Hydrogen Peroxide Mediates Suberization, Root Thickness and Stomatal Movement in Wheats

Abstract Background Whether stomatal movement by darkness in Arabidopsis thaliana is mediated by hydrogen sulfide (H2S) is undiscovered yet, so the interaction between hydrogen peroxide (H2O2) and H2S in the process needs to be elucidated. Results Our results indicated that H2S modulators aminooxy acetic acid (AOA), potassium pyruvate (N3H3KO3) + ammonia (NH3), hydroxylamine (NH2OH), and hypotaurine (HT) inhibited darkness-induced stomatal closure, H2S generation and L-/D-cysteine desulfhydrase (L-/D-CDes) activity increased in wild-type A. thaliana leaves. Darkness induced stomatal closure in wild-type plants, but failed in Atl-cdes and Atd-cdes mutants. Additionally, both L-/D-CDes activity and H2S content were significantly decreased after applying H2O2 modulators salicylhydroxamic acid (SHAM), ascorbic acid (ASA), diphenylene iodonium (DPI), and catalase (CAT) in darkness, but there was almost no effects on H2O2 levels in the presence of AOA, C3H3KO3+NH3, NH2OH, and HT of wild-type plants in darkness. Moreover, darkness couldn't increase H2S content and L-/D-CDes activity of AtrbohF and AtrbohD/F mutants leaves, but increased H2O2 levels in Atl-cdes and Atd-cdes guard cells. Conclusions We observed that L-/D-CDes-generated H2S mediates stomatal closure by darkness, and functions downstream of H2O2 in A. thaliana.

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Peroxidase Localization in Hartmanella Trophozoites

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065778 ◽

1971 ◽

Vol 29 ◽

pp. 346-347 ◽

Cited By ~ 1

Author(s):

George E. Childs ◽

Joseph H. Miller

Keyword(s):

Hydrogen Peroxide ◽

Ultrastructural Localization ◽

Pathogenic Strain ◽

Oxidative Enzymes ◽

Differential Centrifugation ◽

Electron Microscopic ◽

Microscopic Studies ◽

The Subject ◽

Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

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Fluorescent proteins for in vivo imaging, where's the biliverdin?

Biochemical Society Transactions ◽

10.1042/bst20200444 ◽

2020 ◽

Vol 48 (6) ◽

pp. 2657-2667

Author(s):

Felipe Montecinos-Franjola ◽

John Y. Lin ◽

Erik A. Rodriguez

Keyword(s):

Hydrogen Peroxide ◽

In Vivo Imaging ◽

Near Infrared ◽

Fluorescent Protein ◽

Fluorescent Proteins ◽

Fluorescent Imaging ◽

Infrared Light ◽

Red Fluorescent Protein ◽

Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

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Protective effect of chitooligosaccharides on hydrogen peroxide-induced PC-12 cells death by inhibition of oxidative damage

Cell Biology International ◽

10.1042/cbi034s027d ◽

2010 ◽

Vol 34 (8) ◽

pp. S27-S27

Author(s):

Xueling Dai ◽

Ping Chang ◽

Ke Xu ◽

Changjun Lin ◽

Hanchang Huang ◽

...

Keyword(s):

Hydrogen Peroxide ◽

Oxidative Damage ◽

Protective Effect ◽

Pc 12 Cells ◽

Cells Death

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Signal-regulated oxidation of proteins via MICAL

Biochemical Society Transactions ◽

10.1042/bst20190866 ◽

2020 ◽

Vol 48 (2) ◽

pp. 613-620

Author(s):

Clara Ortegón Salas ◽

Katharina Schneider ◽

Christopher Horst Lillig ◽

Manuela Gellert

Keyword(s):

Signal Transduction ◽

Hydrogen Peroxide ◽

Cell Death ◽

Redox Regulation ◽

Signal Transduction Pathways ◽

Cellular Functions ◽

Intracellular Signals ◽

Amino Acid Side Chains ◽

Specific Receptors ◽

Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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