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. 1981 Aug;78(8):4767–4771. doi: 10.1073/pnas.78.8.4767

Structure and heme environment of beef liver catalase at 2.5 A resolution.

T J Reid 3rd, M R Murthy, A Sicignano, N Tanaka, W D Musick, M G Rossmann
PMCID: PMC320244  PMID: 6946424

Abstract

Most of the amino acid side chains of beef liver catalase were clearly identifiable in the 2.5 A 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 beta-pleated sheet domain with helical insertions, followed by a smaller domain containing four alpha-helices. The heme group is buried at least 20 A 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.

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Selected References

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