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  • 1
    Electronic Resource
    Electronic Resource
    A reduced pyridine nucleotides-diaphorase activity associated to the assimilatory nitrite reductase complex from Neurospora crassa (1976)
    Springer
    Archives of microbiology 109 (1976), S. 237-242 
    Details
    ISSN: 1432-072X
    Keywords: Neurospora crassa ; Nitrite reductase ; Diaphorase ; Assimilatory ; Flavin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Neurospora crassa assimilatory NAD(P)H-nitrite reductase complex has associated a NAD(P)H-diaphorase activity. 1. This NAD(P)H-diaphorase activity can use either mammalian cytochrome c, 2,6-dichlorophenol-indophenol, ferricyanide, or menadione as electron acceptor from the reduced pyridine nucleotides, and requires flavin adenine dinucleotide for maximal activity. 2. It is inhibited by p-hydroxymercuribenzoate, 1 μM, and it is unaffected by cyanide, sulfite, or arsenite at concentrations which completely inhibit the NAD(P)H-nitrite reductase activity. 3. Flavin adenine dinucleotide specifically protects the NAD(P)H-diaphorase activities, but not the NAD(P)H-nitrite reductase activities, against thermal inactivation. 4. In vitro preincubation of the Neurospora crassa nitrite reductase complex with reduced pyridine nucleotides plus flavin adenine dinucleotide inactivates the NAD(P)H-nitrite reductase activities, but does not affect to the NAD(P)H-diaphorase activities, indicating that this nitrite reductase inactivation occurs in the part of the enzyme that contain the nitrite reducing center.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446634
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  • 2
    Electronic Resource
    Electronic Resource
    Immunological studies of ferredoxin-nitrite reductases and ferredoxin-glutamate synthases from photosynthetic organisms (1990)
    Springer
    Archives of microbiology 153 (1990), S. 230-234 
    Details
    ISSN: 1432-072X
    Keywords: Photosynthetic organisms ; Chlamydomonas reinhardii ; Ferredoxin-glutamate synthase ; Ferredoxin-nitrite reductase ; Common antigenic determinants ; Ferredoxin-binding domain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Polyclonal antiserum specific for ferredoxin-nitrite reductase (EC 1.7.7.1) from the green alga Chlamydomonas reinhardii recognized the nitrite reductase from other green algae, but did not cross-react with the corresponding enzyme from different cyanobacteria or higher plant leaves. An analogous situation was also found for ferredoxin-glutamate synthase (EC 1.4.7.1), using its specific antiserum. Besides, the antibodies raised against C. reinhardii ferredoxin-glutamate synthase were able to inactivate the ferredoxin-dependent activity of nitrite reductase from green algae. These results suggest that there exist similar domains in ferredoxin-nitrite reductases and ferredoxin-glutamate synthases from green algae. In addition, both types of enzymes share common antigenic determinants, probably located at the ferredoxin-binding domain. In spite of their physicochemical resemblances, no apparent antigenic correlation exists between the corresponding enzymes from green algae and those from higher plant leaves or cyanobacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249073
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  • 3
    Electronic Resource
    Electronic Resource
    Effect of culture conditions on the isocitrate dehydrogenase and isocitrate lyase activities in Chlamydomonas reinhardtii (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 88 (1993), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In the green alga Chlamydomonas reinhardtii, nitrogen staravation induced a reversible increase (2-fold) in NAD-isocitrate dehydrogenase (NAD-IDH; EC 1.1.1.41) and NADP-isocitrate dehydrogenase (NADP-IDH; EC 1.1.1.42) activities. Both enzymes were not affected by the concentration of CO2, the dark or the nature of the nitrogen source (nitrate, nitrite, or ammonium). When cells growing autotrophically were transferred to heterotrophic conditions, a 40% reduction of the NAD-IDH activity was detected, a 2-fold increase of NADP-IDH was observed and isocitrate lyase (ICL; EC 4.1.3.1) activity was induced. The replacement of autotrophic conditions led to the initial activity levels. NAD- and NADP-IDH activities showed markedly different patterns of increase in synchronous cultures of this alga obtained by 12 h light/12 h dark transitions. While NAD-IDH increased in the last 4 h of the dark period, NADP-IDH increased during the last 4 h of the light period, remaining constant for the rest of the cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1993.tb01377.x
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  • 4
    Electronic Resource
    Electronic Resource
    Weakly nonlinear nonaxisymmetric oscillations of capillary bridges at small viscosity (2002)
    [S.l.] : American Institute of Physics (AIP)
    Physics of Fluids 14 (2002), S. 3251-3271 
    Details
    ISSN: 1089-7666
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Weakly nonlinear nonaxisymmetric oscillations of a capillary bridge are considered in the limit of small viscosity. The supporting disks of the liquid bridge are subjected to small amplitude mechanical vibrations with a frequency that is close to a natural frequency. A set of equations is derived for accounting the slow dynamics of the capillary bridge. These equations describe the coupled evolution of two counter-rotating capillary waves and an associated streaming flow. Our derivation shows that the effect of the streaming flow on the capillary waves cannot be a priori ignored because it arises at the same order as the leading (cubic) nonlinearity. The system obtained is simplified, then analyzed both analytically and numerically to provide qualitative predictions of both the relevant large time dynamics and the role of the streaming flow. The case of parametric forcing at a frequency near twice a natural frequency is also considered. © 2002 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1495870
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  • 5
    Electronic Resource
    Electronic Resource
    Linear oscillations of weakly dissipative axisymmetric liquid bridges (1994)
    [S.l.] : American Institute of Physics (AIP)
    Physics of Fluids 6 (1994), S. 438-450 
    Details
    ISSN: 1089-7666
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Linear oscillations of axisymmetric capillary bridges are analyzed for large values of the modified Reynolds number C−1. There are two kinds of oscillating modes. For nearly inviscid modes (the flow being potential, except in boundary layers), it is seen that the damping rate −ΩR and the frequency ΩI are of the form ΩR=ω1C1/2+ω2C+O(C3/2) and ΩI=ω0+ω1C1/2+O(C3/2), where the coefficients ω0(approximately-greater-than)0, ω1〈0, and ω2〈0 depend on the aspect ratio of the bridge and the mode being excited. This result compares well with numerical results if C(approximately-less-than)0.01, while the leading term in the expansion of the damping rate (that was already known) gives a bad approximation, except for unrealistically large values of the modified Reynolds number (C(approximately-less-than)10−6). Viscous modes (involving a nonvanishing vorticity distribution everywhere in the liquid bridge), providing damping rates of the order of C, are also considered.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.868342
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  • 6
    Electronic Resource
    Electronic Resource
    Chaotic oscillations in a nearly inviscid, axisymmetric capillary bridge at 2:1 parametric resonance (1998)
    [S.l.] : American Institute of Physics (AIP)
    Physics of Fluids 10 (1998), S. 1088-1103 
    Details
    ISSN: 1089-7666
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We consider the 2:1 internal resonances (such that Ω1〉0 and Ω2(similar, equals)2Ω1 are natural frequencies) that appear in a nearly inviscid, axisymmetric capillary bridge when the slenderness Λ is such that 0〈Λ〈π (to avoid the Rayleigh instability) and only the first eight capillary modes are considered. A normal form is derived that gives the slow evolution (in the viscous time scale) of the complex amplitudes of the eigenmodes associated with Ω1 and Ω2, and consists of two complex ODEs that are balances of terms accounting for inertia, damping, detuning from resonance, quadratic nonlinearity, and forcing. In order to obtain quantitatively good results, a two-term approximation is used for the damping rate. The coefficients of quadratic terms are seen to be nonzero if and only if the eigenmode associated with Ω2 is even. In that case the quadratic normal form possesses steady states (which correspond to mono- or bichromatic oscillations of the liquid bridge) and more complex periodic or chaotic attractors (corresponding to periodically or chaotically modulated oscillations). For illustration, several bifurcation diagrams are analyzed in some detail for an internal resonance that appears at Λ(similar, equals)2.23 and involves the fifth and eighth eigenmodes. If, instead, the eigenmode associated with Ω2 is odd, and only one of the eigenmodes associated with Ω1 and Ω2 is directly excited, then quadratic terms are absent in the normal form and the associated dynamics is seen to be fairly simple. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.869634
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  • 7
    Electronic Resource
    Electronic Resource
    Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from Chlamydomonas reinhardtii (2003)
    Oxford, UK : Munksgaard International Publishers
    Physiologia plantarum 118 (2003), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Chloroplastic NADP-isocitrate dehydrogenase isoenzyme (NADP-IDH2; EC 1.1.1.42) from the eukaryotic microalga Chlamydomonas reinhardtii was purified to electrophoretic homogeneity by a procedure which included affinity chromatography on Red-Sepharose as the key step. The 70-kDa isoenzyme was found to be a dimer formed by 40-kDa subunits. Antibodies raised against a recombinant tobacco cytosolic NADP-IDH cross-reacted strongly with the cytosolic NADP-IDH1 and weakly with the NADP-IDH2 isoenzyme from this alga. NADPH and GTP were found to inhibit both isoenzymes, whereas intermediates of the tricarboxylic acid cycle, glycolysis or reductive pentose phosphate cycle had no significant effect. The simultaneous presence of isocitrate and Mn2+ protected NADP-IDH2 against thermal inactivation or inhibition by reagents specific for arginine or lysine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2003.00082.x
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  • 8
    Electronic Resource
    Electronic Resource
    Effect of nitrogen starvation on ammonium assimilation by Chlamydomonas reinhardtii (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 75 (1989), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In nitrogen-starved Chlamydomonas reinhardtii, wild type, strain 21 gr cells, consumption of nitrate, nitrite and ammonium may occur in the dark in the absence of an added carbon source. Consumption of ammonium in the dark was about 25% higher than in the light, while consumption of nitrate or nitrite in the dark was lower than in the light.N starvation produced a linear increase with time in the intracellular level of glutamine synthetase (GS, EC 6.3.2.1) and glutamate synthase (NADH-GOGAT, EC 1.4.1.14 and ferredoxin-GOGAT, EC 1.4.7.1) activities in C. reinhardtii. The effect on GS1 (3-fold) and NADH-GOGAT (4.5-fold) was higher than that on GS2 (1.5-fold) and ferredoxin-GOGAT (1.5-fold).Experiments with methylammonium, L-methionine-D, L-sulfoximine (MSX) and azaserine suggest that: 1) Ammonium itself decreases the intracellular levels of glutamine synthetase and ferredoxin-glutamate synthase activities; and 2) a metabolite resulting from ammonium assimilation by the alga may be a negative modulator of NADH-glutamate synthase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1989.tb06182.x
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  • 9
    Electronic Resource
    Electronic Resource
    Purification and molecular properties of nitrite reductase from Anabaena sp. 7119 (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 52 (1981), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Ferredoxin-nitrite reductase (EC 1.7.7.1.) from the cyanobacteria Anabaena sp. 7119 has been purified 763-fold with a specific activity of 21.5 units/nig protein (0.358 μkatals/mg). The enzyme has a molecular mass of 52,000 daltons with a Stokes radius of 3.09 nm and a sedimentation coefficient of 4.07 S. The cellular level of nitrite reductase activity gradually increases in response to the addition of increasing amounts of iron to the culture medium.When partially purified nitrite reductase preparations are subjected to sucrose-density-gradient centrifugation there is a dose correspondence between nitrite reductase activity and absorbance at 400 nm. This suggests the association of a heme chromophore with the enzyme. Furthermore, the presence of an iron-sulfur center is suggested by a close association of acid-labile sulfide with nitrite reductase activity. Carbon monoxide inhibits nitrite reductase activity. The nature and kinetics of this reaction are comparable to other siroheme-containing nitrite reductases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1981.tb06026.x
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  • 10
    Electronic Resource
    Electronic Resource
    Homology predicted structure and functional interaction of ferredoxin from the eukaryotic alga Chlamydomonas reinhardtii with nitrite reductase and glutamate synthase (2000)
    Springer
    JBIC 5 (2000), S. 713-719 
    Details
    ISSN: 1432-1327
    Keywords: Ferredoxin Glutamate synthase Homology modelling Nitrite reductase Site-directed mutagenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. Ferredoxin (Fd) from Chlamydomonas reinhardtii is composed of 94 amino-acid residues and a [2Fe-2S] cluster. The homology modelling technique has been used to predict the tertiary structure of C. reinhardtii Fd. The overall structure shows the typical fifth-stranded β-grasp plus two additional β-sheets and three α-helices. Site-directed mutagenesis of recombinant Fd has allowed us to obtain four point mutants and one double mutant – all mutations being located in the short α-helix at the carboxy-terminal segment – as well as a triple mutant affected on helix α1. Cross-linking studies and measurement of enzymatic activities reveal that the residues changed are critical for the interaction of Fd with glutamate synthase (GOGAT) and nitrite reductase (NiR). Potentiometric analyses of the Fd mutants show that the replacement of glutamate in position 91 drastically changes the redox potential value (70 mV), thereby suggesting that such a glutamate can modulate the reactivity of Fd towards its reaction partners. According to results herein presented, the reported mutations modify the electrostatic interactions within the complex formed between Fd and GOGAT or NiR.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750000160
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