Probing the Interaction of Bovine Cytochrome P450scc (CYP11A1) with Adrenodoxin: Evaluating Site-Directed Mutations by Molecular Modeling-Reference-Cited by-同舟云学术

Probing the Interaction of Bovine Cytochrome P450scc (CYP11A1) with Adrenodoxin: Evaluating Site-Directed Mutations by Molecular Modeling

Published:2002-06-05 Issue:26 Volume:41 Page:8310-8320
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Usanov Sergey A.¹,Graham Sandra E.¹,Lepesheva Galina I.¹,Azeva Tamara N.¹,Strushkevich Natalya V.¹,Gilep Andrei A.¹,Estabrook Ronald W.¹,Peterson Julian A.¹

Affiliation:

1. Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 220141, Minsk, Kuprevicha 5/2, Belarus, and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-9038

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0255928

Reference53 articles.

1. Usanov, S. A., Chashchin, V. L., and Akhrem A. A. (1990) inMolecular Mechanisms of Adrenal Steroidogenesis and Aspects of Regulation and Application(Ruckpaul, K., and Rein, H., Eds.) Vol. 3, pp 1−57, Frontiers in Biotransformation, Akademie-Verlàg, Berlin.

2. Cytochrome P-450scc-adrenodoxin complex. Reduction properties of the substrate-associated cytochrome and relation of the reduction states of heme and iron-sulfur centers to association of the proteins.

3. The use of a specific fluorescence probe to study the interaction of adrenodoxin with adrenodoxin reductase and cytochrome P-450scc.

4. Fluorescein Isothiocyanate Specifically Modifies Lysine 338 of Cytochrome P-450scc and Inhibits Adrenodoxin Binding

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