Structure of calcium nitroprusside tetrahydrate

Punte, G.; Rigotti, G.; Rivero, B. E.; Podjarny, A.; Castellano, Eduardo E.

doi:10.1107/s0567740880006309

Cited by 15 publications

(3 citation statements)

References 14 publications

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“…Absorption spectra of CC2DNB and CC3 DNB were recorded in 100 m M HEPES buffer (pH 7.4, Figure 2 a) and methanol (Figure 2 b), and compared with those of CCDNB under similar conditions. The reported absorption maxima of 348 nm for free N ‐ethyl‐substituted 2,4‐dinitroaniline8 and of 362 nm for 1‐(methylthio)‐2,4‐dinitrobenzene9 in methanol are quite similar to the observed absorption peaks at 350 nm in methanol for the synthesized probes containing the DNB part. In aqueous buffer, the absorption maxima for the coumarin and DNB parts of both CCDNB and CC2DNB were observed at 407 nm and 375 nm, respectively.…”

Section: Fluorescence Quantum Yields Of the Synthesized Probes In Bufsupporting

confidence: 68%

Fluorogenic Protein Labeling through Photoinduced Electron Transfer‐Based BL‐Tag Technology

Sadhu

Mizukami

Lanam

et al. 2011

Chemistry An Asian Journal

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In recent years, protein labeling has been routinely performed with various fluorescent markers. [1] The labeling of proteins allows monitoring of the specific location, movement, and interaction of proteins with other intracellular components using fluorescence microscopy. [2] For several decades, the labeling strategy mostly dealt with green fluorescent protein (GFP) and its variants. In order to overcome the unaltered fluorescent property and uncontrolled expression time of GFP, small molecular probe-based labeling approaches for live-cell imaging methods have been developed. [3] However, most of the reported small-molecule labeling probes do not show different fluorescence properties for the labeled and unlabeled states. Fluorescein-based arsenical hairpin binder (FlAsH) and resorufin-based arsenical hairpin binder (ReAsH) are the pioneer techniques for fluorogenic protein labeling with small molecular probes. [4] In our earlier studies, we developed a site-specific protein labeling technique that employs a genetically modified blactamase (BL-tag). [5] Mutation at a specific position in TEM-1 (class A b-lactamases) provides turn-on fluorogenic biosensors involving a b-lactam ring. The reaction of wildtype TEM-1 (WT TEM) with the b-lactam moiety involves acylation and deacylation steps. [6] We have utilized the BLtag protein for covalent attachment with a substrate. Despite the similar molecular weights of the BL-tag and GFP, fluorogenicity can be introduced only through the BL-tag technology.We have developed a fluorogenic mechanism based on aggregation-elimination processes for highly selective protein labeling with a fluorophore of desired color using the BLtag technology. We have also shown a broad applicability of dinitrobenzene (DNB) as a quencher. [5c,d] However, the limitation of the technology is a slow fluorogenic response of the synthesized probes such as CCDNB, which carries a coumarin fluorophore moiety, a cephalosporin moiety, and DNB (Figure 1). The necessary incubation time for a cell imaging experiment using CCDNB was 60 minutes. To reduce the incubation time for the imaging experiments, we aimed at developing more sophisticated probes that possess the DNB quencher. Herein, we report two newly designed probes with shorter linkers compared to those of CCDNB. In addition, we modified slightly the quencher in one probe. The probe with the modified quencher showed a comparatively fast fluorogenicity in vitro and in live-cell imaging studies. Fluorescence lifetime measurements indicated a different quenching mechanism for the most active probe. A detailed analysis of this new fluorogenic mechanism revealed a photoinduced electron transfer (PET) process [7] from the fluorophore donor to the quencher acceptor.The two new probes CC2 DNB and CC3 DNB that have a comparatively short or no linker between the b-lactam and quencher, respectively, are depicted in Figure 1. 2-(2-Aminoethoxy)ethanamine was used as the linker between the cephalosporin part and the DNB quencher in CC2 DNB. A coumarin deri...

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Section: Fluorescence Quantum Yields Of the Synthesized Probes In Bufsupporting

confidence: 68%

Fluorogenic Protein Labeling through Photoinduced Electron Transfer‐Based BL‐Tag Technology

Sadhu

Mizukami

Lanam

et al. 2011

Chemistry An Asian Journal

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“…Aymonino, Baran, Gentil, Lanfranconi & Varetti, 1976;Castellano, Piro & Rivero, 1977a,b;Castellano, Piro, Podjarny, Rivero, Aymonino, Lesk & Varetti, 1978;Punte, Rigotti, Rivero, Podjarny & Castellano, 1980). Crystals were obtained by slow evaporation from an aqueous solution.…”

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confidence: 99%

Structure of thallium nitroprusside

Rigotti¹,

Punte²,

Rivero³

et al. 1980

Acta Crystallogr Sect B

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“…The six ligands around the Fe-atom are arranged in a distorted octahedral coordination like in other nitroprussides (Castellano et al, 1977;Lanfranconi et al, 1973;Manoharan and Hamilton, 1963;Punte et al, 1980). The four equatorial CN groups emerge slightly from the plane perpendicular to the Fe -NO axis by an amount of 4.3° (in average) towards the fifth CN group (see Table 2).…”

Section: Discussionmentioning

confidence: 87%

Crystal structure of barium nitrosylpentacyanoferrat(III) 6.5 water, Ba[Fe(NO)(CN)₅] 6.5H₂O

Klüfers¹,

Haussühl²

1985

Zeitschrift Für Kristallographie - Crystalline Materials

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Ba[Fe(NO)(CN) s ]-6.5 H z O crystallizes in the polar space group Cmc2 1 with a = 1603.9(6), b = 1153.9(6), c = 1669.6(6) pm, Z=8. The nitroprusside anion exhibits nearly octahedral symmetry as known from other nitroprussides. Ba(l) is coordinated by 5 H 2 0 and 4 CN, Ba(2) by 8 H 2 0 and 2 CN. The NO group exhibits no bond to barium or to water molecules. All NO vectors are inclined towards the polar 2 l axis by ca. 62°.

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Structure of calcium nitroprusside tetrahydrate

Cited by 15 publications

References 14 publications

Fluorogenic Protein Labeling through Photoinduced Electron Transfer‐Based BL‐Tag Technology

Fluorogenic Protein Labeling through Photoinduced Electron Transfer‐Based BL‐Tag Technology

Structure of thallium nitroprusside

Crystal structure of barium nitrosylpentacyanoferrat(III) 6.5 water, Ba[Fe(NO)(CN)₅] 6.5H₂O

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Structure of calcium nitroprusside tetrahydrate

Cited by 15 publications

References 14 publications

Fluorogenic Protein Labeling through Photoinduced Electron Transfer‐Based BL‐Tag Technology

Fluorogenic Protein Labeling through Photoinduced Electron Transfer‐Based BL‐Tag Technology

Structure of thallium nitroprusside

Crystal structure of barium nitrosylpentacyanoferrat(III) 6.5 water, Ba[Fe(NO)(CN)5] 6.5H2O

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Crystal structure of barium nitrosylpentacyanoferrat(III) 6.5 water, Ba[Fe(NO)(CN)₅] 6.5H₂O