Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Oxygen Compounds”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 559 records · Page 31Linked to original sources
PubMed1976

Synthesis of certain spiro compounds.

The synthesis of certain N-substituted azaspirodiones and azaspiranes is described. Fusing equimolecular amounts of 2-oxaspiro [4.4]nonane-1.3-dione with a number of amino compounds afforded the corresponding N-substituted azaspirodiones. However, with certain o-substituted anilines, no condensation took place. Reduction of the N-haloaryl azaspirodiones gave the corresponding oxygen free compounds. Other azaspiranes were isolated as the quaternary methiodides. Applying the Mannich conditions to 2-azaspiro[4.4]nonane-1.3-dione yielded the N-Mannich bases.

Chemical Phenomena↗
PubMed2000

Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (s) nitrosation dependence on the absence or presence of oxygen.

The amino acid sequence of human myoglobin (Mb) is similar to other mammalian Mb except for a unique cysteine residue at position 110 (Cys(110)). Anaerobic treatment of ferrous forms of wild-type human Mb, the C110A variant of human Mb or horse heart Mb, with either authentic NO or chemically derived NO in vitro yields heme-NO complexes as detected by electron paramagnetic resonance spectroscopy (EPR). By contrast, no EPR-detectable heme-NO complex was observed from the aerobic reactions of NO and either the ferric or oxy-Mb forms of wild-type human or horse heart myoglobins. Mass analyses of wild-type human Mb treated aerobically with NO indicated a mass increase of approximately 30 atomic mass units (i.e., NO/Mb = 1 mol/mol). Mass analyses of the corresponding apoprotein after heme removal showed that NO was associated with the apoprotein fraction. New electronic maxima were detected at A(333 nm) (epsilon = 3665 +/- 90 mol(-)(1) cm(-)(1); mean +/- S.D.) and A(545 nm) (epsilon = 44 +/- 3 mol(-)(1) cm(-)(1)) in solutions of S-nitrosated wild-type human Mb (similar to S-nitrosoglutathione). Importantly, the sulfhydryl S-H stretch vibration for Cys(110) measured by Fourier transform infrared (nu approximately 2552 cm(-)(1)) was absent for both holo- and apo- forms of the wild-type human protein after aerobic treatment of the protein with NO. Together, these data indicate that the reaction of wild-type human Mb and NO yields either heme-NO or a novel S-nitrosated protein dependent on the oxidation state of the heme iron and the presence or absence of dioxygen.

Animals↗
PubMed1996

S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control.

A dynamic cycle exists in which haemoglobin is S-nitrosylated in the lung when red blood cells are oxygenated, and the NO group is released during arterial-venous transit. The vasoactivity of S-nitrosohaemoglobin is promoted by the erythrocytic export of S-nitrosothiols. These findings highlight newly discovered allosteric and electronic properties of haemoglobin that appear to be involved in the control of blood pressure and which may facilitate efficient delivery of oxygen to tissues. The role of S-nitrosohaemoglobin in the transduction of NO-related activities may have therapeutic applications.

Allosteric Regulation↗
PubMed2001

Vibrational spectroscopy of the oxygen-evolving complex and of manganese model compounds.

A number of molecularly specific models for the oxygen-evolving complex in photosystem II (PSII) and of manganese-substrate water intermediates that may occur in this process have been proposed recently. We summarize this work briefly. Fourier transform infrared techniques have emerged as fruitful tools to study the molecular structures of Y(Z) and the manganese complex. We discuss recent work in which mid-IR (1000-2000 cm(-1)) methods have been used in this effort. The low-frequency IR region (<1000 cm(-1)) has been more difficult to access for technical reasons, but good progress has been made in overcoming these obstacles. We update recent low-frequency work on PSII and then present a detailed summary of relevant manganese model compounds that will be of importance in understanding the emerging biological data.

Manganese↗
PubMed1980

Superoxide dismutases.

Superoxide dismutases (EC 1.15.1.1) are metalloenzymes that catalytically scavenge the superoxide radical. They are essential for the aerobic survival of all forms of life. There are three types of superoxide dismutase, containing manganese, iron, or copper and zinc. The copper--zinc type has generally been isolated from eukaryotic cells except for the enzyme for the symbiotic marine bacterium Photobacterium leiognathi. The copper--zinc type, from different sources, has a molecular weight of about 32 000, and is composed of two identical subunits, each containing one atom of copper and one atom of zinc. The copper participates in the catalytic activity of the enzyme, while the zinc plays only a structural role. The enzyme has been resolved reversibly. Superoxide dismutases provide protection against oxygen toxicity, against compounds that cause exacerbation of oxygen toxicity, against ionizing radiation, and also against the damaging sequelae of prolonged inflammation.

Aerobiosis↗
PubMed1984

The influence of X ray dose levels on normal tissue radioprotection by WR-2721.

A variation in the degree of radioprotection by WR-2721 with X ray dose level is detectable in several normal tissue studies. A similar effect in tumors has been attributed to differential protection of oxic and hypoxic cells. For normal tissues it was previously postulated that it resulted from greater protection of 1 hit damage at low doses, with less protection of multihit damage. However, more extensive analysis of the normal tissue data, including both single dose and fractionated results show that it is not a universal effect in all normal tissues. It now seems more likely that varying PF values result from differential protection of cells at different oxygen tensions, even though the heterogeneity of oxygenation may not be detectable in the response to X rays alone.

Amifostine↗
PubMed2000

Regulation of leukocyte function by nitric oxide donors: the effect of S-nitroso-thiol complexes.

The aim of this study was to evaluate the effectiveness of a novel protein-bound S-nitroso-thiol, S-nitroso-albumin (S-NO-alb), in modulating neutrophil-endothelial cell adhesion, activation, and interactions. Due to the highly variable kinetics of NO release from the low-molecular-weight thiol adducts S-nitroso-N-acetylpenicillamine (SNAP) and S-nitroso-glutathione (GSNO), we expected S-NO-alb to be a more effective modulator of inflammatory interactions through its slow, steady, and prolonged release of NO. Human umbilical-vein endothelial cells (HUVECs) challenged with lipopolysaccharide (LPS) demonstrated upregulated adhesion of neutrophils that was significantly attenuated by pretreatment with S-NO-alb (1.0-100 microM) (p < .05), but not SNAP or GSNO. Pretreatment with S-NO-alb, SNAP, or GSNO attenuated tumor necrosis factor-alpha primed *O2- release from neutrophils and increased neutrophil cGMP accumulation. On a molar basis, S-NO-alb expressed a 10-fold greater potency than SNAP or GSNO at modulating these effects. Kinetics studies confirmed the relative stability of spontaneous NO release from S-NO-alb compared with highly variable kinetic profiles of SNAP and GSNO. Our results demonstrate that S-NO-alb more effectively modulates endothelial-cell and neutrophil immunoinflammatory responses versus its related low-molecular-weight thiol complexes.

Cell Adhesion↗
PubMed2001

Effect of structural modification on photodynamic activity of hypocrellins.

Aluminum ion complexed 5,8-di-Br-hypocrellin B is a new water-soluble perylenequinonoid derivative with enhanced absorption over hypocrellin B (HB) in the phototherapeutic window (600-900 nm). Electron paramagnetic resonance and 9,10-diphenyl-anthracene bleaching methods were used to investigate the photosensitizing activity of [AL2(5,8-di-Br-HB)Cl4]n in the presence of oxygen. Singlet oxygen, superoxide anion radical and hydroxyl radical can be generated by [AL2(5,8-di-Br-HB)CL4]n photosensitization. Singlet oxygen (1O2) is formed via energy transfer from triplet-state [AL2(5,8-di-Br-HB)CL4]n to ground-state molecular oxygen. 1O2 participates in the generation of a portion of superoxide anion radical (O2.-). Besides superoxide anion radical (O2.-) may originate from the electron transfer between the triplet-state [AL2(5,8-di-Br-HB)CL4]n and the ground-state molecular oxygen. OH is formed through the Fenton-Haber-Weiss reaction and the decomposition of DMPO-1O2 adduct. Compared with HB [AL2(5,8-di-Br-HB)CL4]n primarily remains and enhances the generation efficiency of superoxide anion radical and hydroxyl radical but that of singlet oxygen decreases.

Electron Spin Resonance Spectroscopy↗
PubMed1981

Chemistry and biochemistry of superoxide dismutases.

The univalent reduction of oxygen to the superoxide radical is a commonplace event in biological systems, and the superoxide dismutases, which catalytically scavenge this radical, are the primary defence against its potential cytotoxicity. The superoxide radical and hydrogen peroxide, can interact to generate the hydroxyl radical. Superoxide dismutases are metalloenzymes that can prevent the generation of hydroxyl radical by keeping the level of superoxide radical vanishingly low. Superoxide dismutases are essential for the survival of all oxygen metabolizing organisms. There are three types of superoxide dismutases: the manganese-containing, the iron-containing, and the copper-zinc-containing superoxide dismutases. The copper-zinc containing superoxide dismutases have generally been isolated from eukaryotic cells except for the enzyme from the symbiotic marine bacterium Photobacterium leiogenthi. The copper-zinc containing superoxide dismutases, from different sources, have a molecular weight of about 32,000, are composed of two identical subunits, and contain one atom of copper and one atom of zinc per subunit. The copper participates in the catalytic activity of the enzyme, while the zinc plays only a structural role. The enzyme has been resolved reversibly. Superoxide dismutases have been seen to provide protection against oxygen toxicity, against compounds that cause exacerbation of oxygen toxicity, against ionizing radiation, and also against the damaging sequelae of prolonged inflammation.

Animals↗
PubMed1977

The interaction of some bis-arylhydroxysulphonic acids with a site of known structure in human haemoglobin.

1 Two bis-arylhydroxysulphonic acids were previously designed to interact with the known molecular configuration of the 2,3-diphosphoglycerate (DPG) receptor-site of human haemoglobin. These compounds liberate oxygen from the haemoglobin similarly to DPG. 2 Solutions of haemoglobin have now been observed under physiological conditions by nuclear magnetic resonance (n.m.r.) in the presence of DPG and of the compounds. 3 Two peaks in the n.m.r. spectrum of haemoglobin are shifted when DPG is added to the solution. 4 The same two peaks in the spectrum are affected by the compounds. 5 The observations are compatible with the predicted interaction between the compounds and the haemoglobin receptor site.

Arylsulfonates↗
PubMed2000

Nitrosylation of manganese(II) tetrakis(N-ethylpyridinium-2-yl)porphyrin: a simple and sensitive spectrophotometric assay for nitric oxide.

Reaction between NO(*) and manganese tetrakis(N-ethylpyridinium-2-yl)porphyrin (Mn(III)TE-2-PyP(5+)) was investigated at 25 degrees C. At high excess of NO(*) (1.5 mM) the reaction with the oxidized, air-stable form Mn(III)TE-2-PyP(5+) (5 microM), proceeds very slowly (t(1/2) congruent with 60 min). The presence of excess ascorbate (1 mM) produces the reduced form, Mn(II)TE-2-PyP(4+), which reacts with NO(*) stoichiometrically and in the time of mixing (k congruent with 1 x 10(6) M(-1) s(-1)). The high rate of formation and the stability of the product, Mn(II)TE-2-PyP(NO)(4+) (¿Mn(NO)¿(6)), make the reaction outcompete the reaction of NO(*) with O(2). Our in vitro measurements show a linear absorbance response upon addition of NO to a PBS, pH 7.4, solution containing an excess of ascorbate over Mn(III)TE-2-PyP(5+). Thus, the observed interactions can be the basis of a convenient and sensitive spectrophotometric assay for NO(*). Also, it may have important implications for the in vivo behavior of Mn(III)TE-2-PyP(5+) which is currently exploited as a possible therapeutic agent for various oxygen-radical related disorders.

Ascorbic Acid↗
PubMed1977

Reciprocal interaction of hemoglobin with oxygen and protons. The influence of allosteric polyanions.

The interaction of three inositol esters, inositol hexaphosphate (IHP), inositol pentaphosphate (IPP), and inositol hexasulfate (IHS), with hemoglobin has been investigated. The proton uptake method was used to obtain the six binding constants for deoxy- and oxyhemoglobin. These data combined with oxygen binding curves over a range of cofactor concentrations were used to test theoretical and empirical equations relating the affinity of hemoglobin for oxygen and allosteric effectors. The Bohr and Haldane coefficients in the presence of the inositol esters are unequal at low, but not at high, concentration of the cofactors. The maximum value reached by both parameters increases with the number of negative charges of the polyanion. 2,3-Diphosphoglycerate (DPG) differs sharply from the inositol esters since even at high concentrations of this cofactor, the Haldane coefficient remains elevated. This is a reflection of the negligible affinity of DPG for fully oxygenated hemoglobin.

Adult↗