@article {706,
	title = {Thermal activation of hydrocarbon C-H bonds by Cp*M(NO) complexes of molybdenum and tungsten},
	journal = {Accounts of Chemical Research},
	volume = {36},
	number = {4},
	year = {2003},
	note = {ISI Document Delivery No.: 669GJTimes Cited: 54Cited Reference Count: 36},
	month = {Apr},
	pages = {223-233},
	type = {Review},
	abstract = {Gentle thermolysis of appropriate Cp*M(NO)(hydrocarbyl)(2) complexes (Cp* = eta(5)-C5Me5) of molybdenum and tungsten results in loss of hydrocarbon and the transient formation of 16-electron Cp*M(NO)-containing complexes such as Cp*M(NO)(alkylidene), Cp*M(NO)(eta(2)-benzyne), Cp*M(NO)(eta(2)-acetylene), and Cp*M(NO)(eta(2)-allene) (M = Mo, W). These intermediates effect the single, double, or triple activation of hydrocarbon C-H bonds intermolecularly, the first step of these activations being the reverse of the transformations by which they were generated. This Account summarizes the various types of C-H activations that have been effected with these nitrosyl complexes and also describes the results of kinetic, mechanistic, and theoretical investigations of these processes.},
	keywords = {ALKANES, ALKYLIDENE COMPLEXES, ARENES, CHEMISTRY, INTERMEDIATE, NITROSYL, REACTIVITY, REDUCTIVE ELIMINATION, THERMOLYSIS, TRANSITION-METAL BONDS},
	isbn = {0001-4842},
	url = {<Go to ISI>://000182343300001},
	author = {Pamplin, C. B. and Legzdins,Peter}
}
@article {537,
	title = {Parallel modes of C-H bond activation initiated by Cp*Mo(NO)(CH2CMe3)(C6H5) at ambient temperatures},
	journal = {Journal of the American Chemical Society},
	volume = {124},
	number = {33},
	year = {2002},
	note = {ISI Document Delivery No.: 584EVTimes Cited: 15Cited Reference Count: 32},
	month = {Aug},
	pages = {9680-9681},
	type = {Article},
	keywords = {ALKANES, ARYNE COMPLEXES, CHEMISTRY, HYDROCARBONS, INTERMEDIATE, METAL-COMPLEXES, MOLYBDENUM, REACTIVITY, THERMOLYSIS, TUNGSTEN ALKYLIDENE COMPLEXES},
	isbn = {0002-7863},
	url = {<Go to ISI>://000177455000012},
	author = {Wada, K. and Pamplin, C. B. and Legzdins,Peter}
}
@inbook {423,
	title = {Pre-steady-state kinetics of enzymatic reactions studied by electrospray mass spectrometry with on-line rapid-mixing techniques},
	booktitle = {Enzyme Kinetics and Mechanism, Pt F: Detection and Characterization of Enzyme Reaction Intermediates},
	series = {Methods in Enzymology},
	volume = {354},
	year = {2002},
	note = {ISI Document Delivery No.: BV53FTimes Cited: 8Cited Reference Count: 42Review525 B STREET, SUITE 1900, SAN DIEGO, CA 92101-4495 USA},
	pages = {50-64},
	publisher = {Academic Press Inc},
	organization = {Academic Press Inc},
	address = {San Diego},
	keywords = {ACID, BETA-LACTAMASE, CATALYSIS, COMPLEXES, INTERMEDIATE, ION, IONIZATION, MECHANISM, REAL-TIME},
	isbn = {0076-6879},
	url = {<Go to ISI>://000179267700003},
	author = {Konermann, L. and Douglas, D. J.}
}
@article {5004,
	title = {The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: A study by electrospray ionization mass spectrometry},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {12},
	number = {3},
	year = {2001},
	note = {ISI Document Delivery No.: 408WBTimes Cited: 45Cited Reference Count: 51},
	month = {Mar},
	pages = {317-328},
	type = {Article},
	abstract = {The methanol-induced conformational transitions under acidic conditions for beta -lactoglobulin, cytochrome c, and ubiquitin, representing three different classes of proteins with beta -sheets, alpha -helices, and both alpha -helices and beta -sheets, respectively, are studied under equilibrium conditions by electrospray ionization mass spectrometry (ESI-MS). The folding states of proteins in solution are monitored by the charge state distributions that they produce during ESI and by hydrogen/deuterium (H/D) exchange followed by ESI-MS. The changes in charge state distributions are correlated with earlier studies by optical and other methods which have shown that, in methanol, these proteins form partially unfolded intermediates with induced ct-helix structure. Intermediate states formed at about 35\% methanol concentration are found to give bimodal charge state distributions. The same rate of H/D exchange is shown by the two contributions to the bimodal distributions. This suggests the intermediates are highly flexible and may consist of a mixture of two or more rapidly interconverting conformers. H/D exchange of proteins followed by ESI-MS shows that helical denatured states, populated at around 50\% methanol concentration, transform into more protected structures with further increases in methanol concentration, consistent with previous circular dicroism studies. These more protected structures still produce high charge states in ESI, similar to those of the fully denatured proteins. (C) 2001 American Society for Mass Spectrometry.},
	keywords = {2-DIMENSIONAL NMR, ALPHA-HELIX, AMIDE HYDROGEN-EXCHANGE, COMPLETE SEQUENCE, DENATURED STATES, DEUTERIUM-EXCHANGE, INTERMEDIATE, MYOGLOBIN, PROTEIN, SOLVENT},
	isbn = {1044-0305},
	url = {<Go to ISI>://000167349200010},
	author = {Babu, K. R. and Moradian, A. and Douglas, D. J.}
}
@article {4314,
	title = {Equilibrium unfolding of proteins monitored by electrospray ionization mass spectrometry: Distinguishing two-state from multi-state transitions},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {12},
	number = {8},
	year = {1998},
	note = {ISI Document Delivery No.: ZJ143Times Cited: 79Cited Reference Count: 59},
	pages = {435-442},
	type = {Article},
	abstract = {The acetic acid-induced unfolding of cytochrome c (cyt c) and apomyoglobin (aMb) are studied under equilibrium conditions by electrospray ionization (ESI) mass spectrometry (MS), The folding states of the proteins in solution are monitored by the charge state distributions that they produce during ESI, A tightly folded protein shows lower charge states than the same protein in an unfolded conformation. The ESI-MS data presented in this study show that during the denaturation of cyt c, only two distinct charge state distributions are observed. These can be attributed to the native and to the acid-unfolded conformation, respectively. In the transition region where the folded and the unfolded conformation are both present in solution, these two distributions are observed simultaneously, thus giving rise to a bimodal ESI mass spectrum. These data reflect a highly cooperative (two state) folding behavior. In contrast, the acid-induced unfolding of aMb is accompanied by gradual shifts in the maxima of the observed charge state distribution. This indicates a non cooperative unfolding behavior involving multiple protein conformations. The observations made here suggest that ESI-MS might be a general method for assessing the cooperativity of protein unfolding transitions. This study also addresses the issue of {\textquoteright}secondary{\textquoteright} solvent effects for ESI-MS studies on the acid-induced unfolding of proteins. These effects influence the ESI charge state distribution without being related to conformational changes of the protein in solution and could potentially complicate the interpretation of ESI mass spectra, Data obtained for bovine pancreatic trypsin inhibitor and ubiquitin indicate that secondary solvent effects influence the observed charge state distributions only to a very minor extent between pH 8.5 and 2.5. (C) 1998 John Wiley \& Sons, Ltd.},
	keywords = {CONFORMATIONAL-CHANGES, CYTOCHROME-C, FERRICYTOCHROME-C, FOLDING, HYDROGEN-DEUTERIUM EXCHANGE, INTERMEDIATE, MOLECULAR-BASIS, MOLTEN GLOBULE, NMR-SPECTROSCOPY, POSITIVE-ION, STRUCTURAL CHARACTERIZATION},
	isbn = {0951-4198},
	url = {<Go to ISI>://000073183800005},
	author = {Konermann, L. and Douglas, D. J.}
}
@article {4407,
	title = {Metal-based chirality and spin state change in 16-electron CpML2 systems: a computational study of CpW(NO)(PH3)},
	journal = {Chemical Communications},
	number = {17},
	year = {1998},
	note = {ISI Document Delivery No.: 116QXTimes Cited: 11Cited Reference Count: 35},
	month = {Sep},
	pages = {1903-1904},
	type = {Article},
	abstract = {Density functional theory calculations indicate that CpW(NO)(PH3) possesses a planar triplet ground state, a result with significant implications for the inversion of configuration of 16e, d(6) CpML2 species.},
	keywords = {alkane, ALKYL, BOND ACTIVATION, C-H ACTIVATION, EFFECTIVE CORE POTENTIALS, INTERMEDIATE, IRIDIUM(III) COMPLEXES, METHANE, MOLECULAR CALCULATIONS, REACTIVITY},
	isbn = {1359-7345},
	url = {<Go to ISI>://000075737000060},
	author = {Smith, K. M. and Poli, R. and Legzdins,Peter}
}
@article {4030,
	title = {Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry},
	journal = {Biochemistry},
	volume = {36},
	number = {21},
	year = {1997},
	note = {ISI Document Delivery No.: XB321Times Cited: 74Cited Reference Count: 43},
	month = {May},
	pages = {6448-6454},
	type = {Article},
	abstract = {The acid-induced denaturation of holo-myoglobin (hMb) following a pH-jump from 6.5 to 3.2 has been studied by electrospray ionization (ESI) mass spectrometry in combination with a continuous flow mixing technique (time-resolved ESI MS). Different protein conformations are detected by the different charge state distributions that they generate during ESI. The changes in intensity of the peaks in the mass spectrum as a function of time can be described by two exponential lifetimes of 0.38 +/- 0.06 s and 6.1 +/- 0.5 s, respectively. The acid-induced denaturation of hMb was also studied in stopped-flow experiments by monitoring changes in the Soret absorption. The lifetimes measured by this method are in good agreement with those obtained by time-resolved ESI MS. The shorter lifetime is associated with the formation of a transient intermediate which shows the mass of the intact heme-protein complex but leads to the formation of much higher charge states during ESI than native hMb at pH 6.5. This form of hMb has an absorption spectrum similar to that of the native protein, indicating a relatively unperturbed chromophore environment inside the heme binding pocket. The intermediate can thus be characterized as an unfolded form of hMb with essentially intact heme-protein interactions. The longer of the two lifetimes is associated with the formation of a product which has a blue-shifted absorption spectrum with a much lower maximum absorption coefficient than observed for native hMb. In the ESI mass spectrum, this product appears as the apoprotein with high charge states which indicates the disruption of the native heme-protein interactions and a considerable degree of unfolding compared to native apo-myoglobin. The mechanism of acid-induced denaturation of hMb, therefore, appears to follow the sequence (heme protein)(native) {\textendash}> (heme-protein)(unfolded) {\textendash}> heme + (protein)(unfolded).},
	keywords = {APOMYOGLOBIN, HEME-PROTEINS, INTERMEDIATE, IONS, LOW PH, METMYOGLOBIN, PROBING CONFORMATIONAL-CHANGES, RESOLUTION, SPERM WHALE, STABILITY},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1997XB32100022},
	author = {Konermann, L. and Rosell, F. I. and Mauk, A. G. and Douglas, D. J.}
}
@article {3430,
	title = {A NOVEL SURFACE-STRUCTURE - RH(111)-(ROOT-7X-ROOT-7)R19.1-DEGREES-P},
	journal = {Journal of the American Chemical Society},
	volume = {117},
	number = {49},
	year = {1995},
	note = {ISI Document Delivery No.: TK382Times Cited: 7Cited Reference Count: 26},
	month = {Dec},
	pages = {12344-12345},
	type = {Note},
	keywords = {acetylene, chemisorption, CYCLOTRIMERIZATION, ENERGY-ELECTRON-DIFFRACTION, HETEROCYCLIZATION SITES, INTERMEDIATE, MOLECULAR PATHWAYS, palladium, SUBSTRATE, SULFIDED PD(111) SURFACE},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1995TK38200041},
	author = {Liu, W. and Wong, K. C. and Mitchell, K. A. R.}
}
@article {2925,
	title = {CIRCULAR-DICHROISM ANALYSIS OF A SYNTHETIC PEPTIDE CORRESPONDING TO THE ALPHA,ALPHA-CORNER MOTIF OF HEMOGLOBIN},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {196},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: MC105Times Cited: 1Cited Reference Count: 16},
	month = {Oct},
	pages = {435-439},
	type = {Article},
	keywords = {ALPHA-HELIX, GLOBULAR-PROTEINS, INTERMEDIATE, POLYPEPTIDE-CHAIN, SECONDARY STRUCTURE, STABILITY},
	isbn = {0006-291X},
	url = {<Go to ISI>://A1993MC10500062},
	author = {Tsai, F. C. S. and Sherman, J. C.}
}
@article {2871,
	title = {SYNTHESES OF 2-DEOXY-2-FLUORO MONOSACCHARIDE AND OLIGOSACCHARIDE GLYCOSIDES FROM GLYCALS AND EVALUATION AS GLYCOSIDASE INHIBITORS},
	journal = {Carbohydrate Research},
	volume = {249},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: MD387Times Cited: 41Cited Reference Count: 34},
	month = {Oct},
	pages = {77-90},
	type = {Article},
	abstract = {Several fluorinated oligosaccharides, including 2-deoxy-2-fluoro derivatives of cellobiose, maltose, and maltotriose were synthesized by the action of fluorine or acetyl hypofluorite on the corresponding glycal peracetates. Temperature effects on the stereoselectivities of these reactions were examined. Addition of acetyl hypofluorite to several 2-substituted glycals in the gluco or galacto series gave 2,2-disubstituted arabino- or lyxo-hexose derivatives; 3,4,6-tri-O-acetyl-2-fluoro-D-glucal or the analogous galactal yielded 2-deoxy-2,2-difluoro arabino- or lyxo-hexose peracetates, whereas 2-acetoxy-3,4,6-tri-O-acetyl-D-glucal or the analogous galactal gave 2(R)-2-acetoxy-2-fluoro-arabino- or lyxo-hexose peracetates, respectively. 2-Acetamido-3,4,6-tri-O-acetyl-D-glucal gave 2(R)-2-acetamido-2-acetoxy-3,4,6-tri-O-acetyl-alpha-D-arabino-hexopyrano syl fluoride. 2,4-Dinitrophenyl 2-deoxy-2-fluoro-beta-cellobioside was an inactivator of the exoglucanase from Cellulomonas fimi while 2-deoxy-2-fluoro-alpha-maltosyl and alpha-maltotriosyl fluorides were slow substrates of human pancreatic alpha-amylase and rabbit muscle glycogen debranching enzyme, respectively.},
	keywords = {ACETYL HYPOFLUORITE, beta-glucosidase, CATALYTIC FLEXIBILITY, DERIVATIVES, ENZYME, GLYCOSYLASES, hydration, INTERMEDIATE, MECHANISM},
	isbn = {0008-6215},
	url = {<Go to ISI>://A1993MD38700007},
	author = {McCarter, J. D. and Adam,Michael J. and Braun, C. and Namchuk, M. and Tull, D. and Withers, S. G.}
}
