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The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group. They are widely distributed in many organisms.
"Aquifex aeolicus" is a chemolithoautotrophic, Gram-negative, motile, hyperthermophilic bacterium. "A. aeolicus" is generally rod-shaped with an approximate length of 2.0-6.0μm and a diameter of 0.4-0.5μm. "A. aeolicus" is neither validly nor effectively published and, having no standing in nomenclature, should be styled in quotation marks. It is one of a handful of species in the Aquificae phylum, an unusual group of thermophilic bacteria that are thought to be some of the oldest species of bacteria, related to filamentous bacteria first observed at the turn of the century. "A. aeolicus" is also believed to be one of the earliest diverging species of thermophilic bacteria. "A. aeolicus" grows best in water between 85 °C and 95 °C, and can be found near underwater volcanoes or hot springs. It requires oxygen to survive but has been found to grow optimally under microaerophilic conditions. Due to its high stability against high temperature and lack of oxygen, "A. aeolicus" is a good candidate for biotechnological applications as it is believed to have potential to be used as hydrogenases in an attractive H2/O2 biofuel cell, replacing chemical catalysts. This can be useful for improving industrial processes.
The bacterium, despite its simplicity, contains a well-developed cell structure which is responsible for some of its unique biological structures and pathogenicity. Many structural features are unique to bacteria and are not found among archaea or eukaryotes. Because of the simplicity of bacteria relative to larger organisms and the ease with which they can be manipulated experimentally, the cell structure of bacteria has been well studied, revealing many biochemical principles that have been subsequently applied to other organisms.
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In taxonomy, Natrialba is a genus of the Halobacteriaceae. The genus consists of many diverse species that can survive extreme environmental niches, especially they are capable to live in the waters saturated or nearly saturated with salt (halophiles). They have certain adaptations to live within their salty environments. For example, their cellular machinery is adapted to high salt concentrations by having charged amino acids on their surfaces, allowing the cell to keep its water molecules around these components. The osmotic pressure and these amino acids help to control the amount of salt within the cell.
Rhodobacter sphaeroides is a kind of purple bacterium; a group of bacteria that can obtain energy through photosynthesis. Its best growth conditions are anaerobic phototrophy and aerobic chemoheterotrophy in the absence of light. R. sphaeroides is also able to fix nitrogen. It is remarkably metabolically diverse, as it is able to grow heterotrophically via fermentation and aerobic and anaerobic respiration. Such a metabolic versatility has motivated the investigation of R. sphaeroides as microbial cell factory for biotechnological applications.
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Bacterial glutathione transferases are part of a superfamily of enzymes that play a crucial role in cellular detoxification. The primary role of GSTs is to catalyze the conjugation of glutathione (GSH) with the electrophilic centers of a wide variety of molecules. The most commonly known substrates of GSTs are xenobiotic synthetic chemicals. There are also classes of GSTs that utilize glutathione as a cofactor rather than a substrate. Often these GSTs are involved in reduction of reactive oxidative species toxic to the bacterium. Conjugation with glutathione receptors reders toxic substances more soluble, and therefore more readily exocytosed from the cell.
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Benjamin "Ben" C. Stark is an American biologist and a professor at the Illinois Institute of Technology. He grew up in a small city in mid-Michigan in the 1950s-1960s. After high school he majored in cellular biology at the University of Michigan and later he received his master and doctoral degrees from Yale University with Sidney Altman. After two postdoctoral positions, he took a faculty position at Illinois Institute of Technology, where he has worked since. He has carried out research in the area of genetic engineering and RNA biology.
Rhodoferax is a genus of Betaproteobacteria belonging to the purple nonsulfur bacteriarophic. Originally, Rhodoferax species were included in the genus Rhodocyclus as the Rhodocyclus gelatinous-like group. The genus Rhodoferax was first proposed in 1991 to accommodate the taxonomic and phylogenetic discrepancies arising from its inclusion in the genus Rhodocyclus. Rhodoferax currently comprises four described species: R. fermentans, R. antarcticus, R. ferrireducens, and R. saidenbachensis. R. ferrireducens, lacks the typical phototrophic character common to two other Rhodoferax species. This difference has led researchers to propose the creation of a new genus, Albidoferax, to accommodate this divergent species. The genus name was later corrected to Albidiferax. Based on geno- and phenotypical characteristics, A. ferrireducens was reclassified in the genus Rhodoferax in 2014. R. saidenbachensis, a second non-phototrophic species of the genus Rhodoferax was described by Kaden et al. in 2014.
References
- ↑ Skerman VBD, McGowan V, Sneath PHA, eds. (1989). Approved Lists of Bacterial Names (Amended). Washington, DC: ASM Press. ISBN 978-1-55581-014-6. PMID 20806452.
- 1 2 Stark BC, Dikshit KL, Pagilla KR (2011). "Recent advances in understanding the structure, function, and biotechnological usefulness of the hemoglobin from the bacterium Vitreoscilla". Biotechnol Lett. 33 (9): 1705–1714. doi:10.1007/s10529-011-0621-9. PMID 21603987.
- ↑ Euzéby JP. "List of Prokaryotic names with Standing in Nomenclature - Genus Vitreoscilla". LPSN . Retrieved 2013-05-31.
- ↑ Costerton JW, Murray RG, Robinow CF (1961). "Observations on the motility and the structure of Vitreoscilla". Can J Microbiol. 7: 329–339. doi:10.1139/m61-040. PMID 13695850.
- ↑ Fackrell H (1998). "Vitreoscilla". uwindsor.ca. University of Windsor. Retrieved 2013-06-19.
- ↑ Stark BC, Dikshit KL, Pagilla KR (2012). "The Biochemistry of Vitreoscilla hemoglobin". Computational and Structural Biotechnology Journal. 3 (4): e201210002. doi:10.5936/csbj.201210002. PMC 3962134 .
- ↑ Yu H, Shen Z (1999). "Progress in research of Vitreoscilla hemoglobin and Vitreoscilla hemoglobin gene". Wei Sheng Wu Xue Bao. 39 (5): 478–482. PMID 12555532.
- ↑ Isarankura-Na-Ayudhya C, Panpumthong P, Tangkosakul T, Boonpangrak S, Prachayasittikul V (2008). "Shedding light on the role of Vitreoscilla hemoglobin on cellular catabolic regulation by proteomic analysis". Int J Biol Sci. 4 (2): 71–82. doi:10.7150/ijbs.4.71. PMC 2267286 . PMID 18345284.
