Correction to: Modern Pathology (2003) 16(11), 1067–1075 Owing to an oversight on the authors' part, one of the author's names was reported incorrectly. The author's name is Alfredo Zito, not ...‘Alfredo Vito’.
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GEOZS, IJS, IMTLJ, KILJ, KISLJ, NLZOH, NUK, OILJ, PNG, SAZU, SBCE, SBJE, UILJ, UL, UM, UPCLJ, UPUK, ZAGLJ, ZRSKP
Biological toxicity testing is a rapidly expanding field involving numerous bioanalytical techniques. The enzymatic biosensors are valuable screening tools to identify pollutants and/or toxic agents ...in the environment and/or in food matrices, thus representing a valid alternative to animal testing in analytical toxicology. Inhibition based biosensors here presented have been proved to represent alternative assays for the toxicity evaluation of warfare agents and endocrine disrupting chemicals as well as algal toxins (phycotoxins) in the contamined sea foods (mainly clams and other mollusks). Results obtained by inhibition studies performed by means of several enzymatic biosensors indicate the reliability of the proposed method and the possibility to extend such an experimental approach to other toxicants as a simple, rapid and cheap biotest, to be used easily also "on the spot".
In the hydrophobic patch of azurin from Pseudomonas aeruginosa, an electric dipole was created by changing Met44 into Lys and Met64 into Glu. The effect of this dipole on the electron‐transfer ...properties of azurin was investigated. From a spectroscopic characterization (NMR, EPR and ultraviolet‐visible) it was found that both the copper site and the overall structure of the Lys44, Glu64azurin were not disturbed by the two mutations. A small perturbation of the active site at high pH, similar to that observed for Lys44azurin, occurs in the double mutant. At neutral pH the electron‐self‐exchange rate constant of the double mutant shows a decrease of three orders of magnitude compared with the wild‐type value. The possible reasons for this decrease are discussed. Electron transfer with the proposed physiological redox partners cytochrome c551, and nitrite reductase have been investigated and the data analyzed in the Marcus framework. From this analysis it is confirmed that the hydrophobic patch of azurin is the interaction site with both partners, and that cytochrome c551 uses its hydrophobic patch and nitrite reductase a negatively charged surface area for the electron transfer.
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BFBNIB, DOBA, FZAB, GIS, IJS, IZUM, KILJ, NLZOH, NUK, OILJ, PILJ, PNG, SAZU, SBCE, SBMB, SIK, UILJ, UKNU, UL, UM, UPUK
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