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The long-standing perception of Protein Kinase C (PKC) as a family of oncoproteins has increasingly been challenged by evidence that some PKC isoforms may act as tumor suppressors. To explore the hypothesis that activation, rather than inhibition, of these isoforms is critical for anticancer activity, we isolated and characterized a family of 16 novel phorboids closely-related to tigilanol tiglate (EBC-46), a PKC-activating epoxytigliane showing promising clinical safety and efficacy for intratumoral treatment of cancers. While alkyl branching features of the C12-ester influenced potency, the 6,7-epoxide structural motif and position was critical to PKC activation in vitro. A subset of the 6,7-epoxytiglianes were efficacious against established tumors in mice; which generally correlated with in vitro activation of PKC. Importantly, epoxytiglianes without evidence of PKC activation showed limited antitumor efficacy. Taken together, these findings provide a strong rationale to reassess the role of PKC isoforms in cancer, and suggest in some situations their activation can be a promising strategy for anticancer drug discovery.

The preparation of a series of alkali-metal inclusion complexes of the molecular cube [{CoIII(Me3-tacn)}4{FeII(CN)6}4]4- (Me3-tacn = 1,4,7-trimethyl-1,4,7-triazacyclononane), a mixed-valent Prussian Blue analogue bearing bridging cyanido ligands, has been achieved by following a redox-triggered self-assembly process. The molecular cubes are extremely robust and soluble in aqueous media ranging from 5 M [H+] to 2 M [OH-]. All the complexes have been characterized by the standard mass spectometry, UV-vis, inductively coupled plasma, multinuclear NMR spectroscopy, and electrochemistry. Furthermore, X-ray diffraction analysis of the sodium and lithium salts has also been achieved, and the inclusion of moieties of the form {M-OH2}+ (M = Li, Na) is confirmed. These inclusion complexes in aqueous solution are rather inert to cation exchange and are characterized by a significant decrease in acidity of the confined water molecule due to hydrogen bonding inside the cubic cage. Exchange of the encapsulated cationic {M-OH2}+ or M+ units by other alkali metals has also been studied from a kineticomechanistic perspective at different concentrations, temperatures, ionic strengths, and pressures. In all cases, the thermal and pressure activation parameters obtained agree with a process that is dominated by differences in hydration of the cations entering and exiting the cage, although the size of the portal enabling the exchange also plays a determinant role, thus not allowing the large Cs+ cation to enter. All the exchange substitutions studied follow a thermodynamic sequence that relates with the size and polarizing capability of the different alkali cations; even so, the process can be reversed, allowing the entry of {Li-OH2}+ units upon adsorption of the cube on an anion exchange resin and subsequent washing with a Li+ solution.

CO dehydrogenase (CODH) from the Gram-negative bacterium Oligotropha carboxidovorans is a complex metalloenzyme from the xanthine oxidase family of molybdenum-containing enzymes, bearing a unique binuclear Mo-S-Cu active site in addition to two [2Fe-2S] clusters (FeSI and FeSII) and one equivalent of FAD. CODH catalyzes the oxidation of CO to CO2 with the concomitant introduction of reducing equivalents into the quinone pool, thus enabling the organism to utilize CO as sole source of both carbon and energy. Using a variety of EPR monitored redox titrations and spectroelectrochemistry, we report the redox potentials of CO dehydrogenase at pH 7.2 namely MoVI/V, MoV/IV, FeSI2+/+, FeSII2+/+, FAD/FADH and FADH/FADH-. These potentials are systematically higher than the corresponding potentials seen for other members of the xanthine oxidase family of Mo enzymes, and are in line with CODH utilising the higher potential quinone pool as an electron acceptor instead of pyridine nucleotides. CODH is also active when immobilised on a modified Au working electrode as demonstrated by cyclic voltammetry in the presence of CO.

CO dehydrogenase (CODH) from the Gram-negative bacterium Oligotropha carboxidovorans is a complex metalloenzyme from the xanthine oxidase family of molybdenum-containing enzymes, bearing a unique binuclear Mo-S-Cu active site in addition to two [2Fe-2S] clusters (FeSI and FeSII) and one equivalent of FAD. CODH catalyzes the oxidation of CO to CO2 with the concomitant introduction of reducing equivalents into the quinone pool, thus enabling the organism to utilize CO as sole source of both carbon and energy. Using a variety of EPR monitored redox titrations and spectroelectrochemistry, we report the redox potentials of CO dehydrogenase at pH 7.2 namely MoVI/V, MoV/IV, FeSI2+/+, FeSII2+/+, FAD/FADH and FADH/FADH-. These potentials are systematically higher than the corresponding potentials seen for other members of the xanthine oxidase family of Mo enzymes, and are in line with CODH utilising the higher potential quinone pool as an electron acceptor instead of pyridine nucleotides. CODH is also active when immobilised on a modified Au working electrode as demonstrated by cyclic voltammetry in the presence of CO.

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Bismuth-based organohalides have attracted much attention as potential alternatives to lead halide perovskites and have been explored in various electronic and optoelectronic devices. Developing new bismuth organohalides with rational design has been a dynamic research area. Herein, we developed single-crystals and thin-films of a new class of bismuth-based organohalides (phenethylammonium (C8H12N+, PEA+) bismuth halides). We found that comparable optical properties can be preserved after replacing methylammonium with bulky PEA+ cations. The bulky PEA+ cation significantly promotes the coverage and low surface roughness of bismuth organohalide thin-films in a facile one-step solution method. Newly-prepared (PEA)3Bi2I9 also shows excellent thermal and humidity stability, showing promise for addressing the toxicity and stability of optoelectronic/electronic devices beyond lead halide perovskites.

Contains fulltext : 204880.pdf (Publisher’s version ) (Open Access)

Contains fulltext : 204880.pdf (Publisher’s version ) (Open Access)

Herein, we report the electrocatalytic voltammetry of holo and heme-free human sulfite oxidase (HSO) mediated by the synthetic iron complexes 1,2-bis(1,4,7-triaza-1-cyclononyl)ethane iron(III) bromide, ([Fe(dtne)]Br-3.3H(2)O), potassium ferricyanide (K-3[Fe(CN)(6)]), and ferrocene methanol (FM) at a 5-(4-pyridinyl)-1,3,4-oxadiazole-2-thiol (Hpyt) modified gold working electrode. Holo HSO contains two electroactive redox cofactors, comprising a mostly negatively charged cyt b(5) (heme) domain and a Mo cofactor (Moco) domain (the site of sulfite oxidation), where the surface near the active site is positively charged. We anticipated different catalytic voltammetry based on either repulsive or attractive electrostatic interactions between the holo or heme-free enzymes and the positively or negatively charged redox mediators. Both holo and heme-free HSO experimental catalytic voltammetry has been modeled by using electrochemical simulation across a range of sweep rates and concentrations of substrate and both positive and negatively charged electron acceptors ([Fe(dtne)](3+), [Fe(CN)(6)](3-) and FM+), which provides new insights into the kinetics of the HSO catalytic mechanism. These mediator complexes have almost the same redox potential (all lying in the range +415 to +430mV vs. NHE) and, thus, deliver the same driving force for electron transfer with the Mo cofactor. However, differences in the electrostatic affinities between HSO and the mediator have a significant influence on the electrocatalytic response.

Direct electrochemistry of human sulfite oxidase (HSO) has been achieved on carboxylate-terminated self-assembled monolayers cast on a Au working electrode in the presence of the promoter chitosan. The modified electrode facilitates a well-defined nonturnover redox response from the heme cofactor (Fe-III/II) in 750 mM Tris, MOPS, and bicine buffer solutions. The formal redox potential of the nonturnover response varies slightly depending on the nature of the thiol monolayer on the Au electrode. Upon addition of sulfite to the cell a pronounced catalytic current from HSO-facilitated sulfite oxidation is observed. The measured catalytic rate constant (k(cat)) is around 0.2 s(-1) (compared with 26 s(-1) obtained from solution assays), which indicates that interaction of the enzyme with the electrode lowers overall catalysis although native behavior is retained in terms of substrate concentration dependence, pH dependence, and inhibition effects. In contrast, no catalytic activity is observed when HSO is confined to amine-terminated thiol monolayers although well-defined noncatalytic responses from the heme cofactor are still observed. These differences are linked to flexibility of HSO, which can switch between active and inactive conformations, and also competitive ion exchange processes at the electrode surface involving the enzyme and substrate.

Herein, we report the electrocatalytic voltammetry of holo and heme-free human sulfite oxidase (HSO) mediated by the synthetic iron complexes 1,2-bis(1,4,7-triaza-1-cyclononyl)ethane iron(III) bromide, ([Fe(dtne)]Br-3.3H(2)O), potassium ferricyanide (K-3[Fe(CN)(6)]), and ferrocene methanol (FM) at a 5-(4-pyridinyl)-1,3,4-oxadiazole-2-thiol (Hpyt) modified gold working electrode. Holo HSO contains two electroactive redox cofactors, comprising a mostly negatively charged cyt b(5) (heme) domain and a Mo cofactor (Moco) domain (the site of sulfite oxidation), where the surface near the active site is positively charged. We anticipated different catalytic voltammetry based on either repulsive or attractive electrostatic interactions between the holo or heme-free enzymes and the positively or negatively charged redox mediators. Both holo and heme-free HSO experimental catalytic voltammetry has been modeled by using electrochemical simulation across a range of sweep rates and concentrations of substrate and both positive and negatively charged electron acceptors ([Fe(dtne)](3+), [Fe(CN)(6)](3-) and FM+), which provides new insights into the kinetics of the HSO catalytic mechanism. These mediator complexes have almost the same redox potential (all lying in the range +415 to +430mV vs. NHE) and, thus, deliver the same driving force for electron transfer with the Mo cofactor. However, differences in the electrostatic affinities between HSO and the mediator have a significant influence on the electrocatalytic response.

Direct electrochemistry of human sulfite oxidase (HSO) has been achieved on carboxylate-terminated self-assembled monolayers cast on a Au working electrode in the presence of the promoter chitosan. The modified electrode facilitates a well-defined nonturnover redox response from the heme cofactor (Fe-III/II) in 750 mM Tris, MOPS, and bicine buffer solutions. The formal redox potential of the nonturnover response varies slightly depending on the nature of the thiol monolayer on the Au electrode. Upon addition of sulfite to the cell a pronounced catalytic current from HSO-facilitated sulfite oxidation is observed. The measured catalytic rate constant (k(cat)) is around 0.2 s(-1) (compared with 26 s(-1) obtained from solution assays), which indicates that interaction of the enzyme with the electrode lowers overall catalysis although native behavior is retained in terms of substrate concentration dependence, pH dependence, and inhibition effects. In contrast, no catalytic activity is observed when HSO is confined to amine-terminated thiol monolayers although well-defined noncatalytic responses from the heme cofactor are still observed. These differences are linked to flexibility of HSO, which can switch between active and inactive conformations, and also competitive ion exchange processes at the electrode surface involving the enzyme and substrate.

Mediated electrocatalytic voltammetry of human sulfite oxidase (HSO) is demonstrated with synthetic one electron transfer iron complexes bis(1,4,7-triazacyclononane)iron(III) ([Fe(tacn)(2)](3+)) and 1,2-bis (1,4,7-triaza-1-cyclononyl)ethane iron(III) ([Fe(dtne)](3+)) at a glassy carbon working electrode. The two synthetic electron acceptors for HSO, differing in redox potential by 270 mV, deliver different driving forces for electrocatalysis. Digital simulation of the catalytic voltammetry was achieved with single set of enzyme-dependent kinetic parameters that reproduced the experimental data across a range of sweep rates, and sulfite and mediator concentrations. Amperometry carried out in a stirred solution with the lower potential mediator [Fe(tacn)(2)](3+) was optimised and exhibited a linear increase in steady state current in the sulfite concentration range 5.0 x 10(-6) to 8.0 x 10(-4) M with a detection limit of 0.2 pM (S/N = 3). The HSO coupled electrode was successfully used for the determination of sulfite concentration in white wine and beer samples and the results validated with a standard spectrophotometric method. (C) 2016 Elsevier Ltd. All rights reserved.

Mediated electrocatalytic voltammetry of human sulfite oxidase (HSO) is demonstrated with synthetic one electron transfer iron complexes bis(1,4,7-triazacyclononane)iron(III) ([Fe(tacn)(2)](3+)) and 1,2-bis (1,4,7-triaza-1-cyclononyl)ethane iron(III) ([Fe(dtne)](3+)) at a glassy carbon working electrode. The two synthetic electron acceptors for HSO, differing in redox potential by 270 mV, deliver different driving forces for electrocatalysis. Digital simulation of the catalytic voltammetry was achieved with single set of enzyme-dependent kinetic parameters that reproduced the experimental data across a range of sweep rates, and sulfite and mediator concentrations. Amperometry carried out in a stirred solution with the lower potential mediator [Fe(tacn)(2)](3+) was optimised and exhibited a linear increase in steady state current in the sulfite concentration range 5.0 x 10(-6) to 8.0 x 10(-4) M with a detection limit of 0.2 pM (S/N = 3). The HSO coupled electrode was successfully used for the determination of sulfite concentration in white wine and beer samples and the results validated with a standard spectrophotometric method. (C) 2016 Elsevier Ltd. All rights reserved.

Nitrate reductase (NR) from the plant Arabidopsis thaliana has been employed in the development of an amperometric nitrate biosensor that functions at physiological pH. The anion anthraquinone-2-sulfonate (AQ) is used as an effective artificial electron transfer partner for NR at a glassy carbon (GC) electrode. Nitrate is enzymatically reduced to nitrite and the oxidized form of NR is electrochemically reduced by the hydroquinone form of the mediator (AQH(2)). The GC/NR electrode shows a pronounced cathodic wave for nitrate reduction and the catalytic current increases linearly in the nitrate concentration range of 10-400 A mu M with a correlation coefficient of 0.989. Using an amperometric method, a low detection limit of 0.76 nM (S/N = 3) was achieved. The practical application of the present electrochemical biosensor was demonstrated by the determination of nitrate concentration in natural water samples and the results agreed well with a standard spectroscopic method.

Nitrate reductase (NR) from the plant Arabidopsis thaliana has been employed in the development of an amperometric nitrate biosensor that functions at physiological pH. The anion anthraquinone-2-sulfonate (AQ) is used as an effective artificial electron transfer partner for NR at a glassy carbon (GC) electrode. Nitrate is enzymatically reduced to nitrite and the oxidized form of NR is electrochemically reduced by the hydroquinone form of the mediator (AQH(2)). The GC/NR electrode shows a pronounced cathodic wave for nitrate reduction and the catalytic current increases linearly in the nitrate concentration range of 10-400 A mu M with a correlation coefficient of 0.989. Using an amperometric method, a low detection limit of 0.76 nM (S/N = 3) was achieved. The practical application of the present electrochemical biosensor was demonstrated by the determination of nitrate concentration in natural water samples and the results agreed well with a standard spectroscopic method.

Nitrate reductase (NR) from the plant Arabidopsis thaliana has been employed in the development of an amperometric nitrate biosensor that functions at physiological pH. The anion anthraquinone-2-sulfonate (AQ) is used as an effective artificial electron transfer partner for NR at a glassy carbon (GC) electrode. Nitrate is enzymatically reduced to nitrite and the oxidized form of NR is electrochemically reduced by the hydroquinone form of the mediator (AQH(2)). The GC/NR electrode shows a pronounced cathodic wave for nitrate reduction and the catalytic current increases linearly in the nitrate concentration range of 10-400 A mu M with a correlation coefficient of 0.989. Using an amperometric method, a low detection limit of 0.76 nM (S/N = 3) was achieved. The practical application of the present electrochemical biosensor was demonstrated by the determination of nitrate concentration in natural water samples and the results agreed well with a standard spectroscopic method.

Nitrate reductase (NR) from the plant Arabidopsis thaliana has been employed in the development of an amperometric nitrate biosensor that functions at physiological pH. The anion anthraquinone-2-sulfonate (AQ) is used as an effective artificial electron transfer partner for NR at a glassy carbon (GC) electrode. Nitrate is enzymatically reduced to nitrite and the oxidized form of NR is electrochemically reduced by the hydroquinone form of the mediator (AQH(2)). The GC/NR electrode shows a pronounced cathodic wave for nitrate reduction and the catalytic current increases linearly in the nitrate concentration range of 10-400 A mu M with a correlation coefficient of 0.989. Using an amperometric method, a low detection limit of 0.76 nM (S/N = 3) was achieved. The practical application of the present electrochemical biosensor was demonstrated by the determination of nitrate concentration in natural water samples and the results agreed well with a standard spectroscopic method.

Analogues of the ligand 2,2′-(2-hydroxy-5-methyl-1,3-phenylene)bis(methylene)bis((pyridin-2-ylmethyl)azanediyl)diethanol (CH3H3L1) are described. Complexation of these analogues, 2,6-bis(((2-methoxyethyl)(pyridin-2-ylmethyl)amino)methyl)-4-methylphenol (CH3HL2), 4-bromo-2,6-bis(((2-methoxyethyl)(pyridin-2-ylmethyl)amino)methyl)phenol (BrHL2), 2,6-bis(((2-methoxyethyl)(pyridin-2-ylmethyl)amino)methyl)-4-nitrophenol (NO2HL2) and 4-methyl-2,6-bis(((2-phenoxyethyl)(pyridin-2-ylmethyl)amino)methyl)phenol (CH3HL3) with zinc(II) acetate afforded [Zn2(CH3L2)(CH3COO)2](PF6), [Zn2(NO2L2)(CH3COO)2](PF6), [Zn2(BrL2)(CH3COO)2](PF6) and [Zn2(CH3L3)(CH3COO)2](PF6), in addition to [Zn4(CH3L2)2(NO2C6H5OPO3)2(H2O)2](PF6)2 and [Zn4(BrL2)2(PO3F)2(H2O)2](PF6)2. The complexes were characterized using 1H and 13C NMR spectroscopy, mass spectrometry, microanalysis, and X-ray crystallography. The complexes contain either a coordinated methyl- (L2 ligands) or phenyl- (L3 ligand) ether, replacing the potentially nucleophilic coordinated alcohol in the previously reported complex [Zn2(CH3HL1)(CH3COO)(H2O)](PF6). Functional studies of the zinc complexes with the substrate bis(2,4-dinitrophenyl) phosphate (BDNPP) showed them to be competent catalysts with, for example, [Zn2(CH3L2)]+, kcat = 5.70 ± 0.04 × 10−3 s−1 (Km = 20.8 ± 5.0 mM) and [Zn2(CH3L3)]+, kcat = 3.60 ± 0.04 × 10−3 s−1 (Km = 18.9 ± 3.5 mM). Catalytically relevant pKas of 6.7 and 7.7 were observed for the zinc(II) complexes of CH3L2− and CH3L3−, respectively. Electron donating para-substituents enhance the rate of hydrolysis of BDNPP such that kcatp-CH3 > p-Br > p-NO2. Use of a solvent mixture containing H2O18/H2O16 in the reaction with BDNPP showed that for [Zn2(CH3L2)(CH3COO)2](PF6) and [Zn2(NO2L2)(CH3COO)2](PF6), as well as [Zn2(CH3HL1)(CH3COO)(H2O)](PF6), the 18O label was incorporated in the product of the hydrolysis suggesting that the nucleophile involved in the hydrolysis reaction was a Zn–OH moiety. The results are discussed

Analogues of the ligand 2,2′-(2-hydroxy-5-methyl-1,3-phenylene)bis(methylene)bis((pyridin-2-ylmethyl)azanediyl)diethanol (CH3H3L1) are described. Complexation of these analogues, 2,6-bis(((2-methoxyethyl)(pyridin-2-ylmethyl)amino)methyl)-4-methylphenol (CH3HL2), 4-bromo-2,6-bis(((2-methoxyethyl)(pyridin-2-ylmethyl)amino)methyl)phenol (BrHL2), 2,6-bis(((2-methoxyethyl)(pyridin-2-ylmethyl)amino)methyl)-4-nitrophenol (NO2HL2) and 4-methyl-2,6-bis(((2-phenoxyethyl)(pyridin-2-ylmethyl)amino)methyl)phenol (CH3HL3) with zinc(II) acetate afforded [Zn2(CH3L2)(CH3COO)2](PF6), [Zn2(NO2L2)(CH3COO)2](PF6), [Zn2(BrL2)(CH3COO)2](PF6) and [Zn2(CH3L3)(CH3COO)2](PF6), in addition to [Zn4(CH3L2)2(NO2C6H5OPO3)2(H2O)2](PF6)2 and [Zn4(BrL2)2(PO3F)2(H2O)2](PF6)2. The complexes were characterized using 1H and 13C NMR spectroscopy, mass spectrometry, microanalysis, and X-ray crystallography. The complexes contain either a coordinated methyl- (L2 ligands) or phenyl- (L3 ligand) ether, replacing the potentially nucleophilic coordinated alcohol in the previously reported complex [Zn2(CH3HL1)(CH3COO)(H2O)](PF6). Functional studies of the zinc complexes with the substrate bis(2,4-dinitrophenyl) phosphate (BDNPP) showed them to be competent catalysts with, for example, [Zn2(CH3L2)]+, kcat = 5.70 ± 0.04 × 10−3 s−1 (Km = 20.8 ± 5.0 mM) and [Zn2(CH3L3)]+, kcat = 3.60 ± 0.04 × 10−3 s−1 (Km = 18.9 ± 3.5 mM). Catalytically relevant pKas of 6.7 and 7.7 were observed for the zinc(II) complexes of CH3L2− and CH3L3−, respectively. Electron donating para-substituents enhance the rate of hydrolysis of BDNPP such that kcatp-CH3 > p-Br > p-NO2. Use of a solvent mixture containing H2O18/H2O16 in the reaction with BDNPP showed that for [Zn2(CH3L2)(CH3COO)2](PF6) and [Zn2(NO2L2)(CH3COO)2](PF6), as well as [Zn2(CH3HL1)(CH3COO)(H2O)](PF6), the 18O label was incorporated in the product of the hydrolysis suggesting that the nucleophile involved in the hydrolysis reaction was a Zn–OH moiety. The results are discussed

The bicyclic hexaamine "cage" ligand Me 8tricosaneN 6 (1,5,5,9,13,13,20,20-octamethyl-3,7,11,15,18, 22-hexaazabicyclo[7.7.7]tricosane) is capable of encapsulating octahedral metal ions, yet its expanded cavity allows the complexed metal to adopt a variety of geometries comprising either hexadentate or pentadentate coordination of the ligand. When complexed to Cu II the lability of the metal results in a dynamic equilibrium in solution between hexadentate- and pentadentate- coordinated complexes of Me 8tricosaneN 6. Both [Cu(Me 8tricosaneN 6)](ClO 4) 2 (6-coordinate) and [Cu(Me 8tricosaneN 6)](S 2O 6) (5-coordinate) have been characterized structurally. In weak acid (pH 1) a singly protonated complex [Cu(HMe 8tricosaneN 6)] 3+ has been isolated that finds the ligand binding as a pentadentate with the uncoordinated amine being protonated. vis-NIR and electron paramagnetic resonance (EPR) spectroscopy show that the predominant solution structure of [Cu(Me 8tricosaneN 6)] 2+ at neutral pH comprises a five-coordinate, square pyramidal complex. Cyclic voltammetry of the square pyramidal [Cu(Me 8tricosaneN 6)] 2+ complex reveals a reversible Cu II/I couple. All of these structural, spectroscopic, and electrochemical features contrast with the smaller cavity and well studied "sarcophagine" (sar, 3,6,10,13,16,19-hexaazabicyclo[6.6. 6]eicosane) Cu II complexes which are invariably hexadentate coordinated in neutral solution and cannot stabilize a Cu I form. 2011 American Chemical Society.

The bicyclic hexaamine "cage" ligand Me 8tricosaneN 6 (1,5,5,9,13,13,20,20-octamethyl-3,7,11,15,18, 22-hexaazabicyclo[7.7.7]tricosane) is capable of encapsulating octahedral metal ions, yet its expanded cavity allows the complexed metal to adopt a variety of geometries comprising either hexadentate or pentadentate coordination of the ligand. When complexed to Cu II the lability of the metal results in a dynamic equilibrium in solution between hexadentate- and pentadentate- coordinated complexes of Me 8tricosaneN 6. Both [Cu(Me 8tricosaneN 6)](ClO 4) 2 (6-coordinate) and [Cu(Me 8tricosaneN 6)](S 2O 6) (5-coordinate) have been characterized structurally. In weak acid (pH 1) a singly protonated complex [Cu(HMe 8tricosaneN 6)] 3+ has been isolated that finds the ligand binding as a pentadentate with the uncoordinated amine being protonated. vis-NIR and electron paramagnetic resonance (EPR) spectroscopy show that the predominant solution structure of [Cu(Me 8tricosaneN 6)] 2+ at neutral pH comprises a five-coordinate, square pyramidal complex. Cyclic voltammetry of the square pyramidal [Cu(Me 8tricosaneN 6)] 2+ complex reveals a reversible Cu II/I couple. All of these structural, spectroscopic, and electrochemical features contrast with the smaller cavity and well studied "sarcophagine" (sar, 3,6,10,13,16,19-hexaazabicyclo[6.6. 6]eicosane) Cu II complexes which are invariably hexadentate coordinated in neutral solution and cannot stabilize a Cu I form. 2011 American Chemical Society.

The bicyclic hexaamine "cage" ligand Me 8tricosaneN 6 (1,5,5,9,13,13,20,20-octamethyl-3,7,11,15,18, 22-hexaazabicyclo[7.7.7]tricosane) is capable of encapsulating octahedral metal ions, yet its expanded cavity allows the complexed metal to adopt a variety of geometries comprising either hexadentate or pentadentate coordination of the ligand. When complexed to Cu II the lability of the metal results in a dynamic equilibrium in solution between hexadentate- and pentadentate- coordinated complexes of Me 8tricosaneN 6. Both [Cu(Me 8tricosaneN 6)](ClO 4) 2 (6-coordinate) and [Cu(Me 8tricosaneN 6)](S 2O 6) (5-coordinate) have been characterized structurally. In weak acid (pH 1) a singly protonated complex [Cu(HMe 8tricosaneN 6)] 3+ has been isolated that finds the ligand binding as a pentadentate with the uncoordinated amine being protonated. vis-NIR and electron paramagnetic resonance (EPR) spectroscopy show that the predominant solution structure of [Cu(Me 8tricosaneN 6)] 2+ at neutral pH comprises a five-coordinate, square pyramidal complex. Cyclic voltammetry of the square pyramidal [Cu(Me 8tricosaneN 6)] 2+ complex reveals a reversible Cu II/I couple. All of these structural, spectroscopic, and electrochemical features contrast with the smaller cavity and well studied "sarcophagine" (sar, 3,6,10,13,16,19-hexaazabicyclo[6.6. 6]eicosane) Cu II complexes which are invariably hexadentate coordinated in neutral solution and cannot stabilize a Cu I form. 2011 American Chemical Society.

The bicyclic hexaamine "cage" ligand Me 8tricosaneN 6 (1,5,5,9,13,13,20,20-octamethyl-3,7,11,15,18, 22-hexaazabicyclo[7.7.7]tricosane) is capable of encapsulating octahedral metal ions, yet its expanded cavity allows the complexed metal to adopt a variety of geometries comprising either hexadentate or pentadentate coordination of the ligand. When complexed to Cu II the lability of the metal results in a dynamic equilibrium in solution between hexadentate- and pentadentate- coordinated complexes of Me 8tricosaneN 6. Both [Cu(Me 8tricosaneN 6)](ClO 4) 2 (6-coordinate) and [Cu(Me 8tricosaneN 6)](S 2O 6) (5-coordinate) have been characterized structurally. In weak acid (pH 1) a singly protonated complex [Cu(HMe 8tricosaneN 6)] 3+ has been isolated that finds the ligand binding as a pentadentate with the uncoordinated amine being protonated. vis-NIR and electron paramagnetic resonance (EPR) spectroscopy show that the predominant solution structure of [Cu(Me 8tricosaneN 6)] 2+ at neutral pH comprises a five-coordinate, square pyramidal complex. Cyclic voltammetry of the square pyramidal [Cu(Me 8tricosaneN 6)] 2+ complex reveals a reversible Cu II/I couple. All of these structural, spectroscopic, and electrochemical features contrast with the smaller cavity and well studied "sarcophagine" (sar, 3,6,10,13,16,19-hexaazabicyclo[6.6. 6]eicosane) Cu II complexes which are invariably hexadentate coordinated in neutral solution and cannot stabilize a Cu I form. 2011 American Chemical Society.

Dinuclear class II Co-III/Fe-II mixed-valence complexes of type [LnCo (III)(mu-NC) Fe-II(CN)(3)L-2](m-) (where L-n represents a pentadentate macrocycle and L-2 a bpy ligand or two cyanides) have electronic properties that make them possible sensitizers in DSSC ( dye sensitized solar cells). For this purpose the new complex Na-2[{trans-L14COOCo III( m-NC)} Fe II( CN) 5] has been prepared and characterized by the usual methods and its sensitizer properties compared with those of the already known [{trans-L14COOCo (III)(mu-NC)}Fe-II(CN)(5)](2-)(CN)(3)(bipy)(eq,ax)](ClO4). The complex [{trans-L14COOCo (III)(mu-NC)}Fe-II(CN)(5)](2-) has been designed for the actuation of an electron injection from the cobalt centre on MMCT, while the [{trans-L14COOCo (III)(mu-NC)}Fe-II(CN)(3)(bipy)](+) structure can produce a tuned injection from the iron centre via an MLCT electronic state, as described for similar systems. The characterization on solid oxide semiconductor supports has been carried out for these two complexes and the results have been compared with the behaviour observed in aqueous solution and in solvents of varying polarities. Their use in DSSC has been checked and, while a sensitizer response is observed for [{trans-L14COOCo (III)(mu-NC)}Fe-II(CN)(5)](2-), complex [{trans-L14COOCoIII(mu-NC)}Fe-II(CN)(3)(bipy)(eq,ax)](+) does not produce any electrical current on illumination. The low efficiency of the built DSSC can be easily related both with the very low value of the extinction coefficient of the MMCT band responsible for the electron injection, and with the small driving force for the reduction of the complex with the standard I-2/I-3 (-) system used after electron injection., QC 20100525

End game synthetic strategy studies towards the total synthesis of the vibsanin type diterpenes, vibsanin E, 3-hydroxyvibsanin E, furanovibsanin A, and 3-O-methylfuranovibsanin A are discussed, with focus on construction of the side chain and peripheral functionality associated with this group of natural products is the current focus of this report.

The luminescence lifetimes (in CH 3CN at room temperature) and electrochemical potentials (in CH 3CN) of a range of mono- and bis(bidentate) 2,2′-bipyridine-capped oligothiophene-bridged Ru II complexes based on the 6-(2-thienyl)-2,2′-bipyridine and 4-(2-thienyl)-2,2′-bipyridine motifs have been measured. The redox potentials occurred in a very narrow range and showed only small shifts from that of [Ru(bpy) 3] 2+, which indicates that the inductive effects of the substituents on the 2,2′-bipyridine ligands are very similar across this series. In the complexes that incorporated a bithiophene moiety the oxidation of the bithienyl group occurred at higher potentials than the metal-centered Ru III/II oxidation. No or very weak interaction between the metal cores in the dinuclear complexes was observed. It was found that the luminescence lifetimes of the complexes where the attachment point of the oligothiophene bridge is in the 4-position of a 2,2′-bipyridine ligand were extended compared to [Ru(bpy) 3] 2+, whereas the luminescence was very short-lived (<30 ns) or completely quenched in the complexes where the oligothiophene bridge was attached in the 6-position. The difference in lifetimes is probably due to steric interactions between the thienyl bridge and the auxiliary bipyridyl ligands, resulting in disturbances in coordination symmetry of the metal core.

Cyclic voltammetry of the non-heme diiron enzyme porcine purple acid phosphatase (uteroferrin, Uf) has been reported for the first time. Totally reversible one-electron oxidation responses (FeIII-FeII f FeIII-FeIII) are seen both in the absence and in the presence of weak competitive inhibitors phosphate and arsenate, and dissociation constants of these oxoanion complexes formed with uteroferrin in its oxidized state (Ufo) have been determined. The effect of pH on the redox potentials has been investigated in the range 3 < pH < 6.5, enabling acid dissociation constants for Ufo and its phosphate and arsenate complexes to be calculated.

Cyclic voltammetry of the non-heme diiron enzyme porcine purple acid phosphatase (uteroferrin, Uf) has been reported for the first time. Totally reversible one-electron oxidation responses (FeIII-FeII f FeIII-FeIII) are seen both in the absence and in the presence of weak competitive inhibitors phosphate and arsenate, and dissociation constants of these oxoanion complexes formed with uteroferrin in its oxidized state (Ufo) have been determined. The effect of pH on the redox potentials has been investigated in the range 3 < pH < 6.5, enabling acid dissociation constants for Ufo and its phosphate and arsenate complexes to be calculated.

The tridentate thienopyridines 5-phenyl-7-(pyridin-2-yl)thieno[2,3-c]pyridine (L1), 7-(pyridin-2-yl)-5-(thiophen-2-yl)thieno[2,3-c]pyridine (L2) and 5,7-di(pyridin-2-yl)thieno[2,3-c]pyridine (L3) have been synthesized via the Hurtley reaction. L1 and L2 were synthesized by condensing 3-bromothiophene-2-carboxylic acid with phenyl-1,3-butanedione and 1-thienyl-1,3-butanedione respectively. L3 was synthesized by condensing 3-bromothiophene-2- carboxylic acid with benzoylacetonitrile. Ring closure and a subsequent Negishi or Stille cross-coupling afforded L1, L2 and L3 in an overall yield of 20%, 3% and 6% respectively. The corresponding [Ru(tpy)L]n+ complexes were prepared and their electrochemical and structural properties were examined., Molekylär elektronik

A number of [Ru(tpy)L] complexes (where L is a ligand based on the 6-thien-2-yl-2,2’-bipyridine motif) have been generated to study the ability of this terdentate motif to switch between a N,N,C and a N,N,S binding mode as a function of pH and irradiation. Whilst the parent system 6-thien-2-yl-2,2’-bipyridine (1) displayed facile switching between the orange and purple forms, heavier analogues displayed sluggish switching – most likely resulting from a large moment of inertia about the bond between the S/C-bonded thiophene ring and the chelating bipyridine unit. Prototypic unsymmetrical bimetallic complexes (C7S and C7C) have been generated in order to test if the binding mode of the switching unit can affect the oxidation potential of the remote [Ru(bpy)2(L)] unit. The results of cyclic voltammetry studies suggest that only weak electronic coupling between the metal cores exists, and that the coordination mode (N,N,C or N,N,S) of the thiophene moiety only has a small effect on the oxidation potential of the [Ru(bpy)2(L)] unit.

Two new bis-terdentate ligands, 3,8-bis-(6-thiophen-2-yl-pyridin-2-yl)-[4,7]phenanthroline (L1) and 2,6-bis(6-(thiophen-2-yl)pyridin-2-yl)-1,5-naphthyridine (L2), capable of reversible double cyclometallation have been synthesized. Both syntheses proceeded via a Skraup synthesis followed by Stille cross-coupling with 2-thiophen-2-yl-6-tributylstannylpyridine to yield the final product. The Ru2(tpy)2-complex of L1 was shown to be capable of reversible cyclometallation, where the bis-cyclometallated (C,C) isomer of the complex had an oxidation potential of +249 mV while the oxidation potential of the doubly S-coordinated (S,S) complex was +987 mV. No ground state interaction between the Ru cores was however found. In theory the complex should display a third, mixed, state. An S,C-coordinated isomer would open the way for molecular electronic applications based on ternary logic. However, despite attempts the S,C-coordinated complex could not be generated., Molekylär elektronik