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Increasing Ethanol Tolerance in Industrially Important Ethanol Fermenting Organisms
Published in Ayerim Y. Hernández Almanza, Nagamani Balagurusamy, Héctor Ruiz Leza, Cristóbal N. Aguilar, Bioethanol, 2023
Kalyanasundaram Geetha Thanuja, Subburamu Karthikeyan
The iron-sulfur clusters (ISC) are the prosthetic groups responsible for catalytic and regulatory functions found in both prokaryotes and eukaryotes. The components of the mitochondrial ISC in S. cerevisiae were reported to be related in iron homeostasis due to ethanol tolerance and are encoded by the genes NFS1, ISU1, ISU2, ISA1, ISA2, JAC1, SSQ1, YAH1, GRX5, and IBA5. The over-expression of Jac 1p and Isu 1p in S. cerevisiae UMArn3 was evaluated and revealed their counteracting ability of metabolic unbalance caused by an increase in ROS generation [60]. Further Snf complex of S. cerevisiae, a member of AMP protein kinase family engages in a series of cellular functions and responds to environmental stresses. The effect of Snf over-expression revealed a 39% increase in cell survival rate over parental strain at 8% ethanol accompanied with altered expression of genes involved in glucose transport and accumulation of fatty acids [31].
Applications and challenges of elemental sulfur, nanosulfur, polymeric sulfur, sulfur composites, and plasmonic nanostructures
Published in Critical Reviews in Environmental Science and Technology, 2019
Yong Teng, Qixing Zhou, Peng Gao
Iron-sulfur proteins are found in all life forms, and iron-sulfur clusters as their cofactors, are the oldest and most versatile inorganic cofactors with the function of catalysis, electron transfer, and sensing of iron and oxygen of ambient conditions (Beinert, Holm, & Münck, 1997; Lill, 2009). Fe2S2, Fe3S4, and Fe4S4 clusters containing iron (Fe2+/3+) and sulfide (S2−), and other metal ions for more complex clusters, are the frequent types of iron-sulfur clusters, and they may be inserted or removed from proteins through oxidation-reduction reactions (Beinert et al., 1997). The synthesis and assembly into apoproteins in living cells is complex and a coordinated process and the summarized common biosynthetic rules are as follows (Lill, 2009): (1) the de novo assembly of an Fe-S cluster on a scaffold protein, (2) the transfer of the Fe-S cluster from the scaffold to target apoproteins and its subsequent assembly into the polypeptide chain (Figure 4) (Beinert et al., 1997; Lill, 2009).