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Title 

Surface display of heme- and diflavin-containing cytochrome P450 BM3 in Escherichia coli: a whole cell biocatalyst for oxidation

Authors 

S K YimD H KimHeung Chae JungJae Gu PanH S KangT AhnC H Yun

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2010

Citation 

Journal of Microbiology and Biotechnology, vol. 20, no. 4, pp. 712-717

Keywords 

OxidationP450 BM3Surface displayWhole-cell biocatalyst

Abstract 

Cytochrome P450 enzymes (P450s) are involved in the synthesis of a wide variety of valuable products and in the degradation of numerous toxic compounds. The P450 BM3 (CYP102A1) from Bacillus megaterium was the first P450 discovered to be fused to its redox partner, a mammalian-like diflavin reductase. Here, we report the development of a whole-cell biocatalyst using ice-nucleation protein (Inp) from Pseudomonas syringae to display a heme- and diflavin-containing oxidoreductase, P450 BM3 (a single, 119-kDa polypeptide with domains of both an oxygenase and a reductase) on the surface of Escherichia coli. The surface localization and functionality of the fusion protein containing P450 BM3 were verified by flow cytometry and measurement of enzymatic activities. The results of this study comprise the first report of microbial cell-surface display of a heme- and diflavin-containing enzyme. This system should allow us to select and develop oxidoreductases containing heme and/or flavins into practically useful whole-cell biocatalysts for extensive biotechnological applications, including selective synthesis of new chemicals and pharmaceuticals, bioconversion, bioremediation, live vaccine development, and biochip development.

ISSN 

1017-7825

Link 

http://dx.doi.org/10.4014/jmb.0910.10043

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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