HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 37, 27006-27011, September 14, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/37/27006    most recent M703790200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kimmich, N. Articles by Poulos, T. L. Search for Related Content PubMed PubMed Citation Articles by Kimmich, N. Articles by Poulos, T. L. Social Bookmarking                      What's this?

Electron Transfer between Cytochrome P450cin and Its FMN-containing Redox Partner, Cindoxin^*

Novelle Kimmich, Aditi Das¹, Irina Sevrioukova, Yergalem Meharenna, Stephen G. Sligar, and Thomas L. Poulos²

From the Departments of Molecular Biology and Biochemistry, Chemistry and Physiology, and Biophysics, University of California, Irvine, California 92612-39003900 and Departments of Biochemistry, Chemistry, the Center for Biophysics and Computational Biology, and the College of Medicine, University of Illinois, Urbana, Illinois 61801

Cytochrome P450 reductase, which delivers electrons from NADPH to microsomal P450s, consists of a single polypeptide that contains both FAD and FMN. The bacterial P450cin utilizes a similar electron transport system except the FAD/FMN reductase consists of two separate polypeptides where the FMN protein, cindoxin, shuttles electrons between the FAD-containing cindoxin reductase and P450cin. Here we characterize the kinetics and specificity of electron transfer between cindoxin and P450cin as well as discuss the influence of possible binding surface interactions using homology models.

Received for publication, May 8, 2007 , and in revised form, July 2, 2007.

^* This work was supported in part by National Institutes of Health Grants GM33688 (to T. L. P.), GM067637 (to I. S.), and GM31756 (to S. G. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by National Science Foundation Grant EEC-0118025.

² To whom correspondence should be addressed. Tel.: 949-824-7020; Fax: 949-824-3280; E-mail: poulos{at}uci.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E.-J. Kim, J.-S. Kim, I.-H. Lee, H. J. Rhee, and J. K. Lee Superoxide Generation by Chlorophyllide a Reductase of Rhodobacter sphaeroides J. Biol. Chem., February 15, 2008; 283(7): 3718 - 3730. [Abstract] [Full Text] [PDF]