Synthetic and Physical Approaches to Metalloproteins - Bruce Averill

Abstract

Funding Agency

Agency: National Institute of Health (NIH)
Institute: National Institute of General Medical Sciences (NIGMS)
Type: Research Project (R01)
Project #: 3R01GM032117-09S1
Application #: 3280727
Study Section: Metallobiochemistry Study Section (BMT)

Project Start: 1983-01-01
Project End: 1993-04-30
Budget Start: 1991-06-22
Budget End: 1993-04-30
Support Year: 9
Fiscal Year: 1991
Total Cost
Indirect Cost

Institution

Name: University of Virginia
Department
Type: Schools of Arts and Sciences
DUNS #: 001910777

City: Charlottesville
State: VA
Country: United States
Zip Code: 22904

Related projects


NIH 1994 R01 GM	Iron-Containing Phosphatases - Structure and Mechanism Averill, Bruce A. / University of Virginia
NIH 1993 R01 GM	Iron-Containing Phosphatases - Structure and Mechanism Averill, Bruce A. / University of Virginia
NIH 1991 R01 GM	Synthetic and Physical Approaches to Metalloproteins Averill, Bruce A. / University of Virginia
NIH 1991 R01 GM	Synthetic and Physical Approaches to Metalloproteins Averill, Bruce A. / University of Virginia
NIH 1990 R01 GM	Synthetic and Physical Approaches to Metalloproteins Averill, Bruce A. / University of Virginia
NIH 1989 R01 GM	Synthetic and Physical Approaches to Metalloproteins Averill, Bruce A. / University of Virginia
NIH 1988 R01 GM	Synthetic and Physical Approaches to Metalloproteins Averill, Bruce A. / University of Virginia
NIH 1987 R01 GM	Synthetic and Physical Approaches to Metalloproteins Averill, Bruce A. / University of Virginia
NIH 1986 R01 GM	Synthetic and Physical Approaches to Metallproteins Averill, Bruce A. / University of Virginia
NIH 1985 R01 GM	Synthetic and Physical Approaches to Metallproteins Averill, Bruce A. / University of Virginia

Publications

Orlando, J L; Zirino, T; Quirk, B J et al. (1993) Purification and properties of the native form of the purple acid phosphatase from bovine spleen. Biochemistry 32:8120-9

Averill, B A; Vincent, J B (1993) Electronic absorption spectroscopy of nonheme iron proteins. Methods Enzymol 226:33-51

Wang, Z; Ming, L J; Que Jr, L et al. (1992) 1H NMR and NOE studies of the purple acid phosphatases from porcine uterus and bovine spleen. Biochemistry 31:5263-8

Vincent, J B; Crowder, M W; Averill, B A (1992) Multiple binding sites for tetrahedral oxyanion inhibitors of bovine spleen purple acid phosphatase. Biochemistry 31:3033-7

Vincent, J B; Crowder, M W; Averill, B A (1992) Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. Trends Biochem Sci 17:105-10

Crowder, M W; Vincent, J B; Averill, B A (1992) Electron paramagnetic resonance studies on the high-salt form of bovine spleen purple acid phosphatase. Biochemistry 31:9603-8

Vincent, J B; Crowder, M W; Averill, B A (1991) Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen. J Biol Chem 266:17737-40

Vincent, J B; Crowder, M W; Averill, B A (1991) Spectroscopic and kinetics studies of a high-salt-stabilized form of the purple acid phosphatase from bovine spleen. Biochemistry 30:3025-34

Vincent, J B; Averill, B A (1990) An enzyme with a double identity: purple acid phosphatase and tartrate-resistant acid phosphatase. FASEB J 4:3009-14

Vincent, J B; Averill, B A (1990) Sequence homology between purple acid phosphatases and phosphoprotein phosphatases. Are phosphoprotein phosphatases metalloproteins containing oxide-bridged dinuclear metal centers? FEBS Lett 263:265-8

Showing the most recent 10 out of 14 publications

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