Redox Forms Research Articles

Protonated paramagnetic redox forms of di-o-quinone bridged with p-phenylene-extended TTF: A EPR spectroscopy study.

The chemical oxidation and reduction processes of deprotonated, direduced o-quinone-exTTF-o-quinone in protic solvents were studied by EPR spectroscopy. The formation of relatively stable paramagnetic protonated redox forms of the parent triad was very surprising. The character of spin-density distribution in the semiquinone–quinone and semiquinone–catechol redox forms indicates that the p-phenylene-extended tetrathiafulvalene connector provides a quite effective electronic communication channel between dioxolene coordination sites. It was found that the deprotonated, direduced o-quinone-exTTF-o-quinone is capable to reduction of the metal copper in solution. The radical anion species formed in this reaction exists in solution as a solvent-separated ion pair with a copper cation. A character of spin-density distribution in a radical anion species leads to the conclusion that the ligand corresponds to type III of the Robin–Day classification.

Effect of freezing prior to aging on myoglobin redox forms and CIE color of beef from Nellore and Aberdeen Angus cattle

The objective of this study was to evaluate the effect of freezing prior to wet aging on the color of Nellore and Aberdeen Angus cattle meat. Samples of the Longissimus thoracis muscle were subjected to two treatments: conventional aging (0, 7, 14 and 21days); and freezing (−20°C for 40days) followed by thawing and aging. Freezing promoted (P<0.05) formation of metmyoglobin during aging, especially in Nellore beef. Frozen meats showed (P<0.05) lower lightness (L*) values and higher redness (a*), chroma (C*) and hue angle (h*) values at the first day of storage, deteriorating quickly with aging time. The color of the Nellore meat was less (P<0.05) stable to freezing, being lighter, yellower and less red than Angus meat. The results suggest that color stability in vacuum-packed beef is reduced by freezing prior to aging and that reduction depends on the animal breed.

Bioaccumulation and subcellular partitioning of Cr(III) and Cr(VI) in the freshwater green alga Chlamydomonas reinhardtii

Chromium occurs in aquatic environments under two main redox forms, namely Cr(III) and Cr(VI), with different geochemical and biochemical properties. Cr(VI) readily crosses biological membranes of living organisms and once inside the cells it undergoes a rapid reduction to Cr(III). The route of entry for the latter form is, however, poorly known. Using the radioactive tracer 51Cr we compared the accumulation (absorption and adsorption) of the two Cr forms by the green unicellular alga Chlamydomonas reinhardii after 1h and 72h of exposure to 100nM of either Cr(III) or Cr(VI) at pH 7. Both Cr forms had similar accumulation, with a major part in the extracellular (adsorbed) fraction after 1h and a major part of total accumulated Cr in the intracellular (absorbed) fraction after 72h. We also investigated the intracellular partitioning of Cr using an operational fractionation scheme and found that both Cr forms had similar distributions among fractions: Cr was mostly associated with organelles (23±12% after 1h and 37±7% after 72h) and cytosolic heat-stable proteins and peptides (39±18% after 1h and 35±3% after 72h) fractions. Further investigations using a metallomic approach (SEC-ICP-MS) were performed with the heat-stable proteins and peptides fraction to compare the distribution of the two Cr forms among various biomolecules of this fraction. One Cr-binding biomolecule (∼28kDa) appeared after 1h of exposure for both Cr species. After 72h another biomolecule of lower molecular weight (∼0.7kDa) was involved in binding Cr and higher signal intensities were observed for Cr(VI) than for Cr(III). We show, for the first time, that both Cr(III) and Cr(VI) have similar fate within algal cells, supporting the tenet that a unique redox form occurs within cells.

Changes in Thiol-Disulfide Homeostasis of the Body to Surgical Trauma in Laparoscopic Cholecystectomy Patients.

We aimed to investigate the short-term effect of laparoscopic surgery on serum thiol-disulfide homeostasis levels as a marker of oxidant stress of surgical trauma in elective laparoscopic cholecystectomy patients. Venous blood samples were collected, and levels of native thiols, total thiols, and disulfides were determined with a novel automated assay. Total antioxidant capacity (measured as the ferric-reducing ability of plasma) and serum ischemia modified albumin, expressed as absorbance units assayed by the albumin cobalt binding test, were determined. The major findings of the present study were that native thiol (283 ± 45 versus 241 ± 61 μmol/L), total thiol (313 ± 49 versus 263 ± 67 μmol/L), and disulfide (14.9 ± 4.6 versus 11.0 ± 6.1 μmol/L) levels were decreased significantly during operation and although they increased, they did not return to preoperation levels 24 hours after laparoscopic surgery compared to the levels at baseline. Disulfide/native thiol and disulfide/total thiol levels did not change during laparoscopic surgery. The decrease in plasma level of native and total thiol groups suggests impairment of the antioxidant capacity of plasma; however, the delicate balance between the different redox forms of thiols was maintained during surgery.

Posttranslational forms of beta 2-glycoprotein I in the pathogenesis of the antiphospholipid syndrome.

The antiphospholipid syndrome (APS) is an autoimmune disease characterised by a procoagulant state that predisposes to recurrent thrombosis and miscarriages. Two major discoveries have advanced our understanding of the underlying complex pathogenesis of the APS. The first was the discovery that beta-2 glycoprotein-1 (β2GPI) is the major auto antigen in APS. The second was the discovery in more recent years that β2GPI contains allosteric disulphide bonds susceptible to posttranslational modification that may be involved in the development of autoantibodies in APS. The main allosteric disulphide bond in the fifth domain of β2GPI can exist in two redox states: free thiol or oxidised. It is the conformational transformation of β2GPI from its free thiol form to its more immunogenic oxidised form that exposes neo-epitopes on the first and fifth domains. The purpose of this review is to highlight the recent findings on the posttranslational forms of β2GPI in the pathogenesis of APS. We suggest that novel assays quantitating the different redox forms of β2GPI in plasma or serum may be used to supplement existing clinical and laboratory assays to more accurately stratify risk of thrombosis or miscarriage in APS patients.

Effects of protein phosphorylation on color stability of ground meat.

The influence of protein phosphorylation on meat color stability was investigated in this study. Phosphatase and protein kinase inhibitors were added to minced ovine Longissimus thoracis et lumborum (LTL) muscle to manipulate the global phosphorylation of sarcoplasmic proteins. The data obtained show that the rate and extent of pH decline, along with lactate accumulation in postmortem muscle, were related to protein phosphorylation. Analysis of meat color and the relative content of myoglobin redox forms revealed that meat color stability was inversely related to the phosphorylation of sarcoplasmic proteins. Thus, this study suggests that protein phosphorylation may be involved in meat color development by regulating glycolysis and the redox stability of myoglobin.

Ds-HMGB1 and fr-HMGB induce depressive behavior through neuroinflammation in contrast to nonoxid-HMGB1

High mobility group box 1 (HMGB1) has been implicated as a key factor in several neuroinflammatory conditions. Our previous study suggested that the release of central HMGB1 acts as a late-phase mediator in lipopolysaccharide (LPS)-induced depression. Recent findings indicate that the redox state of HMGB1 is a critical determinant of its immunomodulatory properties. Here, we aimed to investigate the potential mechanisms that link the redox states of HMGB1 to depression in mice. Distinct redox forms of recombinant HMGB1 (rHMGB1) were used that included fully reduced HMGB (fr-HMGB1), which acted as a chemokine, and disulfide-HMGB1 (ds-HMGB1), which possessed cytokine activity. Fr-HMGB1 in vivo was partially oxidized into ds-HMGB1; thus, the mutant protein non-oxidizable chemokine-HMGB (nonoxid-HMGB1) was applied. Concurrent with depressive behavior induced by four-week stress exposure, the HMGB1 concentrations in the serum and cerebral cortex substantially increased. Therefore, a single dose of rHMGB1 (200ng/5μl/mice) or vehicle was administered to mice via intracerebroventricular (i.c.v.) injection. The receptor inhibitors of TLR4/RAGE/CXCR4 (TAK-242/FPS-ZM1/AMD3100) (3mg/kg) were intraperitoneally injected 30min prior to rHMGB1 treatment. Depressive-like behavior was measured 20h post i.c.v. injection. Administration of fr-HMGB1 prolonged the immobility duration in the tail suspension test (TST) and decreased sucrose preference. In addition to depressive behavior, the hippocampal TNF-α protein slightly increased. These depressive behaviors and upregulation of hippocampal TNF-α were alleviated or abrogated by pretreatment with the inhibitors AMD3100, FPS-ZM1, and TAK-242. Alternatively, nonoxid-HMGB1 failed to induce TNF-α protein or prolong the immobility duration. As expected, ds-HMGB1 administration substantially upregulated hippocampal TNF-α protein, increased the immobility time in the TST and decreased sucrose preference. Moreover, both glycyrrhizin and TAK-242 improved ds-HMGB1-induced depressive behavior. Furthermore, TAK-242 significantly blocked the upregulation of hippocampal TNF-α protein and protected hippocampal myelin basic protein from ds-HMGB1-induced reduction. These drugs had no effect on the total or central distance in the open field test. Collectively, this initial experiment demonstrates the role and receptor mechanisms of HMGB1 under different redox states on the induction of depressive-like behavior. Both ds-HMGB1 and fr-HMGB1 may induce depressive-like behavior in vivo mainly via neuroinflammatory response activation.

Adjuvant vitamin C treatment in sepsis—how many oranges a day keep (vasopressor-dependent) septic shock away?

Vitamin C is an essential water-soluble vitamin that is involved in many biosynthetic and metabolic processes. In healthy fasting humans, circulating levels of ascorbate, the redox form of vitamin C, are typically in the range of 50–70 μmol/L (1). Levels <25 μmol/L reflect marginal deficiency (hypovitaminosis C). Severe (scurvy-like) vitamin C deficiency is present when levels fall below 10 μmol/L (2). In the critical care setting, vitamin C is particularly notorious for its strong immunomodulating and antioxidant activity. As such, vitamin C is promoted as adjuvant therapy in conditions characterized by excessive oxidative stress or crippled immunity such as ischemia-reperfusion disorders, trauma, and various inflammatory disease processes (3).

A Dicobalt Complex with an Unsymmetrical Quinonoid Bridge Isolated in Three Units of Charge: A Combined Structural, (Spectro)electrochemical, Magnetic and Spectroscopic Study.

Quinonoid ligands are excellent bridges for generating redox-rich dinuclear assemblies. A large majority of these bridges are symmetrically substituted, with examples of unsymmetrically substituted quinonoid bridges being extremely rare. We present here a dicobalt complex in its various redox states with an unsymmetrically substituted quinonoid bridging ligand. Two homovalent forms and one mixed-valent form have been isolated and characterized by single crystal X-ray diffraction. The complex displays a large comproportionation constant for the mixed-valent state which is three orders of magnitude higher than that observed for the analogous complex with a symmetrically substituted bridge. Results from electrochemistry, UV/Vis/NIR spectroelectrochemistry, SQUID magnetometry, multi-frequency EPR spectroscopy and FIR spectroscopy are used to probe the electronic structures of these complexes. FIR provides direct evidence of exchange coupling. The results presented here display the advantages of using an unsymmetrically substituted bridge: site specific redox chemistry, high thermodynamic stabilization of the mixed-valent form, isolation and crystallization of various redox forms of the complex. This work represents an important step on the way to generating heterodinuclear complexes for use in cooperative catalysis.

Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase-1.

Despite advances in our understanding of the oxidative pathways mediated by free hemoglobin (Hb), the precise contribution of its highly reactive redox forms to tissue and organ toxicities remains ambiguous. Heme, a key degradation byproduct of Hb oxidation, has recently been recognized as a damage‐associated molecular pattern (DAMP) molecule, able to trigger inflammatory responses. Equally damaging is the interaction of the highly redox active forms of Hb with other biological molecules. We determined the kinetics of heme loss from individual Hb redox states—ferrous (Fe2+), ferric (Fe3+), and ferryl (Fe4+)—using two different heme receptor proteins: hemopexin (Hxp), a naturally occurring heme scavenger in plasma, and a double mutant (H64Y/V86F), apomyoglobin (ApoMb), which avidly binds heme released from Hb. We show for the first time that ferric Hb (Fe3+) loses heme at rates substantially higher than that of ferryl Hb (Fe4+). This was also supported by a higher expression of heme oxygenase‐1 (HO‐1) when ferric Hb was added to cultured lung alveolar epithelial cells (E10). The reported cytotoxicity of Hb may therefore be attributed to a combination of accelerated heme loss from the ferric form and protein radical formation associated with ferryl Hb. Targeted therapeutic interventions can therefore be designed to curb specific oxidative pathways of Hb in hemolytic anemias and when Hb is used as an oxygen‐carrying therapeutic.

Protection by Nitric Oxide Donors of Isolated Rat Hearts Is Associated with Activation of Redox Metabolism and Ferritin Accumulation.

Preconditioning (PC) procedures (ischemic or pharmacological) are powerful procedures used for attaining protection against prolonged ischemia and reperfusion (I/R) injury, in a variety of organs, including the heart. The detailed molecular mechanisms underlying the protection by PC are however, complex and only partially understood. Recently, an ‘iron-based mechanism’ (IBM), that includes de novo ferritin synthesis and accumulation, was proposed to explain the specific steps in cardioprotection generated by IPC. The current study investigated whether nitric oxide (NO), generated by exogenous NO-donors, could play a role in the observed IBM of cardioprotection by IPC. Therefore, three distinct NO-donors were investigated at different concentrations (1–10 μM): sodium nitroprusside (SNP), 3-morpholinosydnonimine (SIN-1) and S-nitroso-N-acetylpenicillamine (SNAP). Isolated rat hearts were retrogradely perfused using the Langendorff configuration and subjected to prolonged ischemia and reperfusion with or without pretreatment by NO-donors. Hemodynamic parameters, infarct sizes and proteins of the methionine-centered redox cycle (MCRC) were analyzed, as well as cytosolic aconitase (CA) activity and ferritin protein levels. All NO-donors had significant effects on proteins involved in the MCRC system. Nonetheless, pretreatment with 10 μM SNAP was found to evoke the strongest effects on Msr activity, thioredoxin and thioredoxin reductase protein levels. These effects were accompanied with a significant reduction in infarct size, increased CA activity, and ferritin accumulation. Conversely, pretreatment with 2 μM SIN-1 increased infarct size and was associated with slightly lower ferritin protein levels. In conclusion, the abovementioned findings indicate that NO, depending on its bio-active redox form, can regulate iron metabolism and plays a role in the IBM of cardioprotection against reperfusion injury.

Syntheses, Structures, and Electrochemistry of the Defective ccp [Pt33(CO)38](2-) and the bcc [Pt40(CO)40](6-) Molecular Nanoclusters.

The molecular [Pt33(CO)38](2-) nanocluster was obtained from the thermal decomposition of Na2[Pt15(CO)30] in methanol. The reaction of [Pt19(CO)22](4-) with acids (1-2 equiv) affords the unstable [Pt19(CO)22](3-) trianion, which evolves with time leading eventually to the [Pt40(CO)40](6-) hexa-anion. The total structures of both nanoclusters were determined via single-crystal X-ray diffraction. [Pt33(CO)38](2-) displays a defective ccp Pt33 core and shows that localized deformations occur in correspondence of atomic defects to "repair" them. In contrast, [Pt40(CO)40](6-) shows a bcc Pt40 core and represents the largest Pt cluster with a body-centered structure. The rich electrochemistry of the two high-nuclearity platinum carbonyl clusters was studied by cyclic voltammetry and electrochemical in situ Fourier transform infrared spectroscopy. The redox changes of [Pt33(CO)38](2-) show features of chemical reversibility and electrochemical quasi-reversibility, and the vibrational spectra in the CO stretching region of the nine redox forms of the cluster [Pt33(CO)38](n) (n = 0 to -4, -6 to -9) are reported. Almost all the redox processes exhibited by [Pt40(CO)40](6-) are chemically and electrochemically reversible, and the eight oxidation states of [Pt40(CO)40] from -4 to -11 were spectroscopically characterized. The effect of the more regular bcc Pt-carbonyl cluster structure of [Pt40(CO)40](6-) with respect to that of the defective ccp Pt33 core on the redox behavior is discussed.

Muscle-specific colour stability of blesbok (Damaliscus pygargus phillipsi) meat

The increasing demand for meat from alternative species, such as blesbok (Damaliscus pygargus phillipsi), gives rise to the need for characterizing the quality attributes of fresh meat from these species. While muscle-specific colour stability has been extensively studied in conventional livestock, limited information is available on this phenomenon in game meat. Therefore, the objective of this study was to examine the colour stability of three major blesbok muscles, infraspinatus (IS), longissimus thoracis et lumborum (LTL) and biceps femoris (BF). Instrumental colour, surface myoglobin redox forms, and biochemical attributes influencing colour stability were measured on 2.5-cm steaks from blesbok IS, LTL, and BF during refrigerated storage under aerobic conditions for eight days. IS steaks consistently demonstrated higher (P≤0.05) redness, colour stability, and chroma than the LTL and BF steaks. These findings suggested that blesbok IS muscle is more colour-stable than its LTL and BF counterparts. The game industry may employ muscle-specific strategies to improve marketability of fresh blesbok meat.

Photosystem II Repair and Plant Immunity: Lessons Learned from Arabidopsis Mutant Lacking the THYLAKOID LUMEN PROTEIN 18.3.

Chloroplasts play an important role in the cellular sensing of abiotic and biotic stress. Signals originating from photosynthetic light reactions, in the form of redox and pH changes, accumulation of reactive oxygen and electrophile species or stromal metabolites are of key importance in chloroplast retrograde signaling. These signals initiate plant acclimation responses to both abiotic and biotic stresses. To reveal the molecular responses activated by rapid fluctuations in growth light intensity, gene expression analysis was performed with Arabidopsis thaliana wild type and the tlp18.3 mutant plants, the latter showing a stunted growth phenotype under fluctuating light conditions (Biochem. J, 406, 415–425). Expression pattern of genes encoding components of the photosynthetic electron transfer chain did not differ between fluctuating and constant light conditions, neither in wild type nor in tlp18.3 plants, and the composition of the thylakoid membrane protein complexes likewise remained unchanged. Nevertheless, the fluctuating light conditions repressed in wild-type plants a broad spectrum of genes involved in immune responses, which likely resulted from shade-avoidance responses and their intermixing with hormonal signaling. On the contrary, in the tlp18.3 mutant plants there was an imperfect repression of defense-related transcripts upon growth under fluctuating light, possibly by signals originating from minor malfunction of the photosystem II (PSII) repair cycle, which directly or indirectly modulated the transcript abundances of genes related to light perception via phytochromes. Consequently, a strong allocation of resources to defense reactions in the tlp18.3 mutant plants presumably results in the stunted growth phenotype under fluctuating light.

MP28-14 PROTEASE-ACTIVATED RECEPTOR 4 INDUCES BLADDER PAIN THROUGH DISULFIDE HIGH MOBILITY GROUP BOX-1 ACTING ON RECEPTORS FOR ADVANCED GLYCATION ENDPRODUCTS

You have accessJournal of UrologyBladder & Urethra: Anatomy, Physiology & Pharmacology I1 Apr 2016MP28-14 PROTEASE-ACTIVATED RECEPTOR 4 INDUCES BLADDER PAIN THROUGH DISULFIDE HIGH MOBILITY GROUP BOX-1 ACTING ON RECEPTORS FOR ADVANCED GLYCATION ENDPRODUCTS Dimitrios Kouzoukas, Fei Ma, Katherine Meyer-Siegler, Karin Westlund, David Hunt, and Pedro Vera Dimitrios KouzoukasDimitrios Kouzoukas More articles by this author , Fei MaFei Ma More articles by this author , Katherine Meyer-SieglerKatherine Meyer-Siegler More articles by this author , Karin WestlundKarin Westlund More articles by this author , David HuntDavid Hunt More articles by this author , and Pedro VeraPedro Vera More articles by this author View All Author Informationhttps://doi.org/10.1016/j.juro.2016.02.1064AboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareFacebookTwitterLinked InEmail INTRODUCTION AND OBJECTIVES Pain without obvious bladder pathology is a hallmark of Interstitial Cystitis / Painful Bladder Syndrome (IC/PBS). In a mouse model of bladder pain, urothelial protease activated receptor 4 (PAR4) stimulation causes pain without inflammation through macrophage migration inhibitory factor (MIF) release (Kouzoukas et al 2014). High mobility group box-1 (HMGB1), a ubiquitous nuclear non-histone DNA-binding protein, also mediates bladder pain, but not inflammation (Tanaka et al, 2014). Two redox states of all-thiol and disulfide HGMB1 respectively act through receptors for advanced glycation endproducts (RAGE) and toll-like receptor 4 (TLR4). Which HMGB1 form(s) contribute to bladder pain is unknown. We investigated whether: 1) bladder PAR4 stimulation causes urothelial HMGB1 release; 2) blocking MIF prevents urothelial HMGB1 release; 3) blocking HMGB1 prevents PAR4-induced hypersensitivity; 4) specific HMGB1 redox form causes pain, changes in micturition parameters and/or bladder inflammation; and 5) antagonizing specific HMGB1 receptors affect HMGB1-induced hypersensitivity. METHODS Female C57BL/6 mice were given intravesical PAR4 peptides (100 μM; 1 hr). Intraluminal fluid was collected and assayed for HMGB1, fluid parameters, abdominal hypersensitivity and histology were determined 24 hrs after pretreatment with HMGB1 inhibitor (glycyrrhizin: 50 mg/kg; i.p.), MIF blocker (ISO-1: 20 mg/kg; i.p.), specific HMGB1 redox forms (all-thiol or disulfide; 1, 2, 5, 10, 20, μg/150 μl; 1 hr), RAGE antagonist (FPS-ZM1; 10 mg/kg, i.p.), TLR4 antagonist (TAK-242; 3 mg/kg, i.p.), or vehicle. RESULTS PAR4-AP triggered urothelial HMGB1 release and Intravesical PAR4 induced abdominal hypersensitivity was prevented by blocking HMGB1. MIF inhibition blocked PAR4-mediated urothelial HMGB1 release. Intravesical disulfide HMGB1 (≥ 10 μg) instillation induced abdominal hypersensitivity, decreased micturition volume and increased voiding frequency. Thiol HMGB1 was ineffective. Systemic FPS-ZM1 fully and TAK-242 partially prevented disulfide HMGB1 (10 μg)-induced hypersensitivity. All doses of HMGB1 produced minimal to mild bladder edema and reactive changes. CONCLUSIONS Bladder PAR4 receptor stimulation induced urothelial HMGB1 release, mediated by MIF. Abdominal hypersensitivity, mediated by disulfide HGMB1 (not all-thiol), acted mainly through RAGE receptors. Urothelial MIF and HGMB1 receptors represent novel therapeutic targets for bladder pain conditions. © 2016FiguresReferencesRelatedDetails Volume 195Issue 4SApril 2016Page: e376 Advertisement Copyright & Permissions© 2016MetricsAuthor Information Dimitrios Kouzoukas More articles by this author Fei Ma More articles by this author Katherine Meyer-Siegler More articles by this author Karin Westlund More articles by this author David Hunt More articles by this author Pedro Vera More articles by this author Expand All Advertisement Advertisement PDF downloadLoading ...

Oxidative catalytic evolution of redox- and spin-states of a Fe-phthalocyanine studied by EPR

The catalytic-oxidative evolution of the redox/spin states of a Fe-phthalocyanine (Fe-Pc) catalyst was studied by electron paramagnetic resonance spectroscopy. Under oxidative catalytic conditions, Fe-Pc may evolve via multiple redox/spin conformations. Axial ligation of imidazole, O2 or t-Bu-OOH as oxidant, results in a complex multipath redox/spin landscape that was determined in detail herein. The high-spin conformations of Fe-Pc/imidazole evolve more slowly than the low-spin conformations. Catalytically active vs. inactive conformations were distinguished. A unified physicochemical catalytic reaction mechanism is discussed herein based on the distinct role of the various structural, spin and redox forms.

Cryptochrome 2 mediates directional magnetoreception in cockroaches

The ability to perceive geomagnetic fields (GMFs) represents a fascinating biological phenomenon. Studies on transgenic flies have provided evidence that photosensitive Cryptochromes (Cry) are involved in the response to magnetic fields (MFs). However, none of the studies tackled the problem of whether the Cry-dependent magnetosensitivity is coupled to the sole MF presence or to the direction of MF vector. In this study, we used gene silencing and a directional MF to show that mammalian-like Cry2 is necessary for a genuine directional response to periodic rotations of the GMF vector in two insect species. Longer wavelengths of light required higher photon fluxes for a detectable behavioral response, and a sharp detection border was present in the cyan/green spectral region. Both observations are consistent with involvement of the FADox, FAD(•-) and FADH(-) redox forms of flavin. The response was lost upon covering the eyes, demonstrating that the signal is perceived in the eye region. Immunohistochemical staining detected Cry2 in the hemispherical layer of laminal glia cells underneath the retina. Together, these findings identified the eye-localized Cry2 as an indispensable component and a likely photoreceptor of the directional GMF response. Our study is thus a clear step forward in deciphering the in vivo effects of GMF and supports the interaction of underlying mechanism with the visual system.

Photoelectrocatalytic oxidation of ascorbic acid and electrocatalytic reduction of dioxygen by polyaniline films for renewable energy conversion

A honeycomb-structured polyaniline (PANI) film is used to simultaneously promote the photoelectrocatalytic oxidation of ascorbic acid (AA) and electrocatalytic reduction of dioxygen (O2). The in situ spectroelectrochemical evidences suggest that the PANI film controlled between −0.20 and 0.70V shows four transformable redox forms, among which emeraldine base (EB) and leucoemeraldine base (LEB) can mediate the oxidation of AA and the reduction of O2, respectively. The EB-based electrode exhibits good linear spectral absorbance and/or photovoltaic responses to AA between 0.01 and 1.0mmolL−1 with high sensitivity and good reproducibility. The LEB-based electrode shows a good linear potentiometric response to O2 permeation flux rate between 10 and 60mLmin−1. Furthermore, the CdS nanoparticles and carbon felt (CF) are used to support the PANI film for the preparation of PANI/CdS anode and PANI/CF cathode. The assembled photoelectrochemical fuel cell driven by visible light shows an open-circuit photovoltage of 0.614V, short-circuit photocurrent density of 125.55μAcm−2, maximum power density of 19.05μWcm−2 at 0.492V, fill factor of 0.24 and photoenergy conversion efficiency of 10.58%. The present study provides a new approach for the utilization of renewable energy sources.

The Oxidation Status of Mic19 Regulates MICOS Assembly.

The function of mitochondria depends on the proper organization of mitochondrial membranes. The morphology of the inner membrane is regulated by the recently identified mitochondrial contact site and crista organizing system (MICOS) complex. MICOS mutants exhibit alterations in crista formation, leading to mitochondrial dysfunction. However, the mechanisms that underlie MICOS regulation remain poorly understood. MIC19, a peripheral protein of the inner membrane and component of the MICOS complex, was previously reported to be required for the proper function of MICOS in maintaining the architecture of the inner membrane. Here, we show that human and Saccharomyces cerevisiae MIC19 proteins undergo oxidation in mitochondria and require the mitochondrial intermembrane space assembly (MIA) pathway, which couples the oxidation and import of mitochondrial intermembrane space proteins for mitochondrial localization. Detailed analyses identified yeast Mic19 in two different redox forms. The form that contains an intramolecular disulfide bond is bound to Mic60 of the MICOS complex. Mic19 oxidation is not essential for its integration into the MICOS complex but plays a role in MICOS assembly and the maintenance of the proper inner membrane morphology. These findings suggest that Mic19 is a redox-dependent regulator of MICOS function.

Towards an understanding of redox heterogeneity of the photosystem II cytochrome b559 in the native membrane.

A complex redox titration pattern of cytochrome (Cyt) b559 in preparations of thylakoid membranes and photosystem (PS) II membrane fragments is commonly attributed to the presence of three conformational forms differing by a structure of the heme microenvironment. However, despite decades of research, structural determinants underlying differences between the redox forms of Cyt b559 have not been defined. In this work, we propose a different interpretation of redox heterogeneity in the native population of Cyt b559 assuming redox interaction between the Cyt b559 heme group and a nearby bound quinone (Q). The interacting quinone is supposed to be plastoquinone QC present in the unusual singly protonated form (QCH). The model successfully explains the unique redox properties of Cyt b559 and may provide a simple and effective mechanism of redox regulation of secondary electron transport in PS II. At the present time, the model of heme-quinone redox interaction can be considered as an alternative to the idea of conformational differences between the native redox forms of Cyt b559.