52674-29-0Relevant academic research and scientific papers
Proton-induced reactivity of NO- from a {CoNO}8 complex
Rhine, Melody A.,Rodrigues, Andria V.,Urbauer, Ramona J. Bieber,Urbauer, Jeffrey L.,Stemmler, Timothy L.,Harrop, Todd C.
, p. 12560 - 12563 (2014)
Research on the one-electron reduced analogue of NO, namely nitroxyl (HNO/NO-), has revealed distinguishing properties regarding its utility as a therapeutic. However, the fleeting nature of HNO requires the design of donor molecules. Metal nit
Reactions of Hydroxylamine with Metal Porphyrins
Choi, In-Kyu,Liu, Yanming,Wei, Zhongcheng,Ryan, Michael D.
, p. 3113 - 3118 (1997)
The reaction of hydroxylamine with a series of metal porphyrins was examined in methanol/chloroform media. The reductive nitrosylation reaction was observed for the manganese and iron porphyrins, leading to a nitrosyl complex that precipitated out of the solution in good isolatable yield (80-90%). This reaction could be used synthetically for the generation of iron and manganese porphyrin nitrosyl complexes and was particularly useful for making isotopically labeled nitrosyl complexes. On the other hand, CoII(TPP) and Cr(TPP)(CI) did not react with hydroxylamine under anaerobic conditions. With trace amounts of oxygen, the reaction of CoII(TPP) with hydroxylamine led to the formation of a stable cobalt(III)-bis(hydroxylamine) complex. The infrared, resonance Raman, and proton NMR spectra were consistent with a cobalt(III)-bis(hydroxylamine) complex. The cyclic voltammetry and visible spectroelectrochemistry of this complex were examined. The one-electron reduction of CoIII(TPP)(NH2OH)2+ formed CoIII(TPP), for which there was no evidence for the coordination of hydroxylamine. Further reduction led to CoI(.TPP)-, which reacted with the halogenated solvent to form a cobalt-alkyl complex. The difference in the reactivity of these four metal porphyrins with hydroxylamine correlated well with their E1/2 values. Iron(III) and manganese(III) porphyrins were relatively easy to reduce and readily underwent the reductive nitrosylation reaction, while cobalt(II) and chromium(III) porphyrins are unreactive. The one-electron oxidation of the hydroxylamine complex with a M(IIT) porphyrin would be expected to oxidize the N-atom in the coordinated hydroxylamine. The oxidation of MIII(NH2OH) with the loss of a proton would form MII(NIH2O)+ by an internal electron transfer, which will eventually lead to M(NO). The relationship between the reductive nitrosyl reaction and the enzymatic interconversion of NO and hydroxylamine was discussed.
Tetragonal to triclinic - A phase change for [Fe(TPP)(NO)]
Silvernail, Nathan J.,Olmstead, Marilyn M.,Noll, Bruce C.,Robert Scheldt
, p. 971 - 977 (2009)
The temperature dependence of the crystalline phase of (nitrosyl) (tetraphenylporphinato)iron(II), [Fe(TPP)(NO)], has been explored over the temperature range of 33-293 K. The crystalline complex is found in the tetragonal crystal system at higher tempera
Synthesis, characterization, and binding affinity of hydrosulfide complexes of synthetic iron(II) porphyrinates
Meininger, Daniel J.,Arman, Hadi D.,Tonzetich, Zachary J.
, p. 142 - 149 (2017)
The binding and reactivity of the hydrosulfide ion (HS?) to iron(II) porphyrinates has been examined for several synthetic meso-tetraphenylporphine (TPP) derivatives. In all cases, HS? coordinates to the iron centers in a 1:1 stoichiometry with formation constants (Kf) that reflect the electronic characteristics of the porphyrinate ligands. In the case of the F8TPP ligand (F8TPP?=?dianion of 5,10,15,20-tetrakis(2,6-difluorophenyl)porphine), an intermediate complex proposed as the hydrosulfide bridged dimer, (Bu4N)[Fe2(μ-SH)(F8TPP)2], was identified by NMR spectroscopy en route to formation of (Bu4N)[Fe(SH)(F8TPP)]. A robust procedure is reported for the synthesis and isolation of the parent hydrosulfide adduct, (Bu4N)[Fe(SH)(TPP)], which has permitted a detailed examination of its spectroscopy and chemical reactivity. Electrochemical measurements demonstrate that [Fe(SH)(TPP)]? is oxidized reversibly at a potential of ??0.832?V (vs ferrocene/ferrocenium) consistent with other iron porphyrinates containing sulfur-based ligands. Despite this fact, chemical oxidation of (Bu4N)[Fe(SH)(TPP)] with ferrocenium tetrafluoroborate produced only [Fe(TPP)] indicating that the putative iron(III) hydrosulfide adduct, [Fe(SH)(TPP)], decomposes rapidly. Treatment of (Bu4N)[Fe(SH)(TPP)] with other biologically relevant molecules such as NO and 1,2-dimethylimidazole resulted in simple displacement of the HS? ligand as governed by the relative Kf values of the added ligands. The solid-state structure of one hydrosulfide adduct, (Bu4N)[Fe(SH)(F8TPP)], was determined by X-ray crystallography and found to display the expected five-coordinate geometry about iron with an Fe-S distance of 2.323(1) ?. The relevance of the hydrosulfide chemistry with synthetic iron porphyrinates is discussed in terms of the possible reactivity for H2S and its derivatives at heme sites in biology.
Direct observation of nitrosylated heme in myoglobin and hemoglobin by electrospray ionization mass spectrometry
Upmacis, Rita K.,Hajjar, David P.,Chait, Brian T.,Mirza, Urooj A.
, p. 10424 - 10429 (1997)
Using electrospray ionization mass spectrometry (ESI-MS), we demonstrate the direct observation of NO attached to the heme moiety in;horse heart myoglobin (Mb) and in the α- and β-chains of human hemoglobin (Hb). It was found that a narrow range of ESI-MS conditions conspire to make observation of Fe-NO interactions challenging, and this is presumably the reason why earlier attempts by other research groups to detect intact Fe-NO products by mass spectrometry were unsuccessful For Mb and Hb, mass shifts are observed that are consistent with NO modification of the hemoproteins. ESI mass spectra of the apoprotein portions of Mb and Hb in the presence of NO demonstrated the absence of NO modification of the polypeptide backbones. UV/vis spectra of both Mb/NO and Hb/NO solutions, recorded at the time of ESI-MS analysis, demonstrated hemoprotein(II)-NO formation. To test the hypothesis that intact nitrosylated heme groups are observable by ESI-MS, a nitrosylated model metalloporphyrin was studied. The ESI mass spectrum of nitrosyl-α,β,γ,δ-tetraphenylporphinatoiron(II), [Fe(TPP)NO], showed peaks that were ascribed to [Fe(TPP)]+ and [Fe(TPP)NO]+. To test further our hypothesis that the hemoprotein-NO peaks are due to heme nitrosylation and contain no significant contributions from NO modification of the polypeptide backbone, we determined the ESI-MS conditions necessary for observing S-nitrosation of Cys residues in Hb. Human Hb contains one Cys residue in Hb(α) (Cys 104) and two Cys residues in Hb(β), but only Hb(β) Cys 93 is surface accessible. When metHb was incubated with S-nitroso-N-acetyl-DL-penicillamine (SNAP), the ESI mass spectrum revealed a single SNAP modification in both Hb(β) and apoHb(β). The ESI-MS conditions used for analyzing the Hb/SNAP solution were too harsh for observing intact heme nitrosylation, and thus, we ascribe the SNAP-modified Hb(β) and apoHb(β) peaks to S-nitrosation of Cys 93 in Hb(β). Under appropriate denaturing sample conditions, it proved possible to S-nitrosate all three Cys residues in human apoHb. pur findings demonstrate that (once correct conditions are established) ESI-MS is a powerful tool for the detection of intact Fe-NO interactions in proteins and porphyrins.
Comparative IR study of nitric oxide reactions with sublimed layers of iron(II)- and ruthenium(II)-meso-tetraphenylporphyrinates
Kurtikyan, Tigran S.,Martirosyan, Garik G.,Lorkovic, Ivan M.,Ford, Peter C.
, p. 10124 - 10129 (2002)
The interactions of nitric oxide gas with thin layers of FeII(TPP) and RuII(TPP), obtained by sublimation onto low-temperature substrate (77 K), has been investigated by means of IR spectroscopy (TPP = meso-tetraphenylporphyrinate).
To Transfer or Not to Transfer? Development of a Dinitrosyl Iron Complex as a Nitroxyl Donor for the Nitroxylation of an FeIII-Porphyrin Center
Tseng, Yu-Ting,Chen, Chien-Hong,Lin, Jing-Yu,Li, Bing-Han,Lu, Yu-Huan,Lin, Chia-Her,Chen, Hsin-Tsung,Weng, Tsu-Chien,Sokaras, Dimosthenes,Chen, Huang-Yeh,Soo, Yun-Liang,Lu, Tsai-Te
, p. 17570 - 17573 (2015)
A positive myocardial inotropic effect achieved using HNO/NO-, compared with NO· triggered attempts to explore novel nitroxyl donors for use in clinical applications in vascular and myocardial pharmacology. To develop M-NO complexes for nitroxy
Substituent Effects on the Electronic Absorption and MCD Spectra of Five- and Six-Coordinate Nitrosyl(tetraphenylporphyrinato)iron(II) Complexes
Yoshimura, Tetsuhiko
, p. 3689 - 3691 (1990)
Electronic absorption and MCD spectra of five- and six-coordinate nitrosyl iron(II) complexes of a series of tetrakis(para-substituted phenyl)porphyrins have been investigated in order to elucidate the cis-effect of para-substituents.The MCD spectroscopy was more sensitive to the substituent effect than the electronic absorption spectroscopy.
High-pressure infrared spectroscopic study of the nitric oxide complex of iron(II)-meso-tetraphenyl porphyrinate
Prémont-Schwarz, Mirabelle,Bohle, D. Scott,Gilson, Denis F.R.
, p. 3089 - 3091 (2006)
The infrared spectrum of iron(II)-meso-tetraphenylporphyrinate (FeTPP(NO)) has been measured as a function of pressure up to 3.1 GPa. The N-O stretching frequency decreases with increasing pressure, as expected for the bonding model for nitric oxide bound to iron in porphyrin complexes. Other peaks in the spectrum show positive pressure dependence.
Experimental and density functional theoretical investigations of linkage isomerism in six-coordinate {FeNO}6 iron porphyrins with axial nitrosyl and nitro ligands
Novozhilova, Irina V.,Coppens, Philip,Lee, Jonghyuk,Richter-Addo, George B.,Bagley, Kimberly A.
, p. 2093 - 2104 (2006)
A critical component of the biological activity of NO and nitrite involves their coordination to the iron center in heme proteins. Irradiation (330 2) (TPP = tetraphenylporphyrinato d
