scholarly journals Electron-paramagnetic-resonance spectroscopy studies of iron-sulphur centres of submitochondrial particles from iron- and sulphur-deficient. Candida utilis

1975 ◽  
Vol 146 (1) ◽  
pp. 239-246 ◽  
Author(s):  
T A Gray ◽  
P B Garland ◽  
D J Lowe ◽  
R C Bray

1. Measurements were made at 12 degrees K of the electron-paramagnetic-resonance (e.p.r.) spectra of submitochondrial particles from Candida utilis cells grown under conditions that alter the amount of the mitochondrial NADH dehydrogenase (EC 1.6.99.3). 2. Iron-limited growth decreases the extent of iron-sulphur e.p.r. signals to undetectable values that are less than 1 percent of those normally found with glycerol-limited growth. 3. Small but significant signals attributable to the NADH dehydrogenase were detected in submitochondrial particles from sulphate-limited cells. 4. Measurements made on submitochondrial particles prepared from these and other phenotypically modified cells lead us to conclude that the presence of low-temperature e.p.r.-detectable iron-sulphur centres attributable to the NADH dehydrogenase are necessary but not sufficient for the coupling of ATP synthesis to the NADH dehydrogenase reaction in the mitochondrial membrane of C. utilis. 6. The amplitude of the g=2.01 signal observed in non-reduced submitochondrial particles is approximately tenfold diminished by iron limitation but not significantly altered by sulphate limitation.

1973 ◽  
Vol 134 (4) ◽  
pp. 1051-1061 ◽  
Author(s):  
J. A. Downie ◽  
P. B. Garland

1. During copper-limited growth of Candida utilis in continuous culture on a non-fermentable carbon and energy source there is a selective pressure favouring the emergence of variants that are less dependent on copper. 2. We describe the properties of such a variant that by-passes cytochrome oxidase (EC 1.9.3.1) by utilizing an alternative oxidase communicating with the respiratory chain at about the level of cytochrome b. 3. Both direct studies of isolated mitochondria and calculations based on growth parameters showed that only one of the normal three phosphorylation sites was active. This site was localized between NADH and the cytochromes. 4. Growth of the variant with copper-supplemented media resulted in the return of cytochrome oxidase but not the loss of the alternative oxidase. 5. The alternative oxidase is inhibited by substituted benzhydroxamic acids. 6. Submitochondrial particles from the variant did not exhibit any novel electron-paramagnetic-resonance-spectroscopy features at about g=2.0 either at 80°K or 12°K.


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