Oxygen-dependent coproporphyrinogen-III oxidase fromEscherichia coli: one-step purification and biochemical characterisation

Macieira, Sofia, Martins, Berta M. and Huber, Robert 2003. Oxygen-dependent coproporphyrinogen-III oxidase fromEscherichia coli: one-step purification and biochemical characterisation. FEMS Microbiology Letters 226 (1) , pp. 31-37. 10.1016/S0378-1097(03)00531-7

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Abstract

Coproporphyrinogen-III oxidase (CPO) catalyses the conversion of coproporphyrinogen-III to protoporphyrinogen-IX in the haem biosynthetic pathway, and its deficient activity is associated with human hereditary coproporphyria. The 47% sequence identity between the oxygen-dependent CPO from Escherichia coli and its human counterpart makes the bacterial enzyme a good model system for structural studies of this disease. Therefore, we overexpressed and purified to homogeneity the oxygen-dependent CPO from E. coli and its selenomethionine derivative fused with a His6-tag. Both preparations showed a specific activity of 37 500 U mg−1, had a subunit molecular mass of 35 kDa and behaved as a compact shaped dimer. First crystallisation trials produced plate-shaped diffracting crystals.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	Wiley-Blackwell
ISSN:	0378-1097
Last Modified:	24 Jun 2017 11:00
URI:	https://orca.cardiff.ac.uk/id/eprint/70179

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