@article {529,
	title = {Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography},
	journal = {Journal of the American Chemical Society},
	volume = {124},
	number = {11},
	year = {2002},
	note = {ISI Document Delivery No.: 531UMTimes Cited: 53Cited Reference Count: 79},
	month = {Mar},
	pages = {2485-2496},
	type = {Article},
	abstract = {Ultraviolet resonance Raman spectroscopy (UVRRS), electronic absorption spectroscopy, and X-ray crystallography were used to probe the nature of the binding of 2,3-dihydroxybiphenyl (DHB) to the extradiol ring-cleavage enzyme, 2,3-dihydroxybiphenyl 1,2-dioxygenase (DHBD; EC 1.13.11.39). The lowest lying transitions in the electronic absorption spectrum of DHBD-bound DHB occurred at 299 nm, compared to 305 nm for the monoanionic DHB species in buffer. In contrast, the corresponding transitions in neutral and dianionic DHB occurred at 283 and 348 nm, respectively, indicating that DHBD-bound DHB is monoanionic. These binding-induced spectral changes, and the use of custom-designed optical fiber probes, facilitated UVRR experiments. The strongest feature of the UVRR spectrum of DHB was a Y8a-like mode around 1600 cm(-1), whose position depended strongly on the protonation state of the DHB. In the spectrum of the DHBD-bound species, this feature occurred at 1603 cm-1, as observed in the spectrum of monoanionic DHB. Raman band shifts were observed in deuterated solvent, ruling out dianionic binding of the substrate. Thus, the electronic absorption and UVRRS data demonstrate that DHBD binds its catecholic substrate as a monoanion, definitively establishing this feature of the proposed mechanism of extradiol dioxygenases. This conclusion is supported by a crystal structure of the DHBD:DHB complex at 2.0 Angstrom resolution, which suggests that the substrate{\textquoteright}s 2-hydroxyl substituent, and not the 3-hydroxyl group, deprotonates upon binding. The structural data also show that the aromatic rings of the enzyme-bound DHB are essentially orthogonal to each other. Thus, the 6 nm blue shift of the transition for bound DHB relative to the monoanion in solution could indicate a conformational change upon binding. Catalytic roles of active site residues are proposed based on the structural data and previously proposed mechanistic schemes.},
	keywords = {3, 4-DIOXYGENASE, BIPHENYL, CRYSTAL-STRUCTURE, EXTRADIOL CATECHOL DIOXYGENASES, FE(II) ACTIVE-SITE, FE3+ LIGAND, LIGAND-BINDING, MECHANISM, MOLECULAR-STRUCTURE, PROTOCATECHUATE, SUBSTRATE-BINDING},
	isbn = {0002-7863},
	url = {<Go to ISI>://000174435700037},
	author = {Vaillancourt, F. H. and Barbosa, C. J. and Spiro, T. G. and Bolin, J. T. and Blades, M. W. and Turner, R. F. B. and Eltis, L. D.}
}
@article {529,
	title = {Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography},
	journal = {Journal of the American Chemical Society},
	volume = {124},
	number = {11},
	year = {2002},
	note = {ISI Document Delivery No.: 531UMTimes Cited: 53Cited Reference Count: 79},
	month = {Mar},
	pages = {2485-2496},
	type = {Article},
	abstract = {Ultraviolet resonance Raman spectroscopy (UVRRS), electronic absorption spectroscopy, and X-ray crystallography were used to probe the nature of the binding of 2,3-dihydroxybiphenyl (DHB) to the extradiol ring-cleavage enzyme, 2,3-dihydroxybiphenyl 1,2-dioxygenase (DHBD; EC 1.13.11.39). The lowest lying transitions in the electronic absorption spectrum of DHBD-bound DHB occurred at 299 nm, compared to 305 nm for the monoanionic DHB species in buffer. In contrast, the corresponding transitions in neutral and dianionic DHB occurred at 283 and 348 nm, respectively, indicating that DHBD-bound DHB is monoanionic. These binding-induced spectral changes, and the use of custom-designed optical fiber probes, facilitated UVRR experiments. The strongest feature of the UVRR spectrum of DHB was a Y8a-like mode around 1600 cm(-1), whose position depended strongly on the protonation state of the DHB. In the spectrum of the DHBD-bound species, this feature occurred at 1603 cm-1, as observed in the spectrum of monoanionic DHB. Raman band shifts were observed in deuterated solvent, ruling out dianionic binding of the substrate. Thus, the electronic absorption and UVRRS data demonstrate that DHBD binds its catecholic substrate as a monoanion, definitively establishing this feature of the proposed mechanism of extradiol dioxygenases. This conclusion is supported by a crystal structure of the DHBD:DHB complex at 2.0 Angstrom resolution, which suggests that the substrate{\textquoteright}s 2-hydroxyl substituent, and not the 3-hydroxyl group, deprotonates upon binding. The structural data also show that the aromatic rings of the enzyme-bound DHB are essentially orthogonal to each other. Thus, the 6 nm blue shift of the transition for bound DHB relative to the monoanion in solution could indicate a conformational change upon binding. Catalytic roles of active site residues are proposed based on the structural data and previously proposed mechanistic schemes.},
	keywords = {3, 4-DIOXYGENASE, BIPHENYL, CRYSTAL-STRUCTURE, EXTRADIOL CATECHOL DIOXYGENASES, FE(II) ACTIVE-SITE, FE3+ LIGAND, LIGAND-BINDING, MECHANISM, MOLECULAR-STRUCTURE, PROTOCATECHUATE, SUBSTRATE-BINDING},
	isbn = {0002-7863},
	url = {<Go to ISI>://000174435700037},
	author = {Vaillancourt, F. H. and Barbosa, C. J. and Spiro, T. G. and Bolin, J. T. and Blades, M. W. and Turner, R. F. B. and Eltis, L. D.}
}
@article {4214,
	title = {Novel and improved syntheses of 5,15-diphenylporphyrin and its dipyrrolic precursors},
	journal = {Journal of Porphyrins and Phthalocyanines},
	volume = {2},
	number = {6},
	year = {1998},
	note = {ISI Document Delivery No.: 209DJTimes Cited: 53Cited Reference Count: 66},
	month = {Nov-Dec},
	pages = {455-465},
	type = {Article},
	abstract = {Optimized syntheses of 5,15-diphenylporphyrin (DPP, 1) and its dipynolic precursors are described. A novel procedure for the synthesis of dipyrromethane (2), prepared by hydrodesulfurization of the corresponding di-2-pyrrolylthione (8), is presented, as well as an improved method to isolate large quantities of 5-phenyldipyrromethane (4), prepared by the acid-catalysed condensation of pyrrole with benzaldehyde. These dipyrromethanes are key reagents in two high-yield (2+2)-type syntheses of DPP. 5-Phenyldipyrromethane was formylated to provide 1-formyl- (11) and 1,9-diformyl-5-phenyldipyrromethane (12), and reduction of 11 provided the corresponding hydroxymethyl compound 13, These compounds (11-13), however, were much less efficient precursors to DPP. Two polypyrrolic compounds, 1,1,2,2-dipyrrolylethane (9) and 5,10-diphenyltripyrrane (10), potentially useful for the synthesis of porphyrinic macrocycles, were isolated as side-products during the dipyrromethane and 5-phenyldipyrromethane syntheses. (C) 1998 John Wiley \& Sons, Ltd.},
	keywords = {1, 10-diphenyltripyrrane, 2, 2+2 synthesis, 2-tetrapyrrolylethane, 5, 5-phenyldipyrromethane, ARYLPORPHYRINS, BIPHENYL, CHEMISTRY, COMPLEXES, dipyrromethane, macrocycles, MESO, meso-diphenylporphyrin synthesis, MESOSUBSTITUTED PORPHYRINS, METALLOPORPHYRINS, STEPWISE SYNTHESES, SUBSTITUTED PORPHYRIN},
	isbn = {1088-4246},
	url = {<Go to ISI>://000081032700001},
	author = {Bruckner, C. and Posakony, J. J. and Johnson, C. K. and Boyle, R. W. and James, Brian R. and Dolphin, D.}
}
@article {6960,
	title = {SYNTHESIS OF ISOCYANO AND (HALOALKYNYL) BIPHENYLS - NEW THERMOTROPIC LIQUID-CRYSTALS},
	journal = {Molecular Crystals and Liquid Crystals},
	volume = {198},
	year = {1991},
	note = {ISI Document Delivery No.: FN646Times Cited: 6Cited Reference Count: 913TH INTERNATIONAL LIQUID CRYSTAL CONFJUL 22-27, 1990VANCOUVER, CANADA},
	pages = {417-428},
	type = {Proceedings Paper},
	keywords = {BIPHENYL, HALOALKYNES, ISOCYANIDES, SYNTHESIS, THERMOTROPICS},
	isbn = {1542-1406},
	url = {<Go to ISI>://A1991FN64600041},
	author = {Bailey, A. L. and Bates, G. S.}
}
