
Visible Absorption ◽  
Cellular Compartment ◽  
Cytochromes C ◽  
Mitochondrial Cytochromes

The locations of cytochrome c peroxidase and catalase activities in the two Gram-negative bacteria Pseudomonas stutzeri (N.C.I.B. 9721) and Paracoccus denitrificans (N.C.I.B. 8944) were investigated by the production of spheroplasts. In both species the cytochrome c peroxidase was predominantly periplasmic: 92% of total activity in Ps. stutzeri and 98% of nonmembrane-bound activity in Pa. denitrificans were found in this cellular compartment. In contrast, the catalase was mostly in the cytoplasmic fraction. Purification of the Pa. denitrificans cytochrome c peroxidase showed it to be the haem c-containing polypeptide of Mr 42,000 that has already been described by Bosma, Braster, Stouthamer & Van Versefeld [(1987) Eur. J. Biochem. 165, 665-670] but was not identified by them as a peroxidase. The visible-absorption spectra of the enzyme closely resemble those of cytochrome c peroxidase from Pseudomonas aeruginosa but the donor specificity is different, with the Pa. denitrificans enzyme preferring the basic mitochondrial cytochromes c to the acidic cytochromes c-551 and reacting well with the Pa. denitrificans cytochrome c-550.

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