PubMed · 4065962
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D Henschler. 1985. Specific covalent binding and genotoxicity.. https://pubmed.ncbi.nlm.nih.gov/4065962/
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Haloarchaea with the capacity to degrade alkanes is promising to deal with petroleum pollution in hypersaline environments. However, only a limited number of haloarchaeal species are investigated, and their pathway and mechanism for alkane degradation remain unclear. In this study, Halogranum rubrum RO2-11, a haloarchaeal strain, verified the ability to degrade kerosene and hexadecane in 184 g/L NaCl, with 53% and 52% degradation rates after 9 and 4 days, respectively. Genome sequencing and gene annotation indicated that strain RO2-11 possesses a complete potential alkane-degrading pathway, of which alkane hydroxylases may include CYP450, AlmA, and LadA. Transcriptome and metabolome analyses revealed that the upregulation of related genes in TCA cycle, lysine biosynthesis, and acetylation may help improve hexadecane degradation. Additionally, an alternative degrading pathway of hexadecane based on dual-terminal β-oxidation may occur in strain RO2-11. It is likely to be the first report of alkane degradation by the genus Halogranum, which may be helpful for applications of oil-pollution bioremediation under high-salt conditions.
When the thickness of monolayer membranes formed by bolaform archaeal lipids is reduced to the approximate length of two valinomycin molecules, the zero-current conductance does not show any more a linear dependence on valinomycin concentration; instead, a quadratic behaviour is observed. This suggests that a dimer permeation pore is formed and therefore the conduction mechanism changes from carrier to channel.
The n-alkane-assimilating yeast Candida maltosa contains several structurally related cytochromes P450 (P450) encoded by the CYP52 multigene family, which are inducible by various long-chain hydrocarbons and fatty acids and which are responsible for the initial hydroxylation steps in the metabolism of these substrates. In the present work, the four major n-alkane-inducible C. maltosa P450 forms; CYP52A3, CYP52A4, CYP52A5, and CYP52A9, were enzymatically characterized, taking advantage of heterologous P450/reductase coexpression in Saccharomyces cerevisiae. Testing various alkanes and fatty acids, distinct preferences of the individual P450 forms concerning substrate class and chain length were detected, thus providing new insight into the functional diversity of the C. maltosa CYP52 family. Moreover, the results obtained emphasize these structurally related enzymes as a powerful tool for future studies on P450 structure-function relationships.