Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins

Article ID	Journal	Published Year	Pages	File Type
10871547	FEBS Letters	2012	4 Pages	PDF

Abstract

âº The FMN-heme IET kinetics in full length and truncated oxygenase/FMN construct iNOS proteins were determined at 283-304Â K. âº This is the first study of temperature dependence of the NOS IET kinetics. âº Eyring equation was used to analyze the temperature dependence data. âº The magnitude of activation entropy for the IET in the oxygenase/FMN construct is only one-fifth of that for the holoenzyme. âº The results indicate that the FMN domain in the holoenzyme needs to sample more conformations before the IET takes place.

Keywords

iNOS 5-deazariboflavin IET (6R)-5,6,7,8-Tetrahydrobiopterin Intraprotein electron transfer H4B KET nNOS eNOS NOS DRF flavin adenine dinucleotide neuronal NOS inducible NOS electron transfer endothelial NOS FAD CAM Laser flash photolysis Nitric oxide nitric oxide synthase Temperature dependence Calmodulin