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

Pub. Date : 2012 Jun

PMID : 22407542






3 Functional Relationships(s)
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1 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. Heme calmodulin 3 Homo sapiens
2 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). Heme calmodulin 3 Homo sapiens
3 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). Heme calmodulin 3 Homo sapiens