Crystalline bovine liver catalase

Eventoff, William; Tanaka, Nobuo; Rossmann, Michael G.

doi:10.1016/0022-2836(76)90210-2

Cited by 28 publications

(11 citation statements)

References 12 publications

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“…This information was used in a vector search (44) procedure to locate two major heavy atom sites, A and B, and the molecular center (0,SY,5/6). The latter was determined to be at Sy = 0.65 and is therefore within the limits of0.56 < Sy -0.72 estimated by Eventoffet al (37). The presence oftwo major heavy atom sites, susceptible to mercurial substitution, is consistent with two highly reactive sulfhydryl groups per subunit in beef liver catalase (45).…”

Section: Methodsmentioning

confidence: 56%

“…However, approximately two of the four heme groups are degraded to a high-spin Fe(III)-biliverdin complex (20,21 Catalase was one of the first enzymes to be crystallized (20). Electron microscopy (23,24), electron diffraction (25)(26)(27), and low angle x-ray scattering (28) all show a slightly ellipsoidal molecule with an average radius of 40 A. Single-crystal forms of catalase reported to date (29)(30)(31)(32)(33)(34)(35)(36)(37) contain one or more molecules per asymmetric unit except for bacterial catalase (35), the catalase ofPenicillium vitale (36), and a trigonal form ofbeefliver catalase (37), all ofwhich incorporate one crystallographic 2-fold axis in the molecule. We describe here the preliminary results of a high-resolution structure determination of the beef liver catalase crystals reported by Eventoff et al (37).…”

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confidence: 99%

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

Reid¹,

Murthy²,

Sicignano³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

194

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Catalase (hydrogen peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) occurs in almost all aerobically respiring organisms and in part serves to protect cells from the toxic effects of hydrogen peroxide. The subcellular location of liver catalase is restricted to the peroxisomes, and the enzyme is probably incorporated into these organelles during their biogenesis (1). The properties of catalase have been reviewed by numerous authors including Deisseroth and Dounce (2) and Schonbaum and Chance (3). The overall reaction catalyzed by the enzyme can be written as ROOH + HQOH = QO + ROH + H20, [1] where R is H or an alkyl or acyl group and HQOH is a twoelectron donor in which Q is 0, C=O, or H(CH2)nCH (n = 1, 2, or 3). This reaction proceeds by two steps: (i) oxidation ofthe enzyme (E) by a peroxide E-H20 + ROOH = E-O + ROH + H20, [2] apocatalase I and (ii) oxidation of the substrate E-O + HQOH = E-H20 + QO.

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Section: Methodsmentioning

confidence: 56%

mentioning

confidence: 99%

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

Reid¹,

Murthy²,

Sicignano³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

194

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“…Each subunit has usually 506 amino acids, although some beef liver extracts have been reported with 10 to 15 additional residues (Schroeder, Shelton, Shelton, Robberson, Apell, Fang & Bonaventura, 1982;Schroeder, Shelton, Shelton, Apell, Evans, Bonaventura & Fang, 1982). The crystals are trigonal, have space group P3221 with a = 142.0 and c = 103.7 A and were first reported by Eventoff, Tanaka & Rossmann (1976). The molecule is positioned on a crystallographic diad with two subunits per crystallographic asymmetric unit.…”

Section: Refinement Of the Structure ( A ) Crystal And Molecular Datamentioning

confidence: 97%

The refined structure of beef liver catalase at 2·5 Å resolution

Fita¹,

Silva²,

Murthy³

et al. 1986

Acta Crystallogr Sect B

107

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“…Additionally, the unit-cell parameters of very thin plates of a second P2 1 2 1 2 1 form were determined to be a = 69, b = 173.5, c = 206 Å through both EM and X-ray powder diffraction (Unwin, 1975). Finally, in 1976, a second distinct P3 1 21 or P3 2 21 trigonal form was discovered by Rossmann and Eventoff, with unit-cell parameters a = b = 142.3 (6), c = 104.0 (5) Å (Eventoff et al, 1976).…”

Section: Introductionmentioning

confidence: 97%

Sixty years from discovery to solution: crystal structure of bovine liver catalase form III

Foroughi

Kang

Matzger

2011

Acta Crystallogr D Biol Cryst

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The crystallization and structural characterization of bovine liver catalase (BLC) has been intensively studied for decades. Forms I and II of BLC have previously been fully characterized using single-crystal X-ray diffraction. Form III has previously been analyzed by electron microscopy, but owing to the thinness of this crystal form an X-ray crystal structure had not been determined. Here, the crystal structure of form III of BLC is presented in space group P2(1)2(1)2(1), with unit-cell parameters a = 68.7, b = 173.7, c = 186.3 Å. The asymmetric unit is composed of the biological tetramer, which is packed in a tetrahedron motif with three other BLC tetramers. This higher resolution structure has allowed an assessment of the previously published electron-microscopy studies.

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Crystalline bovine liver catalase

Cited by 28 publications

References 12 publications

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

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

The refined structure of beef liver catalase at 2·5 Å resolution

Sixty years from discovery to solution: crystal structure of bovine liver catalase form III

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