cytochrome-c-t and hydrazine

cytochrome-c-t has been researched along with hydrazine* in 4 studies

Other Studies

4 other study(ies) available for cytochrome-c-t and hydrazine

ArticleYear
A polynuclear Cu(ii) complex for real time monitoring of mitochondrial cytochrome C release during cellular apoptosis.
    Chemical communications (Cambridge, England), 2020, Jun-18, Volume: 56, Issue:48

    A new amide-imine conjugate, 2-hydroxybenzoic acid-(2-hydroxybenzylidene)-hydrazide (L

    Topics: Animals; Apoptosis; Cell Line; Coordination Complexes; Copper; Cytochromes c; Humans; Hydrazines; Mice; Microscopy, Fluorescence; Mitochondria; Spectrophotometry

2020
Effects of cycle duration of an external electrostatic field on anammox biomass activity.
    Scientific reports, 2016, Jan-22, Volume: 6

    In this study, the effects of different cycle durations of an external electrostatic field on an anammox biomass were investigated. The total application time per day was 12 h at 2 V/cm for different cycle durations (i.e., continuous application-resting time) of 3 h-3 h, 6 h-6 h, and 12 h-12 h. Compared with the control reactor, the nitrogen removal rates (NRRs) increased by 18.7%, 27.4% and 8.50% using an external electrostatic field application with a continuous application time of 3 h, 6 h and 12 h. Moreover, after the reactor was running smoothly for approximately 215 days under the optimal electrostatic field condition (mode 2, continuous application-rest time: 6 h-6 h), the total nitrogen (TN) removal rate reached a peak value of approximately 6468 g-N/m(3)/d, which was 44.7% higher than the control. The increase in 16S rRNA gene copy numbers, heme c content and enzyme activities were demonstrated to be the main reasons for enhancement of the NRR of the anammox process. Additionally, transmission electron microscope observations proved that a morphological change in the anammox biomass occurred under an electrostatic field application.

    Topics: Ammonium Compounds; Anaerobiosis; Bacteria; Biomass; Bioreactors; Cytochromes c; Flow Cytometry; Gene Dosage; Heme; Hydrazines; Microscopy, Electron, Transmission; Nitrogen; Oxidation-Reduction; Oxidoreductases; Peroxidase; Polymerase Chain Reaction; RNA, Ribosomal, 16S; Static Electricity

2016
Amphiphilic aminoclay-RGO hybrids: a simple strategy to disperse a high concentration of RGO in water.
    Nanoscale, 2013, Jun-21, Volume: 5, Issue:12

    The aqueous dispersion of graphene or reduced graphene oxide (RGO) is very much important to realize the full potential of these materials in many fields. Herein we present a simple route to prepare highly water dispersible aminoclay-RGO (AC-RGO) hybrids by the in situ condensation of aminoclay over graphene oxide (GO) followed by reduction with hydrazine hydrate. The resultant hybrids are stable in aqueous media even at concentrations up to 7.5 mg RGO per mL. To the best of our knowledge this is the highest concentration of an aqueous dispersion of RGO. Significantly, the hybrids are amphiphilic in nature and show simultaneous adsorption of Cytochrome C through hydrophobic interaction and DNA through electrostatic interaction. This strategy opens up new possibilities for the prospect of RGO in catalysis and biomedical applications.

    Topics: Adsorption; Catalysis; Cytochromes c; DNA; Graphite; Hydrazines; Hydrophobic and Hydrophilic Interactions; Isoelectric Point; Oxides; Static Electricity; Water

2013
Hydrazide derivatives produce active oxygen species as hydrazine.
    Bioorganic chemistry, 2005, Volume: 33, Issue:6

    It is well documented that some hydrazines are quite sensitive to oxidation and may serve as the electron donor for the reduction of oxygen, whereas hydrazides are not believed to react directly with oxygen. Data presented in this paper show that both hydrazides and hydrazines share an N-N moiety, which is assumed to react with atmospheric oxygen and produce oxygen radicals, at various degrees of efficiency. Since spectrometric measurements of hydrazide just after solubilization showed that the molecular mass remains constant in the absence of oxygen, we can conclude that hydrazides do not react with the oxygen through a slow spontaneous hydrolytic release of hydrazine. However, hydrazine is more reactive than hydrazide, which requires hours rather than minutes to produce measurable quantities of radical species. Differences were also apparent for various substituted derivatives. The reaction was significantly enhanced by the presence of metal ions. Data reported here demonstrate that hydrazides cause irreversible damage to the prosthetic group of proteins as well as causing degradation of the polypeptide chain into small fragments.

    Topics: Cytochromes c; Electrophoresis, Polyacrylamide Gel; Hydrazines; Iproniazid; Isoniazid; Light-Harvesting Protein Complexes; Oxidation-Reduction; Reactive Oxygen Species; Spectrometry, Mass, Electrospray Ionization

2005