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1.
Neutron irradiation of Cp2MoCl2 for 24 h afforded the radiotracer Cp299MoCl2 which was characterised by UV–Vis spectroscopy and thin layer chromatography. Binding experiments with the thiol containing protein human serum albumin (HSA) or calf thymus DNA, were monitored for 99Mo using a gamma counter. Under the conditions investigated, molar ratios of binding of 0.2:1 (Cp2MoCl2:DNA) and 9.4:1 (Cp2MoCl2:HSA) were calculated. The results are consistent with in vitro coordination studies that have shown strong preferential interaction of Cp2MoCl2 with thiols versus other donor sites in biomolecules including DNA. 相似文献
2.
P. I. H. Bastiaens S. G. Mayhew E. M. O'Naulláin A. van Hoek A. J. W. G. Visser 《Journal of fluorescence》1991,1(2):95-103
Both a mode-locked argon-ion laser and synchrotron radiation were used as excitation sources to obtain time-resolved polarized fluorescence of the two FAD cofactors in electron transferring flavoprotein fromMegasphaera elsdenii. Red-edge excited and blue-edge detected fluorescence anisotropy decay curves did not contain a fast relaxation process which was observed upon mainband excitation and detection. This relaxation was assigned to homo-energy transfer between the two FAD cofactors. Failure of energy transfer as observed with edge spectroscopy on this protein excludes restricted reorientational motion of the flavins as a possible mechanism of depolarization. From the global analysis of the fluorescence anisotropy decay surface obtained at multiple excitation and detection wavelengths, the distance between and the relative orientation of the flavins could be estimated. The methodology described has general applicability in other multichromophoric biopolymers and has the potential to acquire accurate geometrical parameters in these systems. 相似文献
3.
We prove for a large class of tilings that, given a finite tile set, if it is possible to tile Euclideann-space with isometric copies of this set, then there is a tiling with the ‘local isomorphism property’.
Research supported in part by NSF Grant No. DMS-9001475. 相似文献
4.
5.
Oxidation of cysteine, glutathione and ascorbate by photoexcited proteins from normal and cataractous lenses was investigated using electron paramagnetic resonance in combination with spin trapping. We report that illumination of these proteins in pH 7 buffer with light > 300 nm in the presence of thiols (RSH) and a spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO), afforded DMPO/S-cysteine and DMPO/SG adducts, suggesting the formation of the corresponding thiyl radicals. In a nonbuffered aqueous solution, illumination of the proteins and glutathione also produced superoxide detected as a DMPO/O2H adduct. Irradiation of these proteins in the presence of ascorbate generated ascorbate radical. We conclude that chromophores present in the natural normal and cataractous lenses are capable of initiating photooxidative processes involving endogenous thiols and ascorbic acid. This observation may be pertinent to UV-induced development of cataract. 相似文献
6.
Abstract Porphyrins, which may be introduced into the eye as a result of abnormal porphyrin metabolism (uroporphyrin–Uro) or when used in the diagnosis or photodynamic therapy of certain tumors, including intraocular tumors (hematoporphyrin–Hp and'hematoporphyrin derivative'–Hpd and mesotetra( P -sulfonatophenyl)porphyrin–TPPS) are efficient photosensitizers in biological systems. We have been studying the potential phototoxic side effects of these drugs in the lens of the eye. Encapsulated in the human lens is a mixture of soluble protein crystallins. With little turnover of protein in the lens, any photosensitized modifications will accumulate and may result in an opacification of the lens. To evaluate the potential of different porphyrins to induce such damage, a series of porphyrins were photolyzed (transmission above 295 nm) in the presence of calf lens protein (2 mg m−1 ). Marked photopolymerization and histidine destruction were observed for the lens protein photolyzed in the presence of all of the drugs. We have found that the relative effectiveness of the following porphyrins to induce that damage is: Uro = TPPS Hpd = Hp. Both the singlet oxygen quencher, azide, and the free radical scavenger, penicillamine, decrease this photosensitized oxidative damage to lens protein. TPPS binds significantly to lens protein and this binding leads to conformational changes in that protein. 相似文献
7.
de la Vaissiere C Luth V Abrams GS Amidei D Baden AR Barklow T Boyarski AM Boyer J Breidenbach M Burchat P Burke DL Butler F Dillon JW Dorfan JM Feldman GJ Gidal G Gladney L Gold MS Goldhaber G Golding LG Hanson G Haggerty J Herrup D Himel T Hollebeek RJ Innes WR Jaros JA Juricic I Kadyk JA Klein SR Lankford AJ Larsen RR LeClaire BW Levi ME Lockyer NS Matteuzzi C Nelson ME Ong RA Perl ML Richter B Ross MC Rowson PC Schaad T Schellman H Schmidke WB Sheldon PD Trilling GH Yelton JM Wood DR 《Physical review letters》1985,54(19):2071-2074
8.
Reipa V Mayhew MP Holden MJ Vilker VL 《Chemical communications (Cambridge, England)》2002,(4):318-319
Spectroelectrochemistry measurements are used to demonstrate that active site mutation and binding of an non-natural substrate to P450cam (CYP101) reduces the shift in the redox potential caused by substrate-binding, and thereby results in slower catalytic turnover rate relative to wild-type enzyme with the natural camphor substrate. 相似文献
9.
Joan E. Roberts Stephen J. Atherton James Dillon 《Photochemistry and photobiology》1990,52(4):845-848
Previous studies have shown that mesotetra(p-sulfonatophenyl)porphine (TPPS) binds to lens proteins. This characteristic should increase the residence time of the sensitizer in the lens and therefore enhance the probability of inducing photooxidative damage to that tissue in vivo. Subsequent in vivo studies have verified that contention. The present studies were performed to determine the effect of such binding on the spectroscopy and photophysics of the porphyrins. It was found that the binding of TPPS (1) quenches the fluorescence of lens proteins, (2) causes a shift in the ground state absorption spectra, fluorescence excitation spectra and the triplet excited state spectrum of TPPS to longer wavelengths and (3) results in an increase in the triplet state lifetime of TPPS. In the presence of the isolated crystallins the average triplet lifetime increases in the following order: gamma less than beta less than alpha. 相似文献
10.