Thomas M. Loehr

TL;DR: The first definitive evidence for a bridging, symmetrical peroxo adduct is presented from vibrational spectroscopic studies of the freeze-trapped intermediate of this mutant R2.

TL;DR: To characterize this transient intermediate and establish unambiguously the peroxodiferric assignment, rapid freeze-quenching was used to trap the initial intermediate for resonance Raman investigation, andrete vibrational modes are observed for this intermediate, indicating a single chromophore in a homogeneous state, in agreement with the Mössbauer conclusions.

TL;DR: Conversion of heme to verdoheme by heme oxygenase-1 (HO-1) is thought to involve α-meso-hydroxylation and elimination of the meso-carbon as CO, a reaction supported by both H2O2 and NADPH-cytochrome P450 reductase/O2.

TL;DR: Although the H25A mutant protein shows no heme oxygenase activity, the heme is competent to bind carbon monoxide, and this ferrous heme-H25A HO complex exists as an equilibrium mixture between a five-coordinate, high-spin species and a four-coordinated, intermediate- spin species.

TL;DR: The Raman spectrum of the B2 subunit of Escherichia coli ribonucleotide reductase shows a peak at 496 cm-1 that appears to be in resonance with the 370-nm electronic transition of the binuclear iron center in both the native and radical-free forms of the protein.