Synthesis and reactions of [M(CO)4(Ph2PSiMe3)X] complexes (M = Mn,Re; X = Halogen)

The silylphosphine ligand Ph₂PSiMe₃ reacts readily with a slurry of [Re(CO)₅X] (X  Cl, Br) in polar and in non-polar solvents to yield soluble cis-[Re(CO)₄- (Ph₂PSiMe₃)X] (Ia, X  Cl;Ib, X  Br) via CO substitution. Compound I is readily hydrolyzed by water or silica gel to cis-[Re(CO)₄(Ph₂PH)X]. Compound Ib reacts with [Re(CO)₅Br] to yield [Re₂(CO)₈(μ-PPh₂)- (μ-Br)] (II), and with [Mn(CO)₅Br] to yield [MnRe- (CO)₈(μ-PPh₂)(μ-Br)] (III).The reaction of Ph₂PSiMe₃ with [Mn(CO)₅X] (X=Cl,Br,I) is highly dependent upon reaction conditions.In polar and in non-polar solvents, an excess of ligand gives mainly cis-[Mn(CO)₄(Ph₂PSiMe₃)X] (IVa, X  Cl;IVb, X  Br;IVc, X I). With ligand: [Mn(CO)₅X] reacting ratios in the range 0.5–1.0:1, the products from the three respective halomanganese complexes in THF were: (a) mainly [Mn₂(CO)₈(μ- PPh₂)(μ-Cl) (Va); (b) both [Mn(CO)₄(Ph₂PSiMe₃)Br] and [Mn₂(CO)₈(μ-PPh₂)(μ-Br)] (Vb); and (c) exclusively [Mn(CO)₄(Ph₂PSiMe₃)I]. The compounds IVa-c are stable in solution at ambient temperatures and are readily hydrolyzed by water or methanol to [Mn(CO)₄(Ph₂PH)X]. Compound IVb reacts at room temperature with [Mn(CO)₅Cl] to yield only [Mn₂- (CO)₈(μ-PPh₂)(μ-Br)] (Vb); compound IVc reacts in hot toluene with [Mn(CO)₅Cl] to yield mainly [Mn₂(CO)₈(μ-PPh₂)(μ-I)] (Vc), together with a small amount of the chloro-bridged analog.The dinuclear species II, III and Va-c appear to be formed mainly via an intermolecular elimination of Me₃SiX from the appropriate [M(CO)₄(Ph₂PSiMe₃)X] and metalpentacarbonylhalide (chloride or bromide) complexes.     

Magnetic resonance studies of Mn(II)-, Mn(III)-, and Fe(III)-conalbumin complexes.

Apoconalbumin binds Mn(II) at two sites with association constants of K1 = 7 (+/- 1) X 10(4) and K2 = 0.4 (+/- 0.25) X 10(4) M-1. The binding is tighter in the presence of excess bicarbonate resulting in K1 = 1.8 (+/- 0.2) X 10(5) and K2 = 3 (+/- 2) X 10(4) M-1. The electron paramagnetic resonance spectrum (at both 9 and 35 GHz) of Mn(II) bound at the tight site reveals a rhombic distortion (lambda = E/D approximately equal to 0.25-0.31) in the protein ligand environment of the mental ion. An evaluation of the 1/pT1p, paramagnetic contribution to the longitudinal relaxation rate of solvent protons with Mn(II)-, Mn(III)-, and Fe(III)-derivatives of conalbumin revealed that the mental ion in each site of conalbumin is accessible to one water molecule. For Mn(II)-conalbumin and Mn(III)-conalbumin species, inner coordination sphere protons are rapidly exchanging with the bulk solvent, while slow exchange conditions prevail for Fe(III)-conalbumin.     

Systematic characterization on electronic structures and spectra for a series of complexes, M(IDB)Cl2 (M = Mn, Fe, Co, Ni, Cu and Zn): a theoretical study

Theoretical studies on the coordination stabilities, spectra and DNA-binding trend for the series of metal-varied complexes, M(IDB)Cl₂ (M = Mn, Fe, Co, Ni, Cu and Zn; IDB = N, N -bis(2-benzimidazolylmethyl) amine), have been carried out by using the DFT/B3LYP method and PCM model. The calculated coordination stabilities (S) for these complexes present a trend of S(Ni) > S(Co) > S(Fe) > S(Cu) > S(Zn) > S(Mn). It has been estimated from the molecular orbital energies of the complexes that the DNA-binding affinities (A) of the complexes are in the order of A(Zn) < A(Mn) < A(Fe) ≈ A(Co) < A(Ni) < A(Cu). The studied results indicate that the Cu, Ni and Co complexes with large coordination stabilities present the low virtual orbitals, consequently yielding to the favorable DNA-binding affinities. The spectral properties of excitation energies and oscillator strengths for M(IDB)Cl₂ in the ultraviolet region were calculated by TD-DFT/B3LYP method.     

Halide abstraction reactions of Sb(V) chloride: Synthesis and characterisation of hexachloroantimonate salts of M(II) M = Zn,Mg; M(III) M = Cr; and M(IV) M = Ti,Sn and related Cp2M(IV) M = Ti,Zr and Hf

Reactions of SbCl₅ with various covalent metal halides in MeCN have been studied as a convenient and direct route to metal hexachloroantimonate salts via Sb(V) halide abstraction. The isolation and characterization (Ir, Vis-UV, ¹H NMR spectroscopic and microanalytical) of the complexes [Zn(MeCN)₆][SbCl₆]₂, [CrCl₂(MeCN)₄][SbCl₆], [SnCl₃(MeCN)₃][SbCl₆], [TiCl₂(MeCN)₄][SbCl₆]₂, [Cp₂M(Cl)(MeCN)_x][SbCl₆] M = ti, x = 1; M = Zr, Hf, x = 2, and [Cp₂M(MeCN)_y][SbCl₆]₂ M = Ti, y = 2; M = Zr, Hf, y = 3, is described. The reaction of MgCl₂ with SbCl₅ was carried out in EtOAC as solvent and gave [Mg(EtOAc)₆][SbCl₆]₂. ¹²¹Sb NMR, IR and UV spectroscopic measurements provide positive identification of the SbCl_6⁻ anion.     

Stereoselectivity of (R)- and (S)-hexahydro-difenidol binding to neuroblastoma M1, cardiac M2, pancreatic M3, and striatum M4 muscarinic receptors

(R)-Hexahydro-difenidol has a higher affinity for M1 receptors in NB-OK 1 cells, pancreas M3 and striatum M4 receptors (pKi 7.9 to 8.3) than for cardiac M2 receptors (pKi 7.0). (S)-Hexahydro-difenidol, by contrast, is nonselective (pKi 5.8 to 6.1). Our goal in the present study was to evaluate the importance of the hydrophobic phenyl, and cyclohexyl rings of hexahydro-difenidol for the stereoselectivity and receptor selectivity of hexahydro-difenidol binding to the four muscarinic receptors. Our results indicated that replacement of the phenyl ring of hexahydro-difenidol by a cyclohexyl group (----dicyclidol) and of the cyclohexyl ring by a phenyl moiety (----difenidol) induced a large (4- to 80-fold) decrease in binding affinity for all muscarinic receptors. Difenidol had a significant preference for M1, M3, and M4 over M2 receptors; dicyclidol, by contrast, had a greater affinity for M1 and M4 than for M2 and M3 receptors. The binding free energy decrease due to replacement of the phenyl and the cyclohexyl groups of (R)-hexahydro-difenidol by, respectively, a cyclohexyl and a phenyl moiety was almost additive in the case of M4 (striatum) binding sites. In the case of the cardiac M2, pancreatic M3, or NB-OK 1 M1 receptors the respective binding free energies were not completely additive. These results suggest that the four (R)-hexahydro-difenidol "binding moieties" (phenyl, cyclohexyl, hydroxy, and protonated amino group) cannot simultaneously form optimal interactions with the M1, M2, and M3 muscarinic receptors.(ABSTRACT TRUNCATED AT 250 WORDS)     

Effect of Oxygen Tension, Mn(II) Concentration, and Temperature on the Microbially Catalyzed Mn(II) Oxidation Rate in a Marine Fjord

We present evidence that the oxidation of Mn(II) in a zone above the O₂/H₂S interface in the water column of Saanich Inlet, British Columbia, Canada, is microbially catalyzed. We measured the uptake of ⁵⁴Mn(II) in water samples under in situ conditions of pH and temperature and in the presence and absence of oxygen. Experiments in the absence of oxygen provided a measure of the exchange of the tracer between the dissolved and solid pools of Mn(II); we interpret the difference between experiments in the presence and absence of oxygen to be a measure of Mn(II) oxidation. Using this method we examined the effect of oxygen tension, Mn(II) concentration, and temperature on the initial in situ Mn(II) oxidation rate (V₀). Mn(II) oxidation was almost twice as fast under conditions of 67% air saturation (V₀=5.5 nM h⁻¹) as with the in situ concentration of 15 μM (5% air saturation; V₀=3.1 nM h⁻¹). Additions of ca. 18 μM Mn(II) completely inhibited all Mn(II) oxidation at three different depths in the oxidizing zone, and there was a temperature optimum for Mn(II) oxidation of around 20°C. These results are consistent with biologically mediated Mn(II) oxidation and indicate that the rate is limited by both oxygen and the concentration of microbial binding sites in this environment.     

Autopoietic and (M,R) systems

From the many attempts to produce a conceptual framework for the organization of living systems, the notions of (M,R) systems and Autopoiesis stand out for their rigor, their presupposition of the circularity of metabolism, and the new epistemologies that they imply. From their inceptions, these two notions have been essentially disconnected because each has defined its own language and tools. Here we demonstrate the existence of a deep conceptual link between (M,R) systems and Autopoietic systems. This relationship permits us to posit that Autopoietic systems, which have been advanced as capturing the central aspects of living systems, are a subset of (M,R) systems. This result, in conjunction with previous theorems proved by Rosen, can be used to outline a demonstration that the operation of Autopoietic systems cannot be simulated by Turing machines. This powerful result shows the potential of linking these two models. Finally, we suggest that the formalism of (M,R) systems could be used to model the circularity of metabolism.     

(M,R)-systems, (P,M,C)-nets, hierarchical decay, and biological aging: reminiscences of Robert Rosen

I have the pleasure to present a number of personal experiences that I had with Robert Rosen, both as his student and as a research colleague, and I will describe how this affected my academic career over the past decades. As a matter of fact, Rosen's work with (M,R)-systems as well as his continuing mentorship guided me into my own research in gerontology and geriatrics. Amazingly, this still continues to affect my work in complexity theory after 30 years.     

Hydrothermal and Solvothermal Process Towards Development of LiMPO4 (M = Fe,Mn) Nanomaterials for Lithium‐Ion Batteries

Positive electrodes such as LiFePO₄ and LiMnPO₄ nanomaterials with olivine structures are considered as most efficient cathode materials for application in lithium ion batteries. Recently, several methods have been proposed for the preparation of lithium metal phosphates as cathodes for lithium ion batteries and their electrochemical performances have been investigated. Over the last 20 years, several synthetic methods have been proposed for lithium metal phosphate nanomaterials. In this review, hydrothermal and solvothermal syntheses of LiFePO₄ and LiMnPO₄ nanomaterials at low and high temperatures are discussed, including microwave‐hydrothermal and microwave‐solvothermal methods. The effect of particle size and particle morphology on the electrochemical properties of LiFePO₄ and LiMnPO₄ cathode materials are also discussed. In addition, the recently emerged supercritical solvothermal and supercritical hydrothermal syntheses of LiFePO₄ and LiMnPO₄ nanomaterials and their electrochemical property also been addressed.     

Salt stimulation of the activation of latent protein phosphatase, Fc.M, by Mn++ and by Mn/trypsin

The activation of porcine heart latent protein phosphatase (Fc.M) by pretreatment with Mn++ followed by trypsin (Mn/trypsin) can be stimulated 2.5-fold by including NaCl or KCl in the activation mixtures. The salts also stimulated the activation of the enzyme by Mn++ to the same level as that obtained by Mn/trypsin pretreatment in the absence of salt. The presence of salt in both the Mn++ and Mn/trypsin activations decreased the Mn++ requirement 10-fold in each case. Treatment of latent Fc.M by Mn/trypsin in the presence of 0.2 M NaCl or KCl offers a convenient method of expressing the full potential activity of the protein phosphatase.     

Re-mapping Robert Rosen's (M,R)-systems

The central concern of this paper is to re-evaluate Rosen's replicating (M,R)-systems, presented in his book 'Life Itself ', where M and R signify metabolism and repair, respectively. We look anew at Rosen's model of an organism in the light of extensive research into natural hierarchical systems, and the paper presents conclusions drawn from a comparison between Rosen's relational model and that of a birational complementary natural hierarchy. We accept that Rosen's relational model provides a useful stepping stone to understanding the nature of life, but also suggest that it induces potentially digressive conclusions. We conclude that a binary segregation of relational assemblies into mechanisms and organisms is insufficient, and indicate how a threefold segregation throws new light on Rosen's model. An organism is not 'the complement of a mechanism': the complement of a mechanism is its ecosystem. An organism is the 'complex interface' between mechanism and ecosystem.     

Organizational invariance in (M,R)-systems

Robert Rosen's concept of (M,R)-systems was a fundamental advance in our understanding of the essential nature of a living organism as a self-organizing system, one that is closed to efficient causation, synthesizing, and maintaining all of the catalysts necessary for sustained operation during the whole period of its lifetime. Although it is not difficult to construct a model metabolic system to represent an (M,R)-system, such a model system will typically appear to lack organizational invariance, an essential property of a living (M,R)-system. To have this property, an (M,R)-system must not only be closed to external causation, it must also have its organization coded within itself, i.e., the knowledge of which components are needed for which functions must not be defined externally. In this paper, we discuss how organizational invariance may be achieved, and we argue that the apparent failure of previous models to be organizationally invariant is an artifact of the usual practice of treating catalytic cycles as 'black boxes'. If all of the steps in such a cycle are written as uncatalyzed chemical reactions, then it becomes clear that the organization of the system is fully defined by the chemical properties of the molecules that compose it.     

Synthesis,spectroscopy, electrochemistry,and photochemistry of a series of M(bpym)2Cl2 (M=Mn(II), Co(II), Ni(II), and Cu(II)) complexes. Precursor complexes in the preparation of polymetallic systems

The synthesis, aqueous absorption and reflectance spectra, cyclic voltammetry and ligand field photochemistry of a series of M(bpym)₂Cl₂ (M=Mn(II), Co(II), Ni(II), Cu(II) and bpym=2,2′-bipyrimidine) are reported here. Ligand field electronic spectral assignments are made by comparison to analogous M(bpy)₂Cl₂(s) (bpy=2,2′-bipyridine) and M(bpym)₃²⁺ complexes. Ligand field absorption maxima are shifted to lower energy as a result of bpym loss vs. M(bpym)₃²⁺ complexes. Metal to ligand charge transfer absorption energies increase as a result of d_M orbital stabilization vs. M(bpym)₃²⁺ complexes. Cyclic voltammetry indicates ring opening upon reduction of the complexes. The complexes are photochemically inert (φ_max<0.002) at the irradiated wavelengths.     

Freshwater Pearl mussels of the genus Margaritifera (Mollusca: Bivalvia) described as M. elongata (Lamarck, 1819) and M. borealis (Westerlund, 1871) should be classified with M. margaritifera (Linnaeus, 1758)

The shells of Pearl mussels from the basins of the Solza, Keret’, and Umba rivers flowing into the White Sea have been measured to determine the ratio of shell convexity to its maximum height. This ratio is the main character that, according to Bogatov et al. (2003), allows one to distinguish between three species of the genus Margaritifera: M. margaritifera, M. elongata, and M. borealis. It has been found that the above ratio gradually increases as the shell grows. Therefore, this character is unsuitable for species diagnosis, the more so that no hiatus in it between the three forms of pearl mussels has been revealed in any of the samples studied. On this basis, it may be concluded that Northern Europe, including Russia, is inhabited by only one species of pearl mussels, M. margaritifera.     

Some algebraic properties of (M,R)-systems

On the basis of Rosen's representation of (M, R)-systems as sequential machines (Rosen,Bull. Math. Biophys.,26, 103–111, 1964), the existence of projective limits in categories of general (M, R)-systems is proved.     

Manganese (Mn) Oxidation Increases Intracellular Mn in Pseudomonas putida GB-1

Bacterial manganese (Mn) oxidation plays an important role in the global biogeochemical cycling of Mn and other compounds, and the diversity and prevalence of Mn oxidizers have been well established. Despite many hypotheses of why these bacteria may oxidize Mn, the physiological reasons remain elusive. Intracellular Mn levels were determined for Pseudomonas putida GB-1 grown in the presence or absence of Mn by inductively coupled plasma mass spectrometry (ICP-MS). Mn oxidizing wild type P. putida GB-1 had higher intracellular Mn than non Mn oxidizing mutants grown under the same conditions. P. putida GB-1 had a 5 fold increase in intracellular Mn compared to the non Mn oxidizing mutant P. putida GB-1-007 and a 59 fold increase in intracellular Mn compared to P. putida GB-1 ∆2665 ∆2447. The intracellular Mn is primarily associated with the less than 3 kDa fraction, suggesting it is not bound to protein. Protein oxidation levels in Mn oxidizing and non oxidizing cultures were relatively similar, yet Mn oxidation did increase survival of P. putida GB-1 when oxidatively stressed. This study is the first to link Mn oxidation to Mn homeostasis and oxidative stress protection.     

Synthesis, characterization, and cytotoxicity in vitro of the complex [Mn (Hptc) (phen) (OH)] n

AimsA bridging ligand 2,4,6-pyridine tricarboxylic acid (H₃ptc) and its manganese(II) complex [Mn(Hptc)(phen)(OH)]n(Hptc = 2,4,6-pyridine tricarboxylic acid, phen = 1,10-phenanthroline) have been synthesized and characterized.Main methodsThe interaction with DNA (HeLa and KB) was carried out by fluorescence spectrum and gel electrophoresis assay. In vitro apoptosis assay and cytotoxicity assay detect the manganese (II) complex interaction with cancer cells.Key findingsFluorescence spectrum demonstrated the ability of the complexes to interact with DNA in an intercalative mode. Gel electrophoresis assay exhibited more effective DNA-cleavage activity. In vitro apoptosis assay of the complexes were examined on HeLa and KB cells, exhibited cytotoxic specificity and a significant cancer cell inhibitory rate.SignificanceThe complex may be a latent antitumor agent as a result of its unique interaction mode with DNA and cancer cells inhibition effect.     

Functional expression of M(1), M(3) and M(5) muscarinic acetylcholine receptors in yeast

The goal of this study was to functionally express the three G(q)-coupled muscarinic receptor subtypes, M(1), M(3) and M(5), in yeast (Saccharomyces cerevisiae). Transformation of yeast with expression constructs coding for the full-length receptors resulted in very low numbers of detectable muscarinic binding sites (B(max) < 5 fmol/mg). Strikingly, deletion of the central portion of the third intracellular loops of the M(1), M(3) and M(5) muscarinic receptors resulted in dramatic increases in B(max) values (53-214 fmol/mg). To monitor productive receptor/G-protein coupling, we used specifically engineered yeast strains that required agonist-stimulated receptor/G-protein coupling for cell growth. These studies showed that the shortened versions of the M(1), M(3) and M(5) receptors were unable to productively interact with the endogenous yeast G protein alpha-subunit, Gpa1p, or a Gpa1 mutant subunit that contained C-terminal mammalian Galpha(s) sequence. In contrast, all three receptors gained the ability to efficiently couple to a Gpa1/Galpha(q) hybrid subunit containing C-terminal mammalian Galpha(q) sequence, indicating that the M(1), M(3) and M(5) muscarinic receptors retained proper G-protein coupling selectivity in yeast. This is the first study to report the expression of muscarinic receptors in a coupling-competent form in yeast. The strategy described here, which involves structural modification of both receptors and co-expressed G proteins, should facilitate the functional expression of other classes of G protein-coupled receptors in yeast.