Structure and heme environment of beef liver catalase at 2.5 Å resolution

Abstract

Most of the amino acid side chains of beef liver catalase were clearly identifiable in the 2.5 Å resolution electron-density map, and the results are in good agreement with the sequence [Schroeder, W. A., Shelton, J. R., Shelton, J. B., Roberson, B. & Apell, G. (1969) Arch. Biochem. Biophys. 131, 653-655]. The tertiary structure of one subunit consists of a large antiparallel β -pleated sheet domain with helical insertions, followed by a smaller domain containing four α -helices. The heme group is buried at least 20 Å below the molecular surface and is accessible by a channel lined with hydrophobic residues. The proximal ligand is tyrosine-357, while histidine-74 and asparagine-147 re the important residues on the distal side of the heme. The inhibitor 3-amino-1,2,4-triazole, which has been shown to covalently bond to histidine-74, can be built into the heme cavity with its N(2) atom coordinated to the heme iron.