Metal complexes of anti-inflammatory drugs. Part IV. Tenoxicam complexes of manganese(II), iron(III), cobalt(II), nickel(II) and copper(II)

Bury, Adrian; Underhill, Allan E.; Kemp, D. R.; O'Shea, N.J.; Smith, John; Gomm, P. S.

doi:10.1016/s0020-1693(00)81186-x

Cited by 50 publications

(22 citation statements)

References 29 publications

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“…Superoxide anion radicals were generated using phenazine methosulfate and NADH as previously described (38). Generation of superoxide anion was monitored by observing the reduction of nitroblue tetrazolium to blue formazan at 560 nm (4,7,38).…”

Section: Methodsmentioning

confidence: 99%

“…Between 1 and 59 M amended copper, the percent increase in pMMO to percent increased membrane content per cell was approximately 1 to 0.17. Previous studies have shown a relationship between copper and membrane development in methanotrophs (3,5,7,(27)(28)(29). However, these studies compared only a few copper concentrations, with 10 M amended copper as the maximum concentration examined.…”

Section: Vol 185 2003 Pmmo-ndh Complex From M Capsulatus Bath 5757mentioning

confidence: 96%

“…The structural characterization of Cu-cbc (21) also indicates that this molecule may function as an oxygen radical scavenger: i.e., the copper atom is in an open coordination sphere with a tetrahedral geometry on the surface of the molecule (3,8,15,16,38). To test this activity, the O 2 ⅐ Ϫ scavenging properties of Cu-cbc were examined according to its ability to inhibit the reduction of nitroblue tetrazolium (7,8) (Fig. 10).…”

Section: Vol 185 2003 Pmmo-ndh Complex From M Capsulatus Bath 5757mentioning

confidence: 99%

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The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath

et al. 2003

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Improvements in purification of membrane-associated methane monooxygenase (pMMO) have resulted in preparations of pMMO with activities more representative of physiological rates: i.e., >130 nmol ⅐ min ؊1 ⅐ mg of protein ؊1 . Altered culture and assay conditions, optimization of the detergent/protein ratio, and simplification of the purification procedure were responsible for the higher-activity preparations. Changes in the culture conditions focused on the rate of copper addition. To document the physiological events that occur during copper addition, cultures were initiated in medium with cells expressing soluble methane monooxygenase (sMMO) and then monitored for morphological changes, copper acquisition, fatty acid concentration, and pMMO and sMMO expression as the amended copper concentration was increased from 0 (approximately 0.3 M) to 95 M. The results demonstrate that copper not only regulates the metabolic switch between the two methane monooxygenases but also regulates the level of expression of the pMMO and the development of internal membranes. With respect to stabilization of cell-free pMMO activity, the highest cell-free pMMO activity was observed when copper addition exceeded maximal pMMO expression. Optimization of detergent/ protein ratios and simplification of the purification procedure also contributed to the higher activity levels in purified pMMO preparations. Finally, the addition of the type 2 NADH:quinone oxidoreductase complex (NADH dehydrogenase [NDH]) from M. capsulatus Bath, along with NADH and duroquinol, to enzyme assays increased the activity of purified preparations. The NDH and NADH were added to maintain a high duroquinol/duroquinone ratio.Methanotrophs are a group of gram-negative bacteria that utilize methane or methanol as the sole source of carbon and energy (1,20). The initial oxidation of methane to methanol is catalyzed by methane monooxygenase (MMO). In some methanotrophs, two different MMOs can be expressed, depending on the copper concentration during growth (11, 37, 39): a soluble cytoplasmic MMO (sMMO) and a membrane-associated, or particulate, MMO (pMMO). In cells cultured under low copper/biomass ratios (Յ0.9 nmol of Cu/mg of cell protein), the sMMO is expressed (20, 28). Cells cultured under higher copper/biomass ratios express pMMO, and there is no detectable sMMO expression (35,43). While sMMO is a wellcharacterized enzyme that consists of a hydroxylase component composed of three polypeptides and a hydroxo-bridged binuclear iron cluster-an NADH-dependent reductase component composed of one polypeptide containing both FAD and [Fe 2 S 2 ] cofactors and a regulatory polypeptide (18,26,27,31,47)-information on the molecular properties of pMMO is limited due to the instability of pMMO in cell-free fractions.Purification of the pMMO has been reported from Methylococcus capsulatus Bath (2,25,33, 52) and M. trichosporium

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Section: Methodsmentioning

confidence: 99%

Section: Vol 185 2003 Pmmo-ndh Complex From M Capsulatus Bath 5757mentioning

confidence: 96%

Section: Vol 185 2003 Pmmo-ndh Complex From M Capsulatus Bath 5757mentioning

confidence: 99%

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The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath

et al. 2003

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“…Piroxicam when deprotonated can form conformational rotamers and the most stable rotamer is the ZZZ, the one with the intramolecular H-bond (Scheme 1) [53,54]. It is also reported that enol tautomers of b-dicarbonyls exhibiting keto-enol tautomerism are known to be stabilized by strong intramolecular OHO hydrogen bonding [108,109]. The possibility of piroxicam coordination through O enol instead of O amide cannot be definitely ruled out, although it should be accompanied by a more significant shift of the amide band accordingly to tridentate (<1590 cm À1 ) species.…”

Section: Infrared Spectroscopymentioning

confidence: 99%

Mononuclear metal complexes with Piroxicam: Synthesis, structure and biological activity

Christofis

Katsarou

Papakyriakou

et al. 2005

Journal of Inorganic Biochemistry

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“…Dimethyl sulfoxide (DMSO), N,Ndimethylformamide (DMF), tetrahydrofurane (THF), were high purity compounds from Sigma-Aldrich (Milan, Italy) and used without any further purification. were prepared as previously reported from this laboratory or from procedures analogous to those reported by others [14,19,27,28].…”

Section: Methodsmentioning

confidence: 99%

Release studies from smart hydrogels as carriers for piroxicam and copper(II)–oxicam complexes as anti-inflammatory and anti-cancer drugs. X-ray structures of new copper(II)–piroxicam and –isoxicam complex molecules

Tamasi

Serinelli

Consumi

et al. 2008

Journal of Inorganic Biochemistry

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Metal complexes of anti-inflammatory drugs. Part IV. Tenoxicam complexes of manganese(II), iron(III), cobalt(II), nickel(II) and copper(II)

Cited by 50 publications

References 29 publications

The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath

The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath

Mononuclear metal complexes with Piroxicam: Synthesis, structure and biological activity

Release studies from smart hydrogels as carriers for piroxicam and copper(II)–oxicam complexes as anti-inflammatory and anti-cancer drugs. X-ray structures of new copper(II)–piroxicam and –isoxicam complex molecules

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