Crystal Structure of Inhibitor-Bound P450BM-3 Reveals Open Conformation of Substrate Access Channel,-Reference-Cited by-同舟云学术

Crystal Structure of Inhibitor-Bound P450BM-3 Reveals Open Conformation of Substrate Access Channel,

Published:2008-02-26 Issue:12 Volume:47 Page:3662-3670
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Haines Donovan C.¹,Chen Baozhi¹,Tomchick Diana R.¹,Bondlela Muralidhar¹,Hegde Amita¹,Machius Mischa¹,Peterson Julian A.¹

Affiliation:

1. Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9038, and Department of Chemistry, The University of Texas at Dallas, Dallas, Texas 75083-0688

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi7023964

Reference54 articles.

1. The Repressor Protein, Bm3R1, Mediates an Adaptive Response to Toxic Fatty Acids in Bacillus megaterium

2. Partial characterization of a barbiturate-induced cytochrome P-450-dependent fatty acid monooxygenase from Bacillusmegaterium

3. Cloning of the gene encoding a catalytically self-sufficient cytochrome P-450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts.

4. Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium.

5. Identification and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium.

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