Aluminum-substituted heme domain of P450BM-3 (BMP): Introducing a heme-derived fluorescent probe for studies of substrate binding and protein-protein interactions in cytochromes P450-Reference-Cited by-同舟云学术

Aluminum-substituted heme domain of P450BM-3 (BMP): Introducing a heme-derived fluorescent probe for studies of substrate binding and protein-protein interactions in cytochromes P450

Published:2013-01 Issue:1 Volume:60 Page:41-51
ISSN:0885-4513
Container-title:Biotechnology and Applied Biochemistry
language:en
Short-container-title:Biotechnology and Applied Biochemistry

Author:

Davydov Dmitri R.,Ponomarev Gelii V.¹,Bobrovnikova-Marjon Ekaterina¹,Haines Donovan C.²,Peterson Julian A.²

Affiliation:

1. Institute of Biomedical Chemistry, Russian Academy of Medical Science; Moscow; Russia

2. Department of Biochemistry; The University of Texas Southwestern Medical Center at Dallas; Dallas; TX; USA

Publisher

Wiley

Subject

Process Chemistry and Technology,Drug Discovery,Applied Microbiology and Biotechnology,Biomedical Engineering,Molecular Medicine,General Medicine,Bioengineering,Biotechnology

Reference61 articles.

1. P450BM-3 and other Inducible Bacterial P450 Cytochromes: Biochemistry and Regulation

2. Crystallization and preliminary x-ray diffraction analysis of P450terp and the hemoprotein domain of P450BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily.

3. Reconstitution of the Fatty Acid Hydroxylase Activity of Cytochrome P450BM-3 Utilizing Its Functional Domains

4. 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.

5. Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's

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