Markus Voehler

TL;DR: Fourier-transform ion cyclotron resonance mass spectrometry and nuclear magnetic resonance spectroscopy are used to show that a sulfilimine bond (-S=N-) crosslinks hydroxylysine-211 and methionine-93 of adjoining protomers, a bond not previously found in biomolecules.

TL;DR: Following cloning, expression, and purification of this cytochrome P450, it is shown that it can produce dimer and trimer products from the substrate flaviolin and that the structures of two of the dimeric products were established using mass spectrometry and multiple NMR methods.

TL;DR: It is demonstrated that changing the sample diameter has a pronounced effect on the sample resistance and this results in dramatic improvements of the signal-to-noise ratio and shorter pi/2 pulses.

TL;DR: The findings suggest that CYP158A2 utilizes substrate hydroxyl groups to stabilize active site water and further assist in the iron-linked dioxygen activation and two classes of P450s based on the pathway of proton transfer, one using the highly conserved threonine in the I-helix and the other requiring hydroxym groups of the substrate molecules either directly transferring protons or stabilizing a water pathway for protonTransfer.

TL;DR: Three modified Dickerson–Drew dodecamer sequences, amenable to crystallographic and spectroscopic analyses and containing the 5′-CG-3′ sequence associated with genomic cytosine methylation, were compared and lesion-specific differences observed in the DDD may be implicated in recognition of 5hmC, 5fC, or 5caC in DNA by TDG.