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Literature summary for 1.14.13.39 extracted from

  • Li, W.; Chen, L.; Fan, W.; Feng, C.
    Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins (2012), FEBS Lett., 586, 159-162.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Cofactor

Cofactor Comment Organism Structure
FMN determination of FMN-heme intraprotein electron transfer kinetics in full length and oxygenase/FMN construct of human inducible nitric oxide synthase. The rate constant increases considerably with temperature. The FMN domain in the holoenzyme needs to sample more conformations before the intraprotein electron transfer takes place, and the FMN domain in the oxyFMN construct is better poised for efficient intraprotein electron transfer Homo sapiens