Moscow State University

About: Moscow State University is a education organization based out in Moscow, Russia. It is known for research contribution in the topics: Catalysis & Laser. The organization has 66747 authors who have published 123358 publications receiving 1753995 citations. The organization is also known as: MSU & Lomonosov Moscow State University.

Mean mass-specific metabolic rates are strikingly similar across life's major domains: Evidence for life's metabolic optimum

Abstract: A fundamental but unanswered biological question asks how much energy, on average, Earth's different life forms spend per unit mass per unit time to remain alive. Here, using the largest database to date, for 3,006 species that includes most of the range of biological diversity on the planet-from bacteria to elephants, and algae to sapling trees-we show that metabolism displays a striking degree of homeostasis across all of life. We demonstrate that, despite the enormous biochemical, physiological, and ecological differences between the surveyed species that vary over 10(20)-fold in body mass, mean metabolic rates of major taxonomic groups displayed at physiological rest converge on a narrow range from 0.3 to 9 W kg(-1). This 30-fold variation among life's disparate forms represents a remarkably small range compared with the 4,000- to 65,000-fold difference between the mean metabolic rates of the smallest and largest organisms that would be observed if life as a whole conformed to universal quarter-power or third-power allometric scaling laws. The observed broad convergence on a narrow range of basal metabolic rates suggests that organismal designs that fit in this physiological window have been favored by natural selection across all of life's major kingdoms, and that this range might therefore be considered as optimal for living matter as a whole.

Programmed and altruistic ageing.

Abstract: Ageing is widely believed to be a non-adaptive process that results from a decline in the force of natural selection. However, recent studies in Saccharomyces cerevisiae are consistent with the existence of a programme of altruistic ageing and death. We suggest that the similarities between the molecular pathways that regulate ageing in yeast, worms, flies and mice, together with evidence that is consistent with programmed death in salmon and other organisms, raise the possibility that programmed ageing or death can also occur in higher eukaryotes.

Microwave assisted extraction of secondary metabolites from plants: Current status and future directions

Abstract: Plant secondary metabolites are known to be an important source of foods, fragrances, pigment, drugs and so on. Extraction is one of the crucial steps for research and development of plant secondary metabolites. Over the past 25 years, a large number of manuscripts of microwave assisted extraction have been published and lots of remarkable results have been achieved. However, there are still many theoretical and technical barriers in the area of microwave assisted extraction of plant secondary metabolites, which need to be overcome. This paper reviews recent advances in microwave assisted extraction of plant secondary metabolites, such as flavonoids, quinones, phenylpropanoids, terpenoids and alkaloids. Principles and mechanisms, apparatuses and equipment, advantages and disadvantages of microwave assisted extraction are also summarized. The last part of the paper introduces new and emerging technologies of microwave technique, and then suggests strategies for further research into microwave assisted extraction of plant secondary metabolites.

The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer

Abstract: The crystal structures of cytochrome c oxidase from both bovine and Paracoccus denitrificans reveal two putative proton input channels that connect the heme-copper center, where dioxygen is reduced, to the internal aqueous phase. In this work we have examined the role of these two channels, looking at the effects of site-directed mutations of residues observed in each of the channels of the cytochrome c oxidase from Rhodobacter sphaeroides. A photoelectric technique was used to monitor the time-resolved electrogenic proton transfer steps associated with the photo-induced reduction of the ferryl-oxo form of heme a3 (Fe4+ = O2−) to the oxidized form (Fe3+OH−). This redox step requires the delivery of a “chemical” H+ to protonate the reduced oxygen atom and is also coupled to proton pumping. It is found that mutations in the K channel (K362M and T359A) have virtually no effect on the ferryl-oxo-to-oxidized (F-to-Ox) transition, although steady-state turnover is severely limited. In contrast, electrogenic proton transfer at this step is strongly suppressed by mutations in the D channel. The results strongly suggest that the functional roles of the two channels are not the separate delivery of chemical or pumped protons, as proposed recently [Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. (1995) Nature (London) 376, 660–669]. The D channel is likely to be involved in the uptake of both “chemical” and “pumped” protons in the F-to-Ox transition, whereas the K channel is probably idle at this partial reaction and is likely to be used for loading the enzyme with protons at some earlier steps of the catalytic cycle. This conclusion agrees with different redox states of heme a3 in the K362M and E286Q mutants under aerobic steady-state turnover conditions.