scholarly journals The respiratory chain of a newly isolated Methylomonas Pl1

1977 ◽  
Vol 168 (2) ◽  
pp. 171-178 ◽  
Author(s):  
A K Drabikowska
Keyword(s):  
Respiratory Chain ◽  
Nadh Oxidase ◽  
Difference Spectra ◽  
Whole Cells ◽  
Cytochromes C ◽  
The Difference ◽  
Endogenous Substrates ◽  
Nadh Oxidase Activity ◽  
Electron Carriers ◽  
Aerobic And Anaerobic

1. Whole cells of Methylomonas Pl1 contained ubiquinone, identified as ubiquinone-8. No naphthaquinone was detected. Ubiquinone was located predominantly in the particulate fraction, which also contained most of the NADH oxidase activity. 2. Aerobic incubation of cells with formaldehyde or methanol resulted in about 20% reduction of ubiquinone, irrespective of the presence or absence of dinitrophenol. On inhibition of the respiration by cyanide, ubiquinone became partly reduced by endogenous substrates (15—25%), and a further reduction occurred only in the presence of formaldehyde (up to 60%). When endogenous substrates were completely exhausted, then 44 and 23% of ubiquinone was reduced by formaldehyde or methanol respectively. 3. The difference spectra at room and liquid-N2 temperatures revealed the presence of cytochrome b and two cytochromes c (c-552.5 and c-549) all tightly bound to the membrane. Cytochrome c-552.5 was also found in the soluble fraction. 4. Redox changes of cytochromes b and c, with methanol or formaldehyde as substrates, respond to the aerobic and anaerobic states of the cell and to KCN inhibition in a manner characteristic of the electron carriers of the respiratory chain. 5. The merging point for electron transport from NADH dehydrogenase and formaldehyde dehydrogenase is suggested to be at the level of ubiquinone.

The cytochrome system in Mycobacterium lepraemurium

1974 ◽  
Vol 20 (7) ◽  
pp. 943-947 ◽  
Author(s):  
M. Ishaque ◽  
Laszlo Kato
Keyword(s):  
Cytochrome C ◽  
Respiratory Chain ◽  
Cell Suspensions ◽  
Reduced Form ◽  
Difference Spectra ◽  
Whole Cell ◽  
Chain System ◽  
Cytochrome O ◽  
The Difference ◽  
Mycobacterium Lepraemurium

The respiratory chain system of cell suspensions of Mycobacterium lepraemurium was investigated spectrophotometrically. The results obtained indicated that whole cell preparations contained flavins, cytochromes of the a + a3 and b type, as well as two CO-binding pigments; cytochromes a3–CO and a second pigment similar to cytochrome o. The cytochromes were found to be in the reduced form. The presence of cytochrome systems could only be shown after the cell suspensions in the reference cuvette were exposed to oxygen. The positions of the peaks in the difference spectra were similar when the cell suspensions were reduced anaerobically without added substrate or treated with dithionite. The whole cell suspensions of M. lepraemurium were not found to contain detectable quantities of cytochrome c.

Effect of Near-Ultraviolet Light on the Respiratory Chain of Escherichia coli

1971 ◽  
Vol 49 (5) ◽  
pp. 492-495 ◽  
Author(s):  
P. D. Bragg
Keyword(s):  
Ultraviolet Light ◽  
Cytochrome B ◽  
Respiratory Chain ◽  
Nadh Oxidase ◽  
Reductase Activity ◽  
State Level ◽  
Progressive Increase ◽  
E Coli ◽  
Near Ultraviolet ◽  
Nadh Oxidase Activity

Irradiation of a particulate fraction from E. coli with near-ultraviolet light destroyed NADH oxidase activity. This treatment did not affect markedly the levels of cytochromes b1 and o, and ubiquinone in this preparation. Cytochrome a2 was destroyed by irradiation. A progressive increase in the aerobic steady state level of cytochrome b1 reduction during irradiation confirmed that irradiation affected the cytochrome oxidase region of the respiratory chain. There was a second site of inactivation between substrate and cytochrome b1. This was indicated by lowered NADH:cytochrome b1 reductase activity. Partial reactivation of this activity was obtained by addition of ubiqumone-2 but not ubiquinone-8.

scholarly journals The role of ubiquinone in the respiratory chain of Acetobacter xylinum

1968 ◽  
Vol 108 (2) ◽  
pp. 311-316 ◽  
Author(s):  
Moshe Benziman ◽  
H. Goldhamer
Keyword(s):  
Respiratory Chain ◽  
Nadh Oxidase ◽  
Coenzyme Q ◽  
Spectroscopic Properties ◽  
Acetobacter Xylinum ◽  
Whole Cells ◽  
Oxidation Reduction ◽  
The Individual ◽  
Ubiquinone 10

1. Whole cells of Acetobacter xylinum were found to contain a quinone of the ubiquinone (coenzyme Q) group. The quinone was isolated from the cells and crystallized. It was identified by its physical, chemical and spectroscopic properties as a ubiquinone with 10 isoprene units (ubiquinone-10). No naphthaquinone was detected in the cells. 2. Cell-free extracts prepared by means of a French pressure cell were separated into three fractions by differential centrifugation. The ubiquinone was located predominantly in the particulate fraction sedimenting at 33000g, which also contained most of the NADH oxidase and malate oxidase activities. The concentration of ubiquinone-10 in extracts was similar to that of the flavoproteins and about three times the concentration of the individual cytochromes. 3. Aerobic incubations of crude extracts with either NADH or malate resulted in reduction of the endogenous ubiquinone-10 to steady-state concentrations of 55 and 40% of the total quinone respectively. In the presence of cyanide more than 95% of the endogenous ubiquinone-10 was reduced by either NADH or malate. 4. The initial rate of reduction of endogenous ubiquinone-10 by malate and the rate of ubiquinol oxidation, in A. xylinum extracts, were found to be compatible with the overall rate of malate oxidation with oxygen. 5. The effects of various respiratory inhibitors on the oxidation–reduction reactions of the endogenous quinone indicate that its position on the respiratory chain is between the malate flavoprotein dehydrogenase and the cytochrome chain.

The interaction of bovine milk caseins with the detergent sodium dodecyl sulphate. II. The effect of detergent binding on spectral properties of caseins

1970 ◽  
Vol 37 (2) ◽  
pp. 259-267 ◽  
Author(s):  
G. C. Cheeseman ◽  
Dorothy J. Knight
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Bovine Milk ◽  
Difference Spectrum ◽  
Temperature Dependent ◽  
Difference Spectra ◽  
Negative Change ◽  
Tryptophan Residues ◽  
Hydrophobic Binding ◽  
The Difference

SummaryThe dissociation of casein aggregates by the detergent sodium dodecyl sulphate (SDS) gave rise to difference spectra and these spectra were characteristic for each of the different types of casein. Increase in absorption by the chromophore groups, tyrosine and tryptophan, when αs1- and β-casein aggregates were dissociated indicated binding of the detergent at regions of the molecule containing these residues. A decrease in absorption when κ-casein was dissociated indicated that the tyrosine and tryptophan residues were not in the region of the molecule to which the detergent was bound and that in the κ-casein aggregate these residues were in a more hydrophobic environment. Peaks on the difference spectra were obtained at 280 and 288 nm for αs1-casein and 284 and 291 nm for β-casein and troughs at 278 and 286 nm for κ-casein. The difference spectrum reached a maximum value when the αsl- and β-casein aggregates were dissociated and the further binding of SDS did not alter this value. The large negative change in the difference spectrum of κ-casein did not occur until after most of the aggregates were dissociated and did not reach a maximum until binding with SDS was complete. The value obtained for ΔOD was found to be temperature-dependent for β-casein-SDS interaction, but not for αs1- and κ-casein. Changes in spectra were also observed when αs1- and κ-casein interacted to form aggregates. The data obtained confirmed the importance of hydrophobic binding in casein aggregate formation and indicated the possible involvement of tyrosine and tryptophan residues in this binding.

scholarly journals Multiple light-induced reactions of cytochromes b and c in Rhodopseudomonas spheroides

1969 ◽  
Vol 114 (4) ◽  
pp. 793-799 ◽  
Author(s):  
O. T. G. Jones
Keyword(s):  
Cytochrome C ◽  
Cytochrome B ◽  
Photochemical Reaction ◽  
Room Temperature ◽  
Close Association ◽  
Antimycin A ◽  
Reaction Centre ◽  
Difference Spectra ◽  
Cytochromes C ◽  
Rhodopseudomonas Spheroides

Illumination of chromatophore preparations from Rhodopseudomonas spheroides causes the oxidation of a cytochrome c and a slight oxidation of a cytochrome b with a maximum at 560nm. When illuminated in the presence of antimycin A the oxidation of cytochrome c was more pronounced and cytochrome b560 was reduced; the dark oxidation of cytochrome b560 was biphasic in the presence of succinate, but not in the presence of NADH, a less effective reductant. Split-beam spectroscopy showed that, in addition to the reduction of cytochrome b560, another pigment with maxima at 565 and 537nm. was reduced and was more rapidly oxidized in the dark than cytochrome b560. This pigment, tentatively identified as cytochrome b565, was also detected in spectra at 77°k, after brief illumination at room temperature; the maxima at 77°k were at 562 and 536nm. In the absence of antimycin A, light caused a transient reduction of cytochrome b565 and an oxidation of cytochrome b560. Dark oxidation of b565 was rapid, even in the presence of antimycin A and succinate. Difference spectra, at 77°k, of ascorbate-reduced minus succinate-reduced chromatophores or of anaerobic succinate-reduced minus aerobic succinate-reduced chromatophores suggested that two cytochromes c were present, with maxima at 547 and 549nm. When chromatophores frozen at 77°k were illuminated both these cytochromes c were oxidized, indicating a close association with the photochemical reaction centre. A scheme involving two reaction centres is proposed to explain these results.

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