myo-Inositol monophosphatase (IMP) is a soluble, Li(+)-sensitive protein that catalyzes the removal of a phosphate from myo-inositol phosphate substrates. IMP is required for de novo inositol synthesis from glucose 6-phosphate and for breakdown of inositol trisphosphate, a second messenger generated by the phosphatidylinositol signaling pathway. We cloned the IMP gene from tomato (LeIMP) and show that the plant enzyme is encoded by a small gene family. Three different LeIMP cDNAs encode distinct but highly conserved IMP enzymes that are catalytically active in vitro. Similar to the single IMP from animals, the activities of all three LeIMPs are inhibited by low concentrations of LiCl. LeIMP mRNA levels are developmentally regulated in seedlings and fruit and in response to light. Immunoblot analysis detected three proteins of distinct molecular masses (30, 29, and 28 kD) in tomato; these correspond to the predicted molecular masses of the LeIMPs encoded by the genes. Immunoreactive proteins in the same size range are also present in several other plants. Immunolocalization studies indicated that many cell types within seedlings accumulate LeIMP proteins. In particular, cells associated with the vasculature express high levels of LeIMP protein; this may indicate a coordinate regulation between phloem transport and synthesis of inositol. The presence of three distinct enzymes in tomato most likely reflects the complexity of inositol utilization in higher plants.

A unique distorted trigonal-bipyramidal geometry observed for the non-heme iron center in protocatechuate 3,4-dioxygenase (3,4-PCD) was carefully examined utilizing a sterically hindered iron salen complex, which well reproduces the endogenous His2Tyr2 donor set with water as an external ligand. X-ray crystal structures of a series of iron model complexes containing bis(3,5-dimesitylsalicylidene)-1,2-dimesitylethylenediamine indicate that a distorted trigonal-bipyramidal geometry is achieved upon binding of water as an external ligand. The extent of a structural change of the iron center from a preferred square-pyramidal to a distorted trigonal-bipyramidal geometry varies with the external ligand that is bound in the order Cl << EtO < H2O, which is consistent with the spectrochemical series. The distortion in the model system is not due to steric repulsions but electronic interactions between the external ligand and the iron center, as evidenced from the X-ray crystal structures of another series of iron model complexes with a less-hindered bis(3-xylylsalicylidene)-1,2-dimesitylethylenediamine ligand, as well as by density functional theory calculations. Further spectroscopic investigations indicate that a unique distorted trigonal-bipyramidal geometry is indeed maintained even in solution. The present model study provides a new viewpoint that a unique distorted trigonal-bipyramidal iron site might not be preorganized by a 3,4-PCD protein but could be electronically induced upon the binding of an external hydroxide ligand to the iron(III) center. The structural change induced by the external water ligand is also discussed in relation to the reaction mechanism of 3,4-PCD.

Static properties of a bose-fermi mixture of trapped potassium atoms are studied in terms of coupled Gross-Pitaevskii and Thomas-Fermi equations for both repulsive and attractive bose-fermi interatomic potentials. Qualitative estimates are given for solutions of the coupled equations, and the parameter regions are obtained analytically for the boson-density profile change and for the boson/fermion phase separation. Especially, the parameter ratio Rint is found that discriminates the region of the large boson-profile change. These estimates are applied for numerical results for the potassium atoms and checked their consistency. It is suggested that a small fraction of fermions could be trapped without an external potential for the system with an attractive boson-fermion interaction.

Paramagnetic signals have been observed in the 1 H NMR spectra of copper-containing nitrite reductases (M r ≈ 110 kDa), which provide a detailed fingerprint of the type 1 centres in these proteins.

Aeration of a two-electron reduced cytochrome c oxidase provides a species with two Raman bands at 804 and 356 cm À1 , identifying it as the second intermediate following the O 2 -bound species in the enzymatic O 2 reduction process. It degrades directly to the fully oxidized form with a half-life time of 70 min at pH 8.0. The stability suggests an effective insulation for the active site in an extremely high oxidation state (Fe 4þ with one oxidative equivalent nearby) against spontaneous electron leaks, which would dissipate proton motive force. The formation and degradation of the second intermediate are pH-dependent.

The 11-Gbps 80-km transmission performance of a zero-chirp silicon Mach-Zehnder modulator has been characterized. The zero-chirp characteristic of the silicon modulator is confirmed in the constellation measurement, and gives high tolerance both for positive and negative chromatic dispersion. A low-dispersion-penalty transmission up to 80 km using the 11-Gbps non return-to-zero on-off-keying format is confirmed via bit-error-rate measurements with a performance comparable to that of a commercial lithium-niobate modulator. The dispersion tolerance at 2-dB power penalty for a bit-error-rate of 10(-3) is more than ± 950 ps/nm. Further, 22.3-Gbps binary phase-shift-keying is demonstrated, and the back-to-back power penalty with respect to the lithium-niobate modulator is less than 0.5 dB.

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A laticifer is a cell involved in plant defense against biotic stresses such as herbivores and microorganisms; however, its gene expression is poorly understood. We compared protein accumulation and transcriptomes among laticifers of lignified and unlignified organs of mulberry (Morus alba), which has a non-articulated, branched type of laticifer. LA-a (equivalent to MLX56) and its homolog LA-b (insecticidal chitinase-like proteins containing two chitin-binding domains) were major proteins in laticifers of unlignified organs, and another protein (LA-c) was a major protein in laticifers of lignified organs. Purification, cDNA cloning, and bioassay of LA-c revealed that LA-c was an acidic class I chitinase having antifungal but not insecticidal activity. Comparative mRNA-Seq analysis using a GS-FLX revealed transcripts of other possible defense-related proteins. Jacalin-like lectin, galacturonase-inhibitor, and pathogenesis-related proteins were also abundant; however, the relative amounts differed among laticifers of lignified and unlignified organs. The results suggest a discontinuous laticifer network in planta and adaptation to different potential enemies among these organs.