期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：8
页码：4767-4771
DOI：10.1073/pnas.78.8.4767
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
