Infrared Spectra of Organo-Phosphorus Compounds: Iii. Phosphoramidates, Phosphoramidothionates, and Related Compounds

McIvor, R. A.; Hubley, C. E.

doi:10.1139/v59-118

Cited by 40 publications

(17 citation statements)

References 5 publications

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“…The results of infrared assays showed that the C=O stretching band appeared at a lower frequency (1781 cm −1 ), confirming CrpP wt activity-induced modification of the carboxylic function. Moreover, the absorption bands observed for CIP incubated in presence of CrpP wt were found to be at the same frequency as known organophosphorus compounds [15,16], suggesting that this could be the reason for the few bands that overlap with CIP. In addition, significant changes such as band intensity and the appearance of new bands in the region from 1000 to 700 cm −1 provided evidence about CIP phosphorylation by CrpP wt .…”

Section: Discussionmentioning

confidence: 90%

“…2a), indicating the phosphorylation of CIP by CrpP wt . Phosphorus compounds are known to show absorption bands for P-O-H around 3000-2800 cm −1 and 2400-2200 cm −1 , for P=O(OH) (single OH), 2800-2700 cm −1 , 2400-2300 cm −1 , and 1750-1600 cm −1 broad band [15,16]. At exception of mutation in I26, mutations in Gly7, Asp9, Lys33, and Cys40 in CrpP affect negatively the protein ability to modify the CIP molecule, since the infrared results showed that the -OH and C=O stretching bands remains in the same region at 3100-3000 cm −1 and 1784 cm −1 showing a similar pattern to the CIP without CrpP incubation, (Fig.…”

Section: Conserved Residues Of Crpp Are Important To Cip Modificationmentioning

confidence: 99%

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Identification of Essential Residues for Ciprofloxacin Resistance of Ciprofloxacin-Modifying Enzyme (CrpP) of pUM505

et al. 2020

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The ciprofloxacin-resistance crpP gene, encoded by the pUM505 plasmid, isolated from a P. aeruginosa clinical isolate, confers an enzymatic mechanism of antibiotic phosphorylation, which is ATP-dependent, that decreases ciprofloxacin susceptibility. Homologous crpP genes are distributed across extended spectrum beta-lactamase (ESBL)-producing isolates obtained from Mexican hospitals and which confer decreased susceptibility to CIP. The analysis of sequences of the CrpP of proteins showed that the residues Gly7, Thr8, Asp9, Lys33 and Gly34 (located at the N-terminal region) and Cys40 (located at the C-terminal region) are conserved in all proteins, suggesting that these residues could be essential for CrpP function. The aim of this study was to investigate the amino acids essential to ciprofloxacin resistance, which is conferred by the CrpP protein of pUM505 plasmid. Mutations in the codons encoding Gly7, Asp9, Lys33 and Cys40 of CrpP protein from pUM505 were generated by PCR fusion. The results showed that all mutations generated in CrpP proteins increased ciprofloxacin susceptibility in Escherichia coli . In addition, the CrpP modified proteins were purified and their enzymatic activity on ciprofloxacin was assayed, showing that these modified proteins do not exert catalytic activity on ciprofloxacin. Moreover, by infrared assays it was determined that the modified proteins were are not able to modify the ciprofloxacin molecule. Our findings are the first report that indicate that the amino acids, namely Gly7, Asp9, Lys33 and Cys40, which are conserved in the CrpP proteins, possess an essential role for the enzymatic mechanism that confers ciprofloxacin resistance.

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Section: Discussionmentioning

confidence: 90%

Section: Conserved Residues Of Crpp Are Important To Cip Modificationmentioning

confidence: 99%

Identification of Essential Residues for Ciprofloxacin Resistance of Ciprofloxacin-Modifying Enzyme (CrpP) of pUM505

et al. 2020

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“…This technique permits observation of cyanate species [32] [33] (CN at 2168 cm -1 , Fig. S7a) and phosphates, whether they are free or bonded (to carbamoyl moieties) [34] [35] (PO around 1100 cm -1 , Fig. S6).…”

Section: ) Carbamoyl Phosphate Hydrolysismentioning

confidence: 99%

Carbamoyl phosphate and its substitutes for the uracil synthesis in origins of life scenarios

Ter-Ovanessian

Rigaud

Mezzetti

et al. 2021

Preprint

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The first step of pyrimidine synthesis along the orotate pathway is studied to test the hypothesis of geochemical continuity of protometabolic pathways at the origins of life. Carbamoyl phosphate (CP) is the first high-energy building block that intervenes in the in vivo synthesis of the uracil ring of UMP. Thus, the likelihood of its occurrence in prebiotic conditions is investigated herein. The evolution of carbamoyl phosphate in water and in ammonia aqueous solutions without enzymes was characterised using ATR-IR, 31P and 13C spectroscopies. Carbamoyl phosphate initially appears stable in water at ambient conditions before transforming to cyanate and carbamate/hydrogenocarbonate species within a matter of hours. Cyanate, less labile than CP, remains a potential carbamoylating agent. In the presence of ammonia, CP decomposition occurs more rapidly and generates urea. We conclude that CP is not a likely prebiotic reagent by itself. Alternatively, cyanate and urea may be more promising substitutes for CP, because they are both “energy-rich” (high free enthalpy molecules in aqueous solutions) and kinetically inert regarding hydrolysis. Energy-rich inorganic molecules such as trimetaphosphate or phosphoramidates were also explored for their suitability as sources of carbamoyl phosphate. Although these species did not generate CP or other carbamoylating agents, they exhibited energy transduction, specifically the formation of high-energy P-N bonds. Future efforts should aim to evaluate the role of carbamoylating agents in aspartate carbamoylation, which is the following reaction in the orotate pathway

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“…The strong absorption bands measured in the 900-1,300 cm -1 region, with a maximum at approximately 1,100 cm -1 , can be attributed to the P=O bond of the phosphate species [33][34][35]. The band at 990 cm -1 is related to the asymmetric stretching of the P-O-R bond of the organophosphorus compounds, for example, O=P(OR) 3 [35,36]. The two bands appearing at 935 and 740 cm -1 result from the asymmetric and symmetric stretching vibrations of the P-O-P bonds [31,35], which could be attributed to the presence of poly(organo)phosphate compounds.…”

Section: Atr-ftirmentioning

confidence: 99%

Differences in nano-topography and tribochemistry of ZDDP tribofilms from variations in contact configuration with steel and DLC surfaces

et al. 2021

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In this work, we evaluated the effect of the counter-body material (the same or dissimilar) and contact configuration (moving or stationary body), at similar contact tribological conditions, on the tribochemical and nanotopography characteristics of adsorbed surface films. Zinc dialkyldithiophosphate (ZDDP), the best performing anti-wear additive, was used in self-mated steel/steel and DLC/DLC contacts, which were compared with mixed steel/DLC and DLC/steel contacts in 1-h and 6-h sliding tests. The macroscale (tribometer) and nanoscale (atomic force microscopy) friction, thickness, topography, and chemical (attenuated total reflection-Fourier transform infrared spectroscopy and X-ray photoelectron spectroscopy) properties of the tribofilms were studied. The results revealed unexpectedly large differences in all the studied tribofilm parameters; this is because all the tribofilms are completely different; this includes the chemical composition, which is known to have a crucial effect on the nano- and macro-scale tribological properties. These results clearly demonstrate that the surface material, additives, and common contact operating parameters, that is, pressure, velocity, and temperature, crucially affect the ZDDP tribofilm as well as the position of the moving or stationary surface within the contact, and the material of the moving/stationary bodies.

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Infrared Spectra of Organo-Phosphorus Compounds: Iii. Phosphoramidates, Phosphoramidothionates, and Related Compounds

Cited by 40 publications

References 5 publications

Identification of Essential Residues for Ciprofloxacin Resistance of Ciprofloxacin-Modifying Enzyme (CrpP) of pUM505

Identification of Essential Residues for Ciprofloxacin Resistance of Ciprofloxacin-Modifying Enzyme (CrpP) of pUM505

Carbamoyl phosphate and its substitutes for the uracil synthesis in origins of life scenarios

Differences in nano-topography and tribochemistry of ZDDP tribofilms from variations in contact configuration with steel and DLC surfaces

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