Matsuda et al., Biochim Biophys Acta 1999
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The reduction of the oxidized enzyme ( FAD-FMN ) by NADPH proceeds by both one-electron equivalent and two-electron equivalent mechanisms, and the formation of semiquinone ( increase of absorbance at 590 nm ) was significantly increased in the presence of Ca ( 2+ ) /CaM Daff et al., Biochem Soc Trans 2001
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In order to resolve the mechanism of action of CaM activation we determined reduction potentials for the FMN and FAD cofactors of rat nNOS in the presence and absence of CaM using a recombinant form of the reductase domain
Nishino et al., Arch Biochem Biophys 2007
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In the presence or absence of calcium/calmodulin ( Ca ( 2+ ) /CaM ), reduction of the oxidized flavins ( FAD-FMN ) and air-stable semiquinone ( FAD-FMNH ( * ) ) with NADPH occurred in at least two phases in the absorbance change at 457nm
Narayanasami et al., Nitric Oxide 1997
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FMN release from nNOS, but not from the flavoprotein module, was enhanced by CaM