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Role of an isoform-specific serine residue in FMN–heme electron transfer in inducible nitric oxide synthase

Content Provider	Springer Nature Link
Author	Li, Wenbing Fan, Weihong Chen, Li Elmore, Bradley O. Piazza, Mike Guillemette, J. Guy Feng, Changjian
Copyright Year	2012
Abstract	In the crystal structure of a calmodulin (CaM)-bound FMN domain of human inducible nitric oxide synthase (NOS), the CaM-binding region together with CaM forms a hinge, and pivots on an R536(NOS)/E47(CaM) pair (Xia et al. J Biol Chem 284:30708–30717, 2009). Notably, isoform-specific human inducible NOS S562 and C563 residues form hydrogen bonds with the R536 residue through their backbone oxygens. In this study, we investigated the roles of the S562 and C563 residues in the NOS FMN–heme interdomain electron transfer (IET), the rates of which can be used to probe the interdomain FMN/heme alignment. Human inducible NOS S562K and C563R mutants of an oxygenase/FMN (oxyFMN) construct were made by introducing charged residues at these sites as found in human neuronal NOS and endothelial NOS isoforms, respectively. The IET rate constant of the S562K mutant is notably decreased by one third, and its flavin fluorescence intensity per micromole per liter is diminished by approximately 24 %. These results suggest that a positive charge at position 562 destabilizes the hydrogen-bond-mediated NOS/CaM alignment, resulting in slower FMN–heme IET in the mutant. On the other hand, the IET rate constant of the C563R mutant is similar to that of the wild-type, indicating that the mutational effect is site-specific. Moreover, the human inducible NOS oxyFMN R536E mutant was constructed to disrupt the bridging CaM/NOS interaction, and its FMN–heme IET rate was decreased by 96 %. These results demonstrated a new role of the isoform-specific serine residue of the key CaM/FMN(NOS) bridging site in regulating the FMN–heme IET (possibly by tuning the alignment of the FMN and heme domains).
Starting Page	675
Ending Page	685
Page Count	11
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	17
Issue Number	5
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-03-10
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Electron transfer Nitric oxide synthase Calmodulin Laser flash photolysis Heme Microbiology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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