Bruce A. Averill, Ph.D.

Affiliations: 
Chemistry University of Virginia, Charlottesville, VA 
Website:
http://sites.nationalacademies.org/PGA/Jefferson/ssLINK/PGA_046475
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""Bruce A. Averill""
Bio:

http://www2.chemistry.msu.edu/Genealogy/PID605.shtml

Mean distance: 7.09
 
SNBCP

Parents

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Richard Hadley Holm grad student 1969-1973 MIT
 (Synthetic analogues of the active sites of non-heme iron-sulfur proteins)
Robert Heinz Abeles post-doc Brandeis
William H. Orme-Johnson post-doc 1976 UW Madison

Children

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Julie A. Kovacs research assistant 1981 Michigan State
Susan Kauzlarich grad student 1980-1985 Michigan State
Michael W. Crowder grad student 1993 UVA
Teng-Ming Chen post-doc 1986-1988 UVA
Susan Latturner research scientist 1993 UVA
BETA: Related publications

Publications

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Funhoff EG, de Jongh TE, Averill BA. (2005) Direct observation of multiple protonation states in recombinant human purple acid phosphatase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 550-63
Sträter N, Jasper B, Scholte M, et al. (2005) Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop. Journal of Molecular Biology. 351: 233-46
Funhoff EG, Wang Y, Andersson G, et al. (2005) Substrate positioning by His92 is important in catalysis by purple acid phosphatase. The Febs Journal. 272: 2968-77
Funhoff EG, Bollen M, Averill BA. (2005) The Fe(III)Zn(II) form of recombinant human purple acid phosphatase is not activated by proteolysis. Journal of Inorganic Biochemistry. 99: 521-9
Averill BA. (2004) Dinuclear Hydrolases Comprehensive Coordination Chemistry Ii. 8: 641-676
Dikiy A, Funhoff EG, Averill BA, et al. (2002) New insights into the mechanism of purple acid phosphatase through (1)H NMR spectroscopy of the recombinant human enzyme. Journal of the American Chemical Society. 124: 13974-5
Funhoff EG, Klaassen CH, Samyn B, et al. (2001) The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity. Chembiochem : a European Journal of Chemical Biology. 2: 355-63
Funhoff EG, Ljusberg J, Wang Y, et al. (2001) Mutational analysis of the interaction between active site residues and the loop region in mammalian purple acid phosphatases. Biochemistry. 40: 11614-22
Pinkse MW, Merkx M, Averill BA. (1999) 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. Biochemistry. 38: 9926-36
Merkx M, Pinkse MW, Averill BA. (1999) Evidence for nonbridged coordination of p-nitrophenyl phosphate to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase during enzymatic turnover. Biochemistry. 38: 9914-25
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