Jyllian N. Kemsley

TL;DR: A detailed molecular mechanism has been proposed for IPNS based on spectroscopic and crystallographic studies and the role of cosubstrate ascorbate is proposed to reduce the toxic peroxo byproduct to water.

TL;DR: Experimental and theoretical evidence is provided and an attractive mechanism for the role of ABLM in double-strand cleavage is proposed, which would generate a reactive Fe(IV)=O species, capable of a second DNA strand cleavage, as observed in vivo.

TL;DR: Excited-state ligand field CD and MCD data indicate that the six-coordinate ferrous active site of the resting and N-ethylmaleimide-activated enzyme is not perturbed by the addition of pterin cofactor in the absence of substrate.

TL;DR: Analysis of the products produced by the mutant enzymes shows that although both oxidize pterin at more than twice the rate of wild-type enzyme, these reactions are only approximately 20% coupled to production of L-Tyr, indicating that the first step of the PAH reaction and disease mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site.

TL;DR: In this paper, the authors used X-ray absorption spectroscopy to study the interaction of the biologically relevant FeIIBLM complex with DNA and found that DNA binding significantly perturbs the FeII active site, resulting in a change in intensity ratio of the d d transitions and a decrease in excited-state orbital splitting.