Reid T J, Murthy M R, Sicignano A, Tanaka N, Musick W D, Rossmann M G
Proc Natl Acad Sci U S A. 1981 Aug;78(8):4767-71. doi: 10.1073/pnas.78.8.4767.
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.
在分辨率为2.5埃的电子密度图中，牛肝过氧化氢酶的大多数氨基酸侧链清晰可辨，结果与序列[施罗德，W. A.，谢尔顿，J. R.，谢尔顿，J. B.，罗伯逊，B. & 阿佩尔，G.（1969年）《生物化学与生物物理学报》131卷，653 - 655页]高度一致。一个亚基的三级结构由一个带有螺旋插入的大的反平行β折叠片层结构域组成，随后是一个较小的包含四个α螺旋的结构域。血红素基团深埋在分子表面以下至少20埃处，可通过一条由疏水残基排列而成的通道到达。近端配体是酪氨酸 - 357，而组氨酸 - 74和天冬酰胺 - 147是血红素远端的重要残基。已证明能与组氨酸 - 74共价结合的抑制剂3 - 氨基 - 1,2,4 - 三唑，其N(2)原子与血红素铁配位，可嵌入血红素腔中。
