Cytochrome Oxidase in Higher Plants

Bhagvat, K.; Hill, Robert D.

doi:10.1111/j.1469-8137.1951.tb05173.x

Cited by 49 publications

(12 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Such an interaction is demonstrated in figure 2 and table III. 2 indicates that exposure of the particles to distilled water for a limited time, whether at 00 or at room temperature, is in itself insufficient to cause inactivation of succinoxidase. In the presence of supernatant, however, inactivation is drastic and is much greater at the higher temperature.…”

Section: Methodsmentioning

confidence: 99%

“…Particles from various plant tissues have previously been prepared (2,6,28) which have exhibited both succinoxidase and cytochrome oxidase activity. By and large, these two systems are able to survive considerable manipulation, and it appears probable that the preparations described in the past have been suspensions of mitochondrial fragments similar to those studied by KEILIN (17).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The Physical Environment and Oxidative and Phosphorylative Capacities of Higher Plant Mitochondria

Laties

1953

Plant Physiol.

View full text Add to dashboard Cite

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Physical Environment and Oxidative and Phosphorylative Capacities of Higher Plant Mitochondria

Laties

1953

Plant Physiol.

View full text Add to dashboard Cite

“…In the last two years, the situation has greatly altered: the survey of Bhagvat and Hill (4), and the reports of Price and Thimann (32) on oat and pea seedlings and of Millerd (24) on potato tuber have shown that the earlier negative findings on succinic dehydrogenase were not justified, and have implied its general distribution in plants. Conn et al (8) have brought to light the enzyme causing simultaneous dehydrogenation and decarboxylation of malic acid and shown its wide distribution in plants; and most recently (20,25,26,38), great progress has been made in identifying plant systems corresponding to the animal cyclophorase.…”

mentioning

confidence: 99%

The Estimation of Dehydrogenases in Plant Tissue.

Price

Thimann

1954

Plant Physiol.

View full text Add to dashboard Cite

Although a great deal of information has been amassed concerning dehydrogenases in animal tissues, there was for a long time little evidence that certain of these important enzymes even existed in plants. Malic and citric dehydrogenases were reported in 1929 in cucumber seeds (41), but it was not until 1939 that succinic dehydrogenase was found, first in pollen by Okunuki (28,29) and then in certain other tissues (9,11,14). Nevertheless, the apparent absence or near-absence of succinic dehydrogenase in some tissues (2,3,6,14,42) as well as the occasional reports of the presence of individual enzymes (10,23,41,42) seemed to indicate that the dehydrogenases, at least those of the 4 carbon and 6 carbon acids, were distributed only sporadically. It was during this period that the tricarboxylic acid cycle of Krebs (19), embodying many of these dehydrogenases, was becoming accepted as the main pathway of respiration in animal tissues. Respiration studies in plants (1, 5) pointed in the same direction.In the last two years, the situation has greatly altered: the survey of Bhagvat and Hill (4), and the reports of Price and Thimann (32) on oat and pea seedlings and of Millerd (24) on potato tuber have shown that the earlier negative findings on succinic dehydrogenase were not justified, and have implied its general distribution in plants. Conn et al (8) have brought to light the enzyme causing simultaneous dehydrogenation and decarboxylation of malic acid and shown its wide distribution in plants; and most recently (20,25,26,38), great progress has been made in identifying plant systems corresponding to the animal cyclophorase.While the occurrence of the enzymes is thus no longer in doubt, their properties and their concentrations in plants remain little known. As to their properties, there is evidence that the methods of animal enzymology cannot always be employed unchanged in the study of plant dehydrogenases. For example, Laties (21) has discussed the special osmotic requirements of enzymatic particles from cauliflower, and our own studies (32) showed that the succinic dehydrogenase of oat coleoptiles is not only highly labile but 1 Received

show abstract

“…However, there s!til,l exists some confusion in the literatuire about the number and the identity of the cytoohromes that are generaIlly found in higher plant mitochondria. Thtis, in 1951, Bha.gvat and Hill (5), extending the work of Keilin (33), found that the resspiratory chain in the mittochondria o,f a nuimber of plant materials wa's simi,lar to t'hat of animal tissues and consisted of cytochrome oxi'dase, cytochrome b, and cytochrome c. Later, Martin and Morton (41), and Wiskich, Morton, and Martin (50) found that the respiratory clhain of plant mitochondria consisted of cytochromes b, cl, c, a, and a3. To this sequience, Lundegardh has added cytochrome b3 (38,39,40), a soluble cytochrome first described by HiIll and Scarisbrick (29).…”

mentioning

confidence: 99%

The Respiratory Chain Components of Higher Plant Mitochondria

1968

View full text Add to dashboard Cite

Abstract. Tightly coupled mitochondria have been prepared from a variety of plant sources: white potato (Solanum tuberosum), Jerusalem artichoke (Heliantus tuberosus), cauliflower buds (Brassica oleracea), and mung bean hypocotyls (Phaseolus aureus). Mitochondria with no appreciable coupling were also prepared from skunk cabbage spadices (Symplocarpus foetidus).Room temperature difference spectra show that these mitochondria are very similar in the qualitative and quantitative composition of their electron carriers. The For all kinds of mitochondria, the rates of oxidation of succinate are similar as well as the turnover of cytochrome oxidase sec'1), regardless of the metabolic activities of the tissues. The number of mitochondria per cell appears to be the controlling factor of the intensity of tissue respiration.Higher plant tilssues are characterized by a grea'ter number of components in the mitochondrial respiratory chain than i,s the case wi'th animal tissues (6,7,37,44 (20). However, necessary adjustments had to be made to take into account the fact that the absorption peaks of plant electron carriers are not always the same as those of simitlar carriers of animail mi;tochondria.The identifi'cation of the various cytochromes present in plant mitochondria was best performed at liquid nitrogen temperature (77°K). The oxidized and reduced samples were placed in a 3 mm light path cuvette and cooled in a Dewar flask filled with liquid nitrogen during the scanning of the spectrum (6, 21). Low temperature brings a higher resolution as wdlHl as an enhancement of the absorption peak. By scanning the same sample, first at room temperature and then at low temperature, it is possible to measure the magnitude of the low temperature en'hancement and, by using the same extinction coefficients as before (20) Figure 1 shows a series of room tempera,ture difference spectra obtained with Jerusa,lem artichoke mitoohondria. The tipper spectrum shows a clear identification of the cytochromes after reduotion by dithionite. The a!bsorption peak of cytochrome oxidase (cytochrome a + cytoohrome a3) is located at 602 mju, a few mjm closer to the blue region of the spectrum than cytoc-hrome oxidase from animal mitochondria whose a-band is generally found at 605 mu (52). T.he a-band

show abstract

Cytochrome Oxidase in Higher Plants

Cited by 49 publications

References 18 publications

The Physical Environment and Oxidative and Phosphorylative Capacities of Higher Plant Mitochondria

The Physical Environment and Oxidative and Phosphorylative Capacities of Higher Plant Mitochondria

The Estimation of Dehydrogenases in Plant Tissue.

The Respiratory Chain Components of Higher Plant Mitochondria

Contact Info

Product

Resources

About