• Molecules and Cells
• /
• v.39 no.1
• /
• pp.6-19
• /
• 2016

Redox signalling comprises the biology of molecular signal transduction mediated by reactive oxygen (or nitrogen) species. By specific and reversible oxidation of redoxsensitive cysteines, many biological processes sense and respond to signals from the intracellular redox environment. Redox signals are therefore important regulators of cellular homeostasis. Recently, it has become apparent that the cellular redox state oscillates in vivo and in vitro, with a period of about one day (circadian). Circadian timekeeping allows cells and organisms to adapt their biology to resonate with the 24-hour cycle of day/night. The importance of this innate biological timekeeping is illustrated by the association of clock disruption with the early onset of several diseases (e.g. type II diabetes, stroke and several forms of cancer). Circadian regulation of cellular redox balance suggests potentially two distinct roles for redox signalling in relation to the cellular clock: one where it is regulated by the clock, and one where it regulates the clock. Here, we introduce the concepts of redox signalling and cellular timekeeping, and then critically appraise the evidence for the reciprocal regulation between cellular redox state and the circadian clock. We conclude there is a substantial body of evidence supporting circadian regulation of cellular redox state, but that it would be premature to conclude that the converse is also true. We therefore propose some approaches that might yield more insight into redox control of cellular timekeeping.

• Microbiology and Biotechnology Letters
• /
• v.26 no.2
• /
• pp.167-172
• /
• 1998

In batch cultures of Brevibacterium ketoglutamicum for the L-ornithine production in which the pH and dissolved oxygen concentration were regulated constant, the profiles of redox potential were observed in parallel with the profiles of state variables such as cell, glucose, and ornithine concentrations. It was found that the redox potential had a close relationship with cell concentration and was also affected by ornithine concentration. The effects of ornithine and glucose on redox potential were examined in a separate series of experiments. Based on the experimental results, a correlation of redox potential to glucose, cell and ornithine concentrations has been proposed. The proposed correlation can be used for on-line estimation of ornithine concentration from on-line data of redox potential, glucose concentration, and cell concentration.

• Environmental Sciences Bulletin of The Korean Environmental Sciences Society
• /
• v.10 no.S_2
• /
• pp.65-71
• /
• 2001

The chemical behavior and properties related to the redox state of environmental pollutants were investigated using electrochemical methods. Measurements were taken of variations in the redox potential and cyclic polarization current. The results established the influence of various factors, including concentration, temperature, salt, and pH, on the redox potential and current. These factors were determined to effect the result of the redox reaction. Optimum conditions were also established for each case. It was clearly established that the electrode reaction was from a reversible to an irreversible process, plus it was also mixing reaction current controlled.

• Journal of Life Science
• /
• v.19 no.7
• /
• pp.852-858
• /
• 2009

The homeostasis of the pyridine nucleotide pool [NAD(P)H and NAD(P)$^+$] is maintained in Rhodobacter sphaeroides mutant strains defective in the cytochrome bci complex or the cytochrome c oxidases in terms of its concentration and redox state. Aerobic derepression of the puf operon, which is under the control of the PrrBA two-component system, in the CBB3 mutant strain of R. sphaeroides was shown to be not the result of changes in the redox state of the pyridine nucleotides and the ubiquinone/ubiquinol pool. Using the bc$_1$ complex knock-out mutant strain of R. sphaeroides, we clearly demonstrated that the inhibitory effect of cbb$_3$, oxidase on spectral complex formation is not caused indirectly by the redox change of the ubiquinone/ubiquinol pool.

• BMB Reports
• /
• v.48 no.4
• /
• pp.200-208
• /
• 2015

The field of redox proteomics focuses to a large extent on analyzing cysteine oxidation in proteins under different experimental conditions and states of diseases. The identification and localization of oxidized cysteines within the cellular milieu is critical for understanding the redox regulation of proteins under physiological and pathophysiological conditions, and it will in turn provide important information that are potentially useful for the development of novel strategies in the treatment and prevention of diseases associated with oxidative stress. Antioxidant enzymes that catalyze oxidation/reduction processes are able to serve as redox biomarkers in various human diseases, and they are key regulators controlling the redox state of functional proteins. Redox regulators with antioxidant properties related to active mediators, cellular organelles, and the surrounding environments are all connected within a network and are involved in diseases related to redox imbalance including cancer, ischemia/reperfusion injury, neurodegenerative diseases, as well as normal aging. In this review, we will briefly look at the selected aspects of oxidative thiol modification in antioxidant enzymes and thiol oxidation in proteins affected by redox control of antioxidant enzymes and their relation to disease. [BMB Reports 2015; 48(4): 200-208]

• Journal of the Korean Ceramic Society
• /
• v.52 no.2
• /
• pp.83-91
• /
• 2015

The redox reaction $M^{(x+n)+}+\frac{n}{2}O^{-2}{\rightleftarrows}M^{x+}+\frac{n}{4}O_2$ of multivalent ions in glass melts influences the melting process and final properties of the glass including the fining (removal of bubbles), infrared absorption and homogenization of melts, reaction between metal electrodes and melts or refractory and melts, and transmission and color of glass. In this review paper, the redox behaviors that occur frequently in the glass production process are introduced and the square wave voltammetry (SWV) is described in detail as an in situ method of examining the redox behavior of multivalent ions in the melt state. Finally, some voltammetry results for LCD glass melts are reviewed from the practical viewpoint of SWV.

• Proceedings of the Korean Society of Applied Pharmacology
• /
• 1995.10a
• /
• pp.125-132
• /
• 1995

In neurons, nitric oxide(NO) is produced by neuronal nitric oxide synthase following stimulation of N-methyl-D-aspartate(NMDA) receptors and the subsequent influx of Ca$\^$2+/. NO, induced in this manner, reportedly plays critical roles in neuronal plasticity, including neurite outgrowth, synaptic transmission, and long-term potentiation(LTP) (1-7). However, excessive activation of NMDA receptors has also been shown to be associated with various neurological disorders, including focal ischemia, epilepsy, trauma, neuropathic pain and chronic neurodegenerative maladies, such as Parkinson's disease, Hungtington's disease and amyotrophic lateral sclerosis(8). The paradox that nitric oxide(NO) has both neuroprotective and neurodestructive effects may be explained, at least in part, by the finding that NO effects on neurons are dependent on the redox state. This claim may be supported by the recent finding that tissue concentrations of cysteine approach 700 ${\mu}$M in settings of cerebral ischemia (9), levels of thiol that is expected to influence both the redox state of the system and the NO group itself(10).

• Membrane Journal
• /
• v.19 no.2
• /
• pp.129-135
• /
• 2009

The cation exchange membrane using the block co-polymer of polysulfone and polyphenylenesulfidesulfone was prepared for a separator of all-vanadium redox flow battery. The membrane property of the prepared cation exchange membrane was measured. The thermal stability of the prepared cation exchange analyzed by TG showed a more stable than that of Nafion117. The lowest measured membrane resistance, equilibrated in 1mol/L $H_2SO_4$ aqueous solution, $0.96{\cdot}cm^2$ at 3 cc of CSA (chlorosulfuricacid) which was introduction agent of ion exchange group. Electrochemical property of all-vanadium redox flow battery using the prepared cation exchange membrane was measured. Electromotive force in 100% of state of charge was 1.4 V which was that of all-vanadium redox flow battery, and cell resistance in charge and discharge at each state of charge had a low value compared with that of all-vanadium redox flow battery using Nafion117.

• Bulletin of the Korean Chemical Society
• /
• v.21 no.4
• /
• pp.412-418
• /
• 2000

Association of cytochrome c with anionic membranes involved both electrostatic and hydrophobic interactions and their relative contributions depended on the physical state of the membrane and the redox state of cyto-chromec.Hydrophobic interaction was favored by the membranes in gel phase, by the membranes with a large curvature, and by the membranes with a high surface charge density. Ferrocytochrome c was less dissociable by NaCl than ferricytochrome c suggesting that a lower protein stability is beneficial for hydrophobic interac-tion.Hydrophobic interaction induced larger structural perturbations on cytochrome c as monitored by the loss of the Fe-Met bond and by the increase in the distance between heme and Trp-59. When bound to anionic mem-branes,spin-labeled cytochrome c showed an electron paramagnetic resonance spectrum with two or more components, providing a direct evidence for multiple conformations of bound cytochrome c.

• Journal of Microbiology
• /
• v.39 no.3
• /
• pp.149-153
• /
• 2001

The electron transfer reaction is one of the most essential processes of life. Not only does it provide the means of transforming solar and chemical energy into a utilizable form for all living organisms, it also extends into a range of metabolic processes that support the life of a cell. Thus, it is of great interest to understand the physical basis of the rates and reduction potentials of these reactions. To identify the major determinants of reduction potentials in redox proteins, we have chosen the simplest electron transfer protein, rubredoxin, a small (52-54 residue) iron-sulfur protein family, widely distributed in bacteria and archaea. Rubredoxins can be grouped into two classes based on the correlation of their reduction potentials with the identity of residue 44; those with Ala44 (ex: Pyrococcus furiosus) have reduction potentials that are ∼50 mV higher than those with Va144 (ex: Clostridium pasteurianum). Based on the crystal structures of rubredoxins from C. pasteurianum and P. furiosus, we propose the identity of residue 44 alone determines the reduction potential by the orientation of the electric dipole moment of the peptide bond between 43 and 44. Based on 1.5 $\AA$ resolution crystal structures and molecular dynamics simulations of oxidized and reduced rubredoxins from C. pasteurianum, the structural rearrangements upon reduction suggest specific mechanisms by which electron transfer reactions of rubredoxin should be facilitated.