Nucleotide sequences of two fragments from the coat-protein cistron of bacteriophage R17 ribonucleic acid

Bacteriophage R17 RNA was labelled with ³²P and was subjected to partial digestion with ribonuclease T₁. The products were fractionated by ionophoresis on polyacrylamide gel. Two fragments were purified and their nucleotide sequences determined by methods involving complete and further partial digestion with ribonucleases A and T₁. Fragment 20 had a sequence that coded for the amino acids in positions 32–53 of the coat protein of the bacteriophage. Fragment 20X, on further purification in 7m-urea, gave rise to two smaller nucleotides whose sequences coded for the amino acids in positions 56–66 and 67–76 of the coat protein. The sequence of the two fragments was such that they could be written in the form of loops stabilized by base-pairing.     

Tissue-specific activation of the osmotin gene by ABA,C2H4 and NaCl involves the same promoter region

The gene encoding the antifungal protein osmotin is induced by several hormonal and environmental signals. In this study, tissue-specific and inducer-mediated expression of the reporter gene -glucuronidase (uidA) fused to different fragment lengths of the osmotin promoter was evaluated in transgenic tobacco (Nicotiana tabacum). The region of the promoter between –248 to –108 (Fragment A) was found to be essential and sufficient for inducer (abscisic acid (ABA), C₂H₄ and NaCl)-mediated expression of the reporter gene. Expression of the reporter gene was developmentally regulated and increased with maturity of leaves, stem and flowers. Expression also was tissue-specific being most highly expressed in epidermis and vascular parenchyma of the stem. The regulators ABA, C₂H₄ and NaCl exhibited tissue-specific induction of this promoter. The promoter was specifically responsive to C₂H₄ in flowers at virtually all stages of development, but not responsive in these tissues to ABA or NaCl. Conversely, ABA and NaCl were able to induce reporter gene activity using promoter Fragment A in specific tissues of root where C₂H₄ was unable to induce activity. Further dissection of the promoter Fragment A into fragments containing either the conserved GCC element (PR); PR/AT; or G/AT sequences, and subsequent testing of these fragments fused to GUS in transgenic plants was performed. These experiments revealed that the promoter fragment containing PR element alone, although required, was barely able to allow responsiveness to C₂H₄. However, significant C₂H₄-induced activity was obtained with a promoter fragment containing the AT and PR elements together.     

Molybdate and tungstate transfer by rat ileum competitive inhibition by sulphate

For both MoO₄²⁻ and WO₄²⁻ the maximum rate of uptake by the small intestine of the rat (studied in vitro using the everted sac technique) occurs in the lower ileum. Kinetic constants, derived by a least squares procedure, are compared with those previously obtained for SO₄²⁻ transport. For both V and K_a, SO₄²⁻ > MoO₄²⁻ > WO₄²⁻, with only small differences between sacs IV and V. Mutual inhibition of MoO₄²⁻ and WO₄²⁻ transport and inhibition of both by SO₄²⁻ are competitive processes. This is shown by the generally good agreement between K_a values and derived K_i values and by V values in the presence and absence of the inhibiting species. The three ions SO₄²⁻, MoO₄²⁻ and WO₄²⁻ are probably transferred across the intestine by a common carrier system. Implications for the sulphate-molybdenum interaction in molybdosis are discussed.     

Synthesis of [Tl4Se16]: a novel tetranuclear Tl polyselenide

(Ph₄P)₄[Tl₄Se₁₆] was prepared hydrothermally in a sealed pyrex tube by the reaction of TlCl, K₂Se₄ and Ph₄PCl in a 1:1:1 molar ratio at 110 °C for one day. The red crystals were obtained in 50% yield. Crystals of (Ph₄P)₄[Tl₄Se₁₆]: triclinic P (No. 2), Z=1, a=12.054(9), b=19.450(10), c=11.799(6) Å, α=104.63(4), β=98.86(6), γ=101.99(6)° and V=2555(3) ų at 23 °C, 2θ_max=40.0°, μ=120.7 cm⁻¹, D_calc=2.23. The structure was solved by direct methods. Number of data collected: 5206. Number of unique data having F_o²>3σ(F_o²): 1723. Final R=0.075 and R_w=0.089. [Tl₄Se₁₆]⁴⁻ consists of four, almost already linearly arranged, tetrahedral thallium centers which are coordinated by two chelating Se₄²⁻, two bridging Se₂²⁻ and four bridging Se²⁻ ligands. [Tl₄Se₁₆]⁴⁻ sits on an inversion center and possesses a central {Tl₂Se₂}²⁺ planar core. The Tl(1)–Tl(1)′ distance in this core is 3.583(6) Å. These two thallium atoms are then each linked to two cyclic Tl(Se₄) fragments via bridging Se₂²⁻ and Se²⁻ ligands forming Tl₂Se(Se₂) five-membered rings.     

Conductive and Kinetic Properties of Connexin45 Hemichannels Expressed in Transfected HeLa Cells

Human HeLa cells transfected with mouse connexin Cx45 were used to examine the conductive and kinetic properties of Cx45 hemichannels. The experiments were carried out on single cells using a voltage-clamp method. Lowering the [Ca²⁺]_o revealed an extra current. Its sensitivity to extracellular Ca²⁺ and gap junction channel blockers (18α-glycyrrhetinic acid, palmitoleic acid, heptanol), and its absence in non-transfected HeLa cells suggested that it is carried by Cx45 hemichannels. The conductive and kinetic properties of this current, I _hc, were determined adopting a biphasic pulse protocol. I _hc activated at positive V _m and deactivated partially at negative V _m. The analysis of the instantaneous I _hc yielded a linear function g _hc,inst = f(V _m) with a hint of a negative slope (g _hc,inst: instantaneous conductance). The analysis of the steady-state I _hc revealed a sigmoidal function g _hc,ss = f(V _m) best described with the Boltzmann equation: V _m,0 = −1.08 mV, g _hc,min = 0.08 (g _hc,ss: steady-state conductance; V _{m, 0}:V _m at which g _hc,ss is half-maximally activated; g _hc,min: minimal conductance; major charge carriers: K⁺ and Cl⁻). The g _hc was minimal at negative V _m and maximal at positive V _m. This suggests that Cx45 connexons integrated in gap junction channels are gating with negative voltage. I _hc deactivated exponentially with time, giving rise to single time constants, τ_d. The function τ_d = f(V _m) was exponential and increased with positive V _m (τ_d = 7.6 s at V _m = 0 mV). The activation of I _hc followed the sum of two exponentials giving rise to the time constants, τ_a1 and τ_a2. The function τ_a1 = f(V _m) and τ_a2 = f(V _m) were bell-shaped and yielded a maximum of ≅ 0.6 s at V _m ≅ −20 mV and ≅ 4.9 s at V _m ≅ 15 mV, respectively. Neither τ_a1 = f(V _m) nor τ_a2 = f(V _m) coincided with τ_d = f(V _m). These findings conflict with the notion that activation and deactivation follow a simple reversible reaction scheme governed by first-order voltage-dependent processes.     

An NMR investigation of putative interresidue H-bonding in methyl α-cellobioside in solution

Methyl α-cellobioside (methyl β-d-glucopyranosyl-(1→4)-α-d-glucopyranoside) was labeled with ¹³C at C4′ for use in NMR studies in DMSO-d₆ solvent to attempt the detection of a trans-H-bond J-coupling (^3hJ_CCOH) between C4′ and OH3. Analysis of the OH3 signal at 600 MHz revealed only the presence of two homonuclear J-couplings: ³J_H3,OH3 and a smaller, longer range J_HH. No evidence for ^3hJ_C4′,OH3 was found. The longer range J_HH was traced to ⁴J_H4,OH3 based on 2D ¹H–¹H COSY data and inspection of the H2 and H4 signal lineshapes. A limited set of DFT calculations was performed on a methyl cellobioside mimic to evaluate the structural dependencies of ⁴J_H2,O3H and ⁴J_H4,O3H on the H3–C3–O3–H torsion angle. Computed couplings range from about −0.7 to about +1.1 Hz, with maximal values observed when the C–H and O–H bonds are roughly diaxial.     

Specific growth rate as a determinant of the carbon isotope composition of the temperate seagrass Zostera marina

The seasonal variability of specific growth rate and the carbon stable isotope ratio (δ¹³C) of leaf blades (δ¹³C_leaf) of a temperate seagrass, Zostera marina (within 10 days old) were measured simultaneously, together with the δ¹³C of dissolved inorganic carbon (δ¹³C_DIC) at three sites in the semi-closed Akkeshi estuary system, northeastern Japan, in June, September, and November 2004. The δ¹³C_leaf ranged from −16.2 to −6.3‰ and decreased from summer to winter. The simultaneous measurement of the δ¹³C_leaf, growth rate, and morphological parameters (mean leaf length and width, mean number of leaves per shoot, and sheath length) of the seagrass and δ¹³C_DIC in the surrounding water allowed us to compare directly the δ¹³C_leaf and specific growth rate of seagrass. The difference in the δ¹³C of seagrass leaves relative to the source DIC (Δδ¹³C_{leaf − DIC}) was the least negative (−11 to −7‰) in June at all three sites and became more negative (−17 to −8‰) as the specific growth rate decreased. This positive correlation between Δδ¹³C_{leaf − DIC} and specific growth rate can be used to diagnose the growth of seagrasses. Δδ¹³C_{leaf − DIC} changed by −1.7 ± 0.2‰ when the leaf specific growth rate decreased by 1% d⁻¹.     

Isolation and study of a fragment of human serum albumin containing one of the antigenic sites of the whole molecule

1. A fragment of human serum albumin called `inhibitor' has been degraded by trypsin, and one of the degradation products, designated fragment F1, has been isolated. Fragment F1 has a molecular weight of 6600. It contains neither tyrosine nor tryptophan. It is not precipitated with rabbit anti-sera to human serum albumin. 2. Fragment F1 was coupled to p-aminobenzylcellulose to form an insoluble conjugate. Rabbit anti-(human serum albumin) antibodies reacting with fragment F1 were specifically adsorbed on this conjugate and were desorbed by glycine–hydrochloric acid buffer. The isolated antibodies are composed of γ-globulin and β₂-macroglobulin. 3. Human serum albumin and fragment F1 formed with 7s anti-(fragment F1) antibodies soluble complexes that were studied by passive haemagglutination, ultracentrifugation and electrophoresis. Fragment F1 was shown to contain only one of the antigenic sites of albumin molecule. The 7s anti-(fragment F1) antibodies were shown to be bivalent and monospecific.     

Synthesis and magnetic properties of bis(μ-hydroxo)bis[(2,2 ′-bipyridyl)copper(II)] squarate. Crystal structure of bis(μ-hydroxo)bis[(2,2′-bipyridyl)copper(II)] squarate tetrahydrate

The compound [Cu₂(bipy)₂(OH)₂](C₄O₄)·5.5H₂O, where bipy and C₄O₄²⁻ correspond to 2,2′-bipyridyl and squarate (dianion of 3,4-dihydroxy-3-cyclo- butene-1,3-dione) respectively, has been synthesized. Its magnetic properties have been investigated in the 2–300 K temperature range. The ground state is a spin-triplet state, with a singlet-triplet separation of 145 cm⁻¹. The EPR powder spectrum confirms the nature of the ground state.Well-formed single crystals of the tetrahydrate, [Cu₂(bipy)₂(OH)₂](C₄O₄)·4H₂O, were grown from aqueous solutions and characterized by X-ray diffraction. The system is triclinic, space group P , with a = 9.022(2), b = 9.040(2), c = 8.409(2) Å, α = 103.51(2), β = 103.42(3), γ = 103.37(2)°, V = 642.9(3) ų, Z = 1, D_x = 1.699 g cm⁻³, μ(Mo Kα) = 17.208 cm⁻¹, F(000) = 336 and T= 295 K. A total of 2251 data were collected over the range 1θ25°; of these, 1993 (independent and with I3σ(I)) were used in the structural analysis. The final R and R_w residuals were 0.034 and 0.038 respectively. The structure contains squarato-O¹, O³-bridged bis(μ-hydroxo)bis[(2,2′-bipyridyl)copper(II)] units forming zigzag one-dimensional chains. Each copper atom is in a square-pyramidal environment with the two nitrogen atoms of 2,2′-bipyridyl and the two oxygen atoms of the hydroxo groups building the basal plane and another oxygen atom of the squarate lying in the apical position.The magnetic properties are discussed in the light of spectral and structural data and compared with the reported ones for other bis(μ-hydroxo)bis[(2,2′-bipyridyl)copper(II)] complexes.     

Genetic Mapping of the Mouse Genes Encoding the Voltage-Sensitive Calcium Channel Subunits

The genes encoding the α₁ and β subunits of voltage-sensitive calcium channel were mapped in the mouse by analysis of the progeny of two multilocus crosses. The α₁, β₂, and β₄ subunit genes, termed Cchna1, Cchb2, and Cchb4, are located at different sites on proximal Chr 2, while the β₃ subunit gene Cchb3 maps to Chr 15 near Wnt1. These results together with previous mapping data indicate that the calcium channel genes are dispersed in the mouse genome, unlike the sodium channel genes, which are clustered.     

Syntheses, structures and spectroscopy of new heteroselenometalates

[PPh₄]₂[MoSe₄] and [PPh₄]₂[WSe₄] react with two equivalents of AuCN in CH₃CN to afford [PPh₄]₂[(NC)Au(μ-Se)₂-Mo(μ-Se)₂Au(CN)] · CH₃CN (bd1) and [PPh₄]₂[(NC)Au(μ-Se)₂Au(CN)] · CH₃CN (bd2), respectively. Compounds 1 and 2 are isostructural. Compound 1 crystallizes in the triclinic space group with two formula units in a cell dimensions a=13.181(4), b=14.239(4), C=14.684(4) Å, α=73.00(3), β=73.66(2), γ=79.06(2)° at 113 K. Full anisotropic refinement of the structure of 1 on F² led to a value of R₁=0.0562 for those 9075 data having F_o² . 2σ(F_o²). The [(NC)Au(μ-Se)₂Mo(μ-Se)₂Au(CN)]²⁻ anion of 1 comprises two AuCN fragments ligating the opposite edges of a tetrahedral [MoSe₄]²⁻ moiety. Compounds 1 and 2 exhibit an IR band at 2250 cm⁻¹ that may be assigned to a CN stretching mode of the CH₃CH solvate; such a solvate molecule was found in the crystal structure of 1. The ⁷⁷Se NMR spectra show a resonance at 1104 ppm for 1 and 832 ppm for 2. Addition of excess PME₂Ph to the same solutions that produce 1 and 2 results in the formation of [PPh₄][(Me₂PhP)Au(μ-Se)₂MoSe₂] (3) and [PPh₄][(Me₂PhP)Au(μ-Se)₂WSe₂] (4), respectively. Compounds 3 and 4 are not isostructural. Compound 3 crystallizes in the monoclinic space gorup Cc with four formula units in a cell of dimensions a=21.912(4), B=9.809(2), C=15.959(3) Å, β=100.79(3) at 113 K. Full anisotropic refinement of the structure of 1 on F² led to a value of R₁=0.0481 for those 6851 data having F_o² > 2σ(F_o²). Compound 4 crystallizes in the triclinic space group with two formula units in a cell of dimensions a=11.315(2), B=13.053(3), C=14.173(3) Å, α=103.59(3), β=103.55(3), γ=114.75(3)δ at 113 K. Full anisotropic refinement of the structure of 4 on F² led to a value of R₁=0.0414 for those 7825 data having F_o² > 2σ(F_o²). The [(Me₂]PhP)Au(μ-Se)₂MoSe₂]⁻ anion of 3 and the [(Me₂PhP)Au(μ-Se)₂WSe₂]⁻ anion of 4 comprise an [(Me₂PhP)Au]⁺ fragment ligated across an edge of a tetrahedral (MSe₄]²⁻ moiety. [PPh₄]₂[MoSe₄] and [PPh₄]₂[WSe₄] react with one equivalent of AuCN in CH₃CH to afford [PPh₄]₂[(NC)Au(μ-Se)₂MoSe₂] (5) and [PPh₄]₂[(NC)Au(μ-Se)₂WSe₂] (6), respectively. Compounds 5 and 6 are isostructural. Compounds 5 crystallizes in the monoclinic space group C2/c with four formula units in a cell of dimensions a=11.234(15), B=20.329(28), C=20.046(28) Å, β=91.81(5)° at 113 K. Full anisotropic refinement of the structure of 5 on F² led to a value of R₁=0.0457 for those 4003 data having F_o² > 2σ(F_o²). The [(NC)Au(μ-Se)₂MoSe₂]²⁻ anion of 5, which has a crystallographically imposed twofold axis, comprises an AuCN fragment ligated across an edge of a tetrahedral [MoSe₄]²⁻ moiety. The reaction of [PPh₄]₂(NC)Cu(μ-Se)₂MoSe₂] with one equivalent of AuCN in CH₃CN produces a precipitate that is then redissolved through reaction with an excess of PMe₂Ph to afford [PPh₄][(Me₂PhP)₂Cu(μ-Se)₂MoSe₂] (7). Compound 7 crystallizes in the monoclonic space group P1₁/c with four formula units in a cell of dimensions a=9.975(1), B=30.391(7), C=14.541(6) Å, β=109.66(3) at 113 K. Full anisotropic refinement of the structure of 7 on F² led to a value of R₁=0.0305 for those 5205 data having F_o² > 2σ(F_o²). The [(Me₂PhP)₂Cu(μ-Se)₂MoSe₂]⁻ anion of 7 comprises an [(Me₂PhP)₂Cu]⁺ fragment ligated across an edge of the [MoSe₄]²⁻ moiety to provide a tetrahedral geometry about the Cu atom. The NMR, IR and UV-Vis spectroscopic data for these compounds are consistent with their solid-state structures.     

Isotopic composition and morphology of living Globorotalia scitula: a new proxy of sub-intermediate ocean carbonate chemistry?

Abundance, isotopic composition and morphological imprints of the planktonic foraminifera Globorotalia scitula (Brady) were closely examined for possible use as a novel reconstruction tool of chemical environments in sub-intermediate depth seawater in the past. Based on the MOCNES plankton tow observation of dwelling depths of G. scitula and the isotopic compositions together with hydrochemistry data, the empirical relations between isotopic disequilibria in carbon (Δδ¹³C=δ¹³C_{G. scitula}−δ¹³C_DIC) and oxygen (Δδ¹⁸O=δ¹⁸O_{G. scitula}−δ¹⁸O_w) isotopes in the carbonate tests and the seawater δ¹⁸O and δ¹³C of dissolved inorganic carbon (DIC), respectively, are introduced. The morphological information such as pore density and porosity is also examined for significant relations to carbonate chemistry. Shell porosity is strongly correlated saturation state of calcite. The dissolution of living G. scitula tests may promote the observed isotopic differences as well as the increases in porosity. Δδ¹⁸O of G. scitula is found effectively to be linear function of both water temperature and calcite saturation state (Ω), and thereby temperature equation for G. scitula is provided, while Δδ¹³C of G. scitula is a linear function of only calcite saturation state.The equation was validated by using Globorotalia scitula collected by a sediment trap in intermediate water depths. Satisfactory agreements were found between observed and calculated Δδ¹⁸O from the empirical equations based on temperature and hydrochemistry data at sediment trap deployment site, indicating that the equation may be useful in paleo-environmental reconstruction of sub-intermediate water. The sediment trap observation further suggests that the abundance of G. scitula does not necessarily correspond to surface water productivity and to POC flux, but instead, it correlates well with the supply of fine organic matter, which appears to be a result of water convection. Thus, G. scitula may be an unambiguous and excellent paleo-environmental recorder for carbonate chemistry and for fine organic matter transport to the depths, if isotopic and morphological observations are combined.     

Conformational properties of Eu(III) complexes of 3,3′; 5,3″-polymethylene bridged derivatives of 2,2′; 6,2″-terpyridine

The complex [Eu(tpy)₃](ClO₄)₃ where TPY=2,2′; 6,2″-terpyridine, has been prepared and reexamined. The complex appears to be stable in acetonitrile solution with respect to decomplexation of the ligands but the addition of water does cause partial replacement of tpy. Analogous complexes have been prepared with 3,3′; 5,3″-polymethylene bridged derivatives of tpy having two or three carbons in the bridge. The bridging enforces a cisoid geometry of the ligand and prohibits its replacement by added water. An X-ray determination was carried out for [Eu(3b)₃](ClO₄)₃, where 3b=3,3′; 5,3″-dimethylene tpy, which crystallizes in the monoclinic space group P2₁/c with a=11.908(4), b=15.768(5), c=29.513(9) Å, β=93.60(2)°, μ=13.5 cm⁻¹ and Z=4. The complex forms a tricapped trigonal prism with each of the ligands adopting the same dl conformation. Variable temperature NMR analysis of the bridged ligand complexes indicates that conformational inversion of the bound ligand is not a concerted process and barriers for inversion of individual methylene units can be estimated from coalescence of the signals from the geminal methylene protons. The luminescence properties of the bridged tpy complexes are similar to the parent unbridged system.     

Kinetics and mechanism of CO substitution of [η-CpFe(CO)3]PF6 with PPh3 in the presence of substituted pyridine N-oxide

The kinetics of substitution reactions of [η-CpFe(CO)₃]PF₆ with PPh₃ in the presence of R-PyOs have been studied. For all the R-PyOs (R = 4-OMe, 4-Me, 3,4-(CH)₄, 4-Ph, 3-Me, 2,3-(CH)₄, 2,6-Me₂, 2-Me), the reactions yeild the same product [η⁵-CpFe(CO)₂PPh₃]PF₆, according to a second-order rate law that is first order in concentrations of [η⁵-CpFe(CO)₃]PF₆ and of R-PyO but zero order in PPh₃ concentration. These results, along with the dependence of the reaction rate on the nature of R-PyO, are consistent with an associative mechanism. Activation parameters further support the bimmolecular nature of the reactions: ΔH^≠ = 13.4 ± 0.4 kcal mol⁻¹, ΔS^≠ = −19.1 ± 1.3 cal k⁻¹ mol⁻¹ for 4-PhPyO; ΔH^≠ = 12.3 ± 0.3 kcal mol⁻¹, ΔS^≠ = 24.7 ±1.0 cal K⁻¹ mol⁻¹ for 2-MePyO. For the various substituted pyridine N-oxides studied in this paper, the rates of reaction increase with the increasing electron-donating abilities of the substituents on the pyridine ring or N-oxide basicities, but decrease with increasing ¹⁷O chemical shifts of the N-oxides. Electronic and steric factors contributing to the reactivity of pyridine N-oxides have been quantitatively assessed.     

Relative stability of α-melanotropin and related analogues to rat brain homogenates

α-Melanotropin (α-MSH) retains less than 1% of its original activity after a 60 min incubation with 10% rat brain homogenate. [Nle⁴, D-Phe⁷]-α-MSH is nonbiodegradable in rat serum (240 min incubation) and still maintains 10% of its original activity in 10% rat brain homogenate (240 min incubation). The related fragment analogue, Ac-[Nle⁴, D-Phe⁷]-α-MSH_4–10-NH₂, retains 50% of its activity after a 240 min incubation in rat brain homogenate, whereas Ac-[Nle⁴, D-Phe⁷]-α-MSH_4–11-NH₂ is totally resistant to inactivation by rat brain homogenate. Both [Nle⁴, D-Phe⁷]-fragments are resistant to degradation by rat serum, but [Nle⁴]-α-MSH, Ac-[Nle⁴]-α-MSH_4–10-NH₂ and Ac-[Nle⁴]-α-MSH_4–11-NH₂ are rapidly inactivated under both conditions. The cyclic melanotropin, [ ]-α-MSH, is inactivated in rat brain homogenate as is the shorter Ac-[ ]-α-MSH_4–10-NH₂ analogue, but neither cyclic melanotropin is inactivated upon incubation in serum from rats. Ac-[ ]-α-MSH_4–10-NH₂ is resistant to inactivation by either rat serum or a brain homogenate. Some of these melanotropin analogues may provide useful probes for the localization and characterization of putative melanotropin receptors in both the central nervous system and peripheral tissues.     

Landscape patterns of CH4 fluxes in an alpine tundra ecosystem

We measured CH₄ fluxes from three major plant communities characteristic of alpine tundra in the Colorado Front Range. Plant communities in this ecosystem are determined by soil moisture regimes induced by winter snowpack distribution. Spatial patterns of CH₄ flux during the snow-free season corresponded roughly with these plant communities. InCarex-dominated meadows, which receive the most moisture from snowmelt, net CH₄ production occurred. However, CH₄ production in oneCarex site (seasonal mean=+8.45 mg CH₄ m^–2 d^–1) was significantly larger than in the otherCarex sites (seasonal means=–0.06 and +0.05 mg CH₄ m^–2 d^–1). This high CH₄ flux may have resulted from shallower snowpack during the winter. InAcomastylis meadows, which have an intermediate moisture regime, CH₄ oxidation dominated (seasonal mean=–0.43 mg CH₄ m^–2 d^–1). In the windsweptKobresia meadow plant community, which receive the least amount of moisture from snowmelt, only CH₄ oxidation was observed (seasonal mean=–0.77 mg CH₄ m^–2 d^–1). Methane fluxes correlated with a different set of environmental factors within each plant community. In theCarex plant community, CH₄ emission was limited by soil temperature. In theAcomastylis meadows, CH₄ oxidation rates correlated positively with soil temperature and negatively with soil moisture. In theKobresia community, CH₄ oxidation was stimulated by precipitation. Thus, both snow-free season CH₄ fluxes and the controls on those CH₄ fluxes were related to the plant communities determined by winter snowpack.     

C-nuclear magnetic resonance studies of 85% C-enriched amino acids and small peptides: pH effects on the chemical shifts, coupling constants, kinetics of cis-trans isomerisation and conformation aspects

The ¹³C chemical shifts of several 85% ¹³C-enriched amino acids and small peptides were studied as a function of pH. The results show that the chemical shifts of carbon atoms of ionizable groups vary significantly within the zone of their pK. Generally with the pH going from 7 to 1 all the δC are shifted more or less upfield with the exception of the carbonyl group of the second last residue which is shifted slightly downfield. This suggests the formation of an hydrogen bond at acid pH involving in a seven-membered ring the C=O in question and the COOH terminal.The percentage of cis and trans conformers of glycyl-l-proline and glycyl-l-prolylglycine were studied as a function of pH. The trans form is always preponderant whatever the pH. The accessibility of the carbonyl group to protonation of the proline residue strongly influences the cis-trans equilibrium. Thus, with the pH varying from 7 to 1, the trans isomer changes from 61 to 85% for glycyl-l-proline and only from 77 to 80% for glycyl-l-prolylglycine.The proton NMR studies underline the important differences existing between the two molecular forms of glycyl-l-proline. The cis conformation is characterized with regard to the trans form by the non-equivalence of the α-protons of the glycine residue, by a lower pK₁ and by a larger ΔδH_α of the proline residue as a function of pH. These results could suggest an end-to-end interaction in the cis form of the glycyl-l-proline molecule.The ¹³C-¹³C coupling constants were also studied as a function of pH. The results show that J_Co-Cα of a C-terminal residue, varying from 5 to 6 Hz and reflecting the pK of the carboxylate group, is a linear function of δ_Co and δ_Cα as in the case of the amino acids. The total variation of the electron density of those two carbons in an amino acid is approximately 40% weaker than in a C-terminal residue. The charge distribution along the C_α−C_o bond, however, is practically the same in both cases.Finally the ratios of the conversion rate constants of the two isomers cis-trans of glycyl-proline were calculated at different pH values; the relations between the isomer percentages and δ_Co, δ_Cα on the one hand and the J_Co-Cα on the other were established.     

Decarboxylation kinetics for the carbonatotris(pyridine)cobalt(III) ion in perchloric acid solutions

The kinetics of the decomposition reactions of the CO(py)₃(CO₃)(H₂O)⁺ ion have been investigated in aqueous perchloric acid solutions over a range of hydrogen ion concentrations (0.10 to 5.0 M) and at two ionic strengths (I = 1.0 and 5.0 M). At the lower ionic strength, plots of ln (A_t–A_∞ versus time show a nonlinearity that is consistent with that expected for consecutive first-order reactions. The rates of the faster reaction are similar to those reported for the spontaneous reduction of aquopyridine-cobalt(III) cations. At the higher ionic strength, the above noted curvature is not apparent and the decarboxylation kinetics of the title complex may be described by a pseudo-first-order rate constant: k_obs = k[H₃O⁺]. At 20°C, k = (1.75−+0.09) s⁻¹ M⁻¹ with activation parameters ofΔH^‡ = (97 −+ 4) kJ mol⁻¹ and ΔS^‡ = −(54 −+ 32) J deg⁻¹ mol⁻¹. These kinetic parameters are compared with those previously reported for the similar complexes, Co(py)₄CO₃⁺ and Co(py)₂(CO₃)(H₂O)₂⁺.     

A spectroscopic model for the high pH form of sulfite oxidase

The syntheses and spectroscopic properties of two monomeric oxo-Mo(V) complexes [NMe₄][MoO(SC₆H₄---CH=N---C₆H₄O)(SAr)₂] (Ar=Ph (2a), PhCH₃ (2b)) exhibiting a novel S₃NO coordination site are described. The EPR parameters of the Mo(V) complexes are almost identical with the parameters for the high pH form of sulfite oxidase, allowing further predictions for the unknown coordination site of the molybdenum cofactor in such molybdenum-containing enzymes. The Mo(V) compounds react with water to form a μ-oxo-bridged Mo(V) dimer, which is readily oxidized by oxygen to give the monomeric dioxo-Mo(VI) complex MoO₂(SC₆H₄---CH=N---C₆H₄O)(sol) (4) (sol=acetonitrile; dimethyl sulfoxide (DMSO)). The structure of 4 has been determined by X-ray crystallography (space group P (No. 2), a=7.855(4), b=9.530(3), c=11.676(6) Å, α=103.96(3), β=99.03(3), γ=100.73(3)°, V=814.5 ų, ρ_calc=1.79 g cm⁻³, Z=2, R(F)=0.026, R(wF)=0.026). The geometry about the molybdenum is distorted octahedral, with two terminal oxo groups cis to each other.     

Pressure jump relaxation kinetics of frog skin open circuit voltage and short circuit current

The relaxation kinetics of frog skin open circuit voltage, V_oc, and short circuit current I_sc, was studied by analyzing the effects of subjecting the tissue to sudden increments of hydrostatic pressure. Both V_oc and I_sc are perturbed by the pressure jump. Changes in V_oc can be resolved into three components: a rapid decrease (phase I), a second, additional decrease with time constant 2.2 s (phase II), and finally a very slow increase found only in some preparations. The amplitudes of phases I and II are linear in the range of pressures studied (<350 atm) and have respective pressure coefficients of −1.2 · 10⁻⁴atm⁻¹ and −3.7 · 10⁻⁴atm⁻¹.Under short circuit conditions phases I and II persist. The pressure coefficients of the amplitudes of phase I and II, −4.3 · 10⁻⁴atm⁻¹ and −5.0 · 10⁻⁴atm⁻¹, respectively, are larger than those of V_oc, but the time constant of phase II, 2.2 s, is the same. The sum of the amplitudes of phases I and II is directly proportional to I_sc when it is inhibited with ouabain. It is argued that in both electrical states pressure perturbs the same transport mechanism giving rise to phases I and II of V_oc and I_sc.The magnitude of the pressure coefficients of these processes implies that they arise from chemical reactions, rather than from simple, physical solution properties. Comparison of the pressure jump kinetics with the previous spectral analysis of the electrical fluctuations of frog skin suggests a common origin for both sets of phenomena.