Crystallization Of The Terminal Oxygenase Component Of Biphenyl Dioxygenase Derived From Rhodococcus Sp. Strain Rha1

Title: Crystallization Of The Terminal Oxygenase Component Of Biphenyl Dioxygenase Derived From Rhodococcus Sp. Strain Rha1

Volume: 10 Issue: 4

Author(s): Venugopalan Nagarajan, Nobuyuki Sakurai, Miho Kubota, Takamasa Nonaka, Hiroaki Nagumo, Hisashi Takeda, Tomoko Nishizaki, Eiji Masai, Masao Fukuda and the late Yukio Mitsui

Affiliation:

Keywords: biphenyl dioxygenase, polychlorinated biphenyl, rieske iron-sulfur center, non-heme iron

Abstract: The terminal oxygenase component of the biphenyl dioxygenase (BphA1A2 complex) was over-expressed with a novel over expression system in recombinant Rhodococcus strain and purified. The purified enzyme has been crystallized by the hanging drop vapor diffusion method and subjected to X-ray diffraction analysis. The crystals belong to the tetragonal system in the space group P4 1 2 1 2 or P4 3 2 1 2 and diffract to better than 2.2Å resolution.

Cite this article as:

Nagarajan Venugopalan, Sakurai Nobuyuki, Kubota Miho, Nonaka Takamasa, Nagumo Hiroaki, Takeda Hisashi, Nishizaki Tomoko, Masai Eiji, Fukuda Masao and Mitsui the late Yukio, Crystallization Of The Terminal Oxygenase Component Of Biphenyl Dioxygenase Derived From Rhodococcus Sp. Strain Rha1, Protein & Peptide Letters 2003; 10 (4) . https://dx.doi.org/10.2174/0929866033478889