China
Africa
Explore chapters and articles related to this topic
Ferrihemoglobin in Normal Blood
Published in Manfred Kiese, Methemoglobinemia: A Comprehensive Treatise, 2019
Hayashi et al.2419 devised an enzyme system which reduces ferrihemoglobin and ferrimyoglobin and keeps them in the ferrous state during studies of oxygen equilibria. The system consists of NADPH generating system, ferredoxin, ferredoxin-NADP reductase, and catalase.
A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity
Published in Nanotoxicology, 2023
Lidija Izrael Živković, Nico Hüttmann, Vanessa Susevski, Ana Medić, Vladimir Beškoski, Maxim V. Berezovski, Zoran Minić, Ljiljana Živković, Ivanka Karadžić
The downregulation of glutathione (GSH)-related enzymes (glutathione peroxidase and hydrolase), (Table 1) and unaltered levels of glutathione reductase (Supplementary Table 1) is intriguing, since disturbed redox homeostasis usually increases the amount of glutathione and related enzymes in the cell. The reduction potentials of pyocyanin and GSH point out their direct reaction, as well as the reaction between GSH and ROS induced by pyocyanin, both depleting intracellular GSH levels. This is only partially reimbursed by glutathione reductase, leaving cells deficient in GSH and more sensitive to redox stress (Das et al. 2017). Interestingly, the downregulation of polyhydroxyalkanoate synthesis protein, PhaF, was found. This enzyme can cause lowered synthesis of polyhydroxyalkanoates, which function as a reducing equivalent pool to maintain cellular redox balance (Ayub, Tribelli, and Lopez 2009). The lack of polyhydroxylalkanoate implies altered redox homeostasis and fatty acid biosynthesis, as found in this study. Upregulation of flavoprotein pyridine nucleotide transhydrogenase, responsible for the conversion of NADPH to NADH, and ferredoxin-NADP reductase (Table 1), was observed, aligning with enhanced superoxide radical production.