Key result
Ferrous-NO adducts of Trp-409Tyr/Phe nNOS mutants exhibit spectra distinct from wild-type, indicating cleavage of the Fe-S bond and a predominantly five-coordinate state.
The conserved tryptophan-409 in neuronal nitric oxide synthase plays a significant role in stabilizing the Fe-S bond, as its mutation leads to Fe-S bond cleavage in the ferrous-NO state.
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Trp40 mutation disrupts NOS NO complex regulation; extends mechanistic insights but leaves open any cardiovascular therapeutic relevance.
Voegtle et al. (2003) studied this question. Trp-409Tyr/Phe mutation of neuronal nitric oxide synthase (nNOS) vs. Wild-type nNOS was evaluated on Spectroscopic characteristics (UV-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopy). Ferrous-NO adducts of Trp-409Tyr/Phe nNOS mutants exhibit spectra distinct from wild-type, indicating cleavage of the Fe-S bond and a predominantly five-coordinate state.
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