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• W2113342234 abstract "The FMN-heme intraprotein electron transfer (IET) kinetics in a human inducible NOS (iNOS) oxygenase/FMN (oxyFMN) construct co-expressed with NCaM, a truncated calmodulin (CaM) construct that includes only its N-terminal globular domain consisting of residues 1–75, were determined by laser flash photolysis. The IET rate constant is significantly decreased by nearly fourfold (compared to the iNOS oxyFMN co-expressed with full length CaM). This supports an important role of full length CaM in proper interdomain FMN/heme alignment in iNOS. The IET process was not observed with added excess EDTA, suggesting that Ca2+ depletion results in the FMN domain moving away from the heme domain. The results indicate that a Ca2+-dependent reorganization of the truncated CaM construct could cause a major modification of the NCaM/iNOS association resulting in a loss of the IET." @default.
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• W2113342234 date "2010-09-22" @default.
• W2113342234 modified "2023-10-15" @default.
• W2113342234 title "Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin" @default.
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• W2113342234 doi "https://doi.org/10.1016/j.febslet.2010.09.028" @default.
• W2113342234 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2956772" @default.
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