JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Iwasaki, M.
Right arrow Articles by Negishi, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Iwasaki, M.
Right arrow Articles by Negishi, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 266, Issue 6, 3380-3382, Feb, 1991

Alteration of high and low spin equilibrium by a single mutation of amino acid 209 in mouse cytochromes P450

M Iwasaki, R Juvonen, R Lindberg and M Negishi
Pharmacogenetics Section, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709.

The identities of the amino acid at position 209 are most critical in determining specific coumarin 7- and steroid 15 alpha-hydroxylase activity in P450coh and P450(15)alpha, respectively. This system, therefore, provides us with an excellent model to study the structural basis for P450 specificity as a monooxygenase. We expressed in Saccharomyces cerevisiae a series of the mutated P450s in which residue 209 was substituted with the various amino acids and characterized the spectral property and hydroxylase activity of these mutated P450s. The positioning of a hydrophobic residue including Phe, Leu, and Val at position 209 resulted in shifting the P450 to the high-spin state, while a charged amino acid such as Lys or Asp produced the low-spin form. Moreover, a P450 with Asn or Gly in this position exhibited spectra indicating a mixture of the high- and low-spin forms. This spin alteration, depending upon the hydrophobicity and size of residue at position 209, indicates that this position is likely to reside close to the sixth axial ligand on the distal surface of the heme in these P450s. This proximity of residue 209 to the ligand may explain the critical role of this residue in determining the hydroxylase specificity and activity of these P450s.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Pharmacol. Exp. Ther.Home page
H.-L. Lin, U. M. Kent, H. Zhang, L. Waskell, and P. F. Hollenberg
The Functional Role of Threonine-205 in the Mechanism-Based Inactivation of P450 2B1 by Two Ethynyl Substrates: The Importance of the F Helix in Catalysis
J. Pharmacol. Exp. Ther., December 1, 2004; 311(3): 855 - 863.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. R. Harlow and J. R. Halpert
Alanine-scanning Mutagenesis of a Putative Substrate Recognition Site in Human Cytochrome P450 3A4. ROLE OF RESIDUES 210AND 211IN FLAVONOID ACTIVATION AND SUBSTRATE SPECIFICITY
J. Biol. Chem., February 28, 1997; 272(9): 5396 - 5402.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
W. Song and A. Brash
Purification of an allene oxide synthase and identification of the enzyme as a cytochrome P-450
Science, August 16, 1991; 253(5021): 781 - 784.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1991 by the American Society for Biochemistry and Molecular Biology.