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Results: 1-10 |
Results: 10
The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity
Authors: Funhoff, EG Klaassen, CHW Samyn, B Van Beeumen, J Averill, BA
Citation: Eg. Funhoff et al., The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity, CHEMBIOCHEM, 2(5), 2001, pp. 355-363
Mutational analysis of the interaction between active site residues and the loop region in mammalian purple acid phosphatases
Authors: Funhoff, EG Ljusberg, J Wang, YL Andersson, G Averill, BA
Citation: Eg. Funhoff et al., Mutational analysis of the interaction between active site residues and the loop region in mammalian purple acid phosphatases, BIOCHEM, 40(38), 2001, pp. 11614-11622
History of catalysis
Authors: van Santen, RA van Leeuwen, PWNM Moulijn, JA Averill, BA
Citation: Ra. Van Santen et al., History of catalysis, ST SURF SCI, 123, 1999, pp. 3-28
Bonding and elementary steps in catalysis
Authors: Averill, BA Rietjens, IMCM van Leeuwen, PWNM van Santen, RA
Citation: Ba. Averill et al., Bonding and elementary steps in catalysis, ST SURF SCI, 123, 1999, pp. 109-208
Biocatalysis
Authors: Averill, BA Laane, NWM Straathof, AJJ Tramper, J
Citation: Ba. Averill et al., Biocatalysis, ST SURF SCI, 123, 1999, pp. 343-371
The first binuclear Mo-S cluster compound containing citrate ligands, K-5(NH4)[Mo2O2(mu-S)(2)(C6H4O7)(2)]center dot CH3OH center dot 5H(2)O, characterized by X-ray single crystal structure determination
Authors: Xu, JQ Zhou, XH Zhou, LM Wang, TG Huang, XY Averill, BA
Citation: Jq. Xu et al., The first binuclear Mo-S cluster compound containing citrate ligands, K-5(NH4)[Mo2O2(mu-S)(2)(C6H4O7)(2)]center dot CH3OH center dot 5H(2)O, characterized by X-ray single crystal structure determination, INORG CHIM, 285(1), 1999, pp. 152-154
Evidence for nonbridged coordination of p-nitrophenyl phosphate to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase duringenzymatic turnover
Authors: Merkx, M Pinkse, MWH Averill, BA
Citation: M. Merkx et al., Evidence for nonbridged coordination of p-nitrophenyl phosphate to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase duringenzymatic turnover, BIOCHEM, 38(31), 1999, pp. 9914-9925
Fluoride inhibition of bovine spleen purple acid phosphatase: Characterization of a ternary enzyme-phosphate-fluoride complex as a model for the active enzyme-substrate-hydroxide complex
Authors: Pinkse, MWH Merkx, M Averill, BA
Citation: Mwh. Pinkse et al., Fluoride inhibition of bovine spleen purple acid phosphatase: Characterization of a ternary enzyme-phosphate-fluoride complex as a model for the active enzyme-substrate-hydroxide complex, BIOCHEM, 38(31), 1999, pp. 9926-9936
Probing the role of the trivalent metal in phosphate ester hydrolysis: Preparation and characterization of purple acid phosphatases containing (AlZnII)-Zn-III and (InZnII)-Zn-III active sites, including the first example of an active aluminum enzyme
Authors: Merkx, M Averill, BA
Citation: M. Merkx et Ba. Averill, Probing the role of the trivalent metal in phosphate ester hydrolysis: Preparation and characterization of purple acid phosphatases containing (AlZnII)-Zn-III and (InZnII)-Zn-III active sites, including the first example of an active aluminum enzyme, J AM CHEM S, 121(28), 1999, pp. 6683-6689
Nitric oxide binding to the ferri- and ferroheme states of nitrophorin 1, a reversible NO-binding heme protein from the saliva of the blood-sucking insect, Rhodnius prolixus
Authors: Ding, XD Weichsel, A Andersen, JF Shokhireva, TK Balfour, C Pierik, AJ Averill, BA Montfort, WR Walker, FA
Citation: Xd. Ding et al., Nitric oxide binding to the ferri- and ferroheme states of nitrophorin 1, a reversible NO-binding heme protein from the saliva of the blood-sucking insect, Rhodnius prolixus, J AM CHEM S, 121(1), 1999, pp. 128-138
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