Easy Ligand Activation in the Coordination Sphere of Ru inside the [PW11O39]7– Backbone

Irradiation of the Keggin-type [PW11O39{Ru(NO)}]4− (Ru-NO) polyoxometalate in CH3CN results in rapid NO ligand elimination with the formation of [PW11O39{RuIII(CH3CN)}]4− (Ru-CH3CN). This complex offers an easy entry into the Ru-based chemistry of the {PW11Ru} complex. Attempts to substitute N3− for CH3CN in the presence of an NaN3 excess lead a variety of products: (i) [PW11O39{RuIII(N3)}]4− (Ru-N3); (ii) [PW11O39{RuIII(N4HC-CH3)}]4− (Ru-Tz) as a click-reaction product; and (iii) [PW11O39{RuII(N2)}]5− (Ru-N2). UV-VIS, CV, and HR-ESI-MS techniques were used for the reaction monitoring and characterization of the products.

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Characterization of thirty-nine polymethoxylated flavonoids (PMFs) in the branches of Murraya paniculata by HPLC-DAD-ESI-MS/MS

Chinese Journal of Natural Medicines ◽

10.3724/sp.j.1009.2013.00063 ◽

2014 ◽

Vol 11 (1) ◽

pp. 63-70 ◽

Cited By ~ 9

Author(s):

Jia-Yu ZHANG ◽

Jian-Qiu LU ◽

Xiao-Yan GAO ◽

Qian ZHANG ◽

Ning LI ◽

...

Keyword(s):

Esi Ms ◽

Murraya Paniculata

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Biological activities of two polypore macrofungi (Basidiomycota) and characterization of their compounds using HPLC–DAD and LC–ESI–MS/MS

Folia Microbiologica ◽

10.1007/s12223-021-00884-y ◽

2021 ◽

Author(s):

Samaneh Chaharmiri Dokhaharani ◽

Masoomeh Ghobad-Nejhad ◽

Hamid Moghimi ◽

Abbas Farazmand ◽

Hossein Rahmani

Keyword(s):

Biological Activities ◽

Esi Ms

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Synthesis and characterization of a series of N, N' ‐substituted urea derivatives by using electrospray ionization tandem mass spectrometry (ESI‐MS/MS): Differentiation of positional isomers

Rapid Communications in Mass Spectrometry ◽

10.1002/rcm.9161 ◽

2021 ◽

Author(s):

Dilip Kumar Singh ◽

Siddheshwar Kisan Chauthe ◽

Prakash Anjanappa ◽

Sumit Kumar ◽

Ruba A. Arulraj ◽

...

Keyword(s):

Mass Spectrometry ◽

Tandem Mass Spectrometry ◽

Electrospray Ionization ◽

Synthesis And Characterization ◽

Tandem Mass ◽

Positional Isomers ◽

Urea Derivatives ◽

Esi Ms ◽

Ionization Tandem Mass Spectrometry

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Spectroscopic (LC‐ESI‐MS/MS, FT‐IR, NMR) and functional characterization of fruit seed oils extracted with green technology: A comparative study with Prunus cerasus and Punica granatum oils

Journal of Food Processing and Preservation ◽

10.1111/jfpp.15451 ◽

2021 ◽

Author(s):

Bülent Başyiğit ◽

Hidayet Sağlam ◽

İbrahim Hayoğlu ◽

Mehmet Karaaslan

Keyword(s):

Comparative Study ◽

Functional Characterization ◽

Punica Granatum ◽

Green Technology ◽

Prunus Cerasus ◽

Seed Oils ◽

Esi Ms ◽

Ft Ir

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Proteomic Characterization of Bacteriophage Peptides from the Mastitis Producer Staphylococcus aureus by LC-ESI-MS/MS and the Bacteriophage Phylogenomic Analysis

Foods ◽

10.3390/foods10040799 ◽

2021 ◽

Vol 10 (4) ◽

pp. 799

Author(s):

Ana G. Abril ◽

Mónica Carrera ◽

Karola Böhme ◽

Jorge Barros-Velázquez ◽

Benito Cañas ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Dairy Products ◽

Phylogenomic Analysis ◽

Esi Ms ◽

Complement Inhibitors ◽

Staphylococcus Spp ◽

The Relationship ◽

Phage Proteins ◽

Identification And Characterization

The present work describes LC-ESI-MS/MS MS (liquid chromatography-electrospray ionization-tandem mass spectrometry) analyses of tryptic digestion peptides from phages that infect mastitis-causing Staphylococcus aureus isolated from dairy products. A total of 1933 nonredundant peptides belonging to 1282 proteins were identified and analyzed. Among them, 79 staphylococcal peptides from phages were confirmed. These peptides belong to proteins such as phage repressors, structural phage proteins, uncharacterized phage proteins and complement inhibitors. Moreover, eighteen of the phage origin peptides found were specific to S. aureus strains. These diagnostic peptides could be useful for the identification and characterization of S. aureus strains that cause mastitis. Furthermore, a study of bacteriophage phylogeny and the relationship among the identified phage peptides and the bacteria they infect was also performed. The results show the specific peptides that are present in closely related phages and the existing links between bacteriophage phylogeny and the respective Staphylococcus spp. infected.

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