Bruce A. Averill

Learn More
Polyclonal antibodies were used to identify heme or copper nitrite reductases in the following groups: 23 taxonomically diverse denitrifiers from culture collections, 100 numerically dominant denitrifiers from geographically diverse environments, and 51 denitrifiers from a culture collection not selected for denitrification. Antisera were raised against(More)
Formation of phosphate esters by kinases has long been recognized as an important process in biochemistry, but the reverse reaction, hydrolysis of phosphate esters by phosphatases, has attracted less attention. Recent work suggests that phosphatases are as important as kinases in regulatory processes, and that they constitute a diverse group of enzymes that(More)
A copper-containing nitrite reductase gene (nirU) from Pseudomonas sp. strain G-179 was found in a 1.9-kb EcoRI-BamHI DNA fragment. The coding region contained information for a polypeptide of 379 amino acids. The encoded protein had 78% identity in amino acid sequence to the nitrite reductase purified from Achromobacter cycloclastes. The ligands for type 1(More)
A new purification scheme has been developed for the purple acid phosphatase from beef spleen; typical yields are 8 mg of homogeneous enzyme per kg of spleen in only five steps. Kinetics studies have shown that the enzyme is strongly inhibited by fluoride, phosphate, and [p-(acetylamino)-benzyl]phosphonate, a nonhydrolyzable substrate analogue; the last two(More)
The tartrate-resistant acid phosphatases or purple acid phosphatases constitute a class of related mammalian enzymes. Spectroscopic and magnetic studies have revealed that the purple phosphatases contain a novel dinuclear iron active site that is responsible for the purple color. More biologically and biomedically oriented research has shown that the(More)
Mammalian purple acid phosphatases (PAPs) can be divided into two groups, which exhibit distinct spectroscopic and kinetics properties: PAPs that consist of a single 36 kDa polypeptide, and PAPs that have undergone limited proteolysis to give two fragments with masses of 16 and 20 kDa, respectively. Proteolysis results in an increase in enzymatic activity,(More)
A spectrophotometric assay for dissimilatory nitrite reductases has been developed utilizing mammalian cytochrome c (equine heart) as reductant and spectrophotometric agent. The copper-containing nitrite reductase from Achromobacter cycloclastes has been shown to have apparent Km's for reduced cytochrome c and nitrite of 86 +/- 5 and 5.63 +/- 0.03 microM,(More)
Reduction of NO2- by the Cu-containing nitrite reductase from Achromobacter cycloclastes produces NO as the primary product initially, but as NO accumulates, NO production levels-off and N2O production becomes significant. Reaction of the enzyme with NO2- in the presence of NO increases the amount of N2O product significantly, while trapping the NO product(More)
The purple acid phosphatase (PAP) from bovine spleen has been shown to exist as a single ca. 36-kDa polypeptide in intact spleen tissue. The previously isolated microheterogeneous complex of 15-kDa and 23- or 21-kDa subunits appears to arise from proteolytic cleavage of an exposed, highly variable loop in the polypeptide chain. Small amounts of a single(More)