Joann Sanders Loehr

  • Citations Per Year
Learn More
The amino acid sequence of hemerythrin from the sipunculid worm, Themiste dyscritum, was determined by sequenator analyses of the S-pyridylethylated protein and fragments derived by further chemical and enzymatic cleavages. The fragments were obtained by cleavage of the intact protein with hydroxylamine, trypsin digestion of citraconylated intact protein,(More)
Resonance Raman, optical absorption, circular dichroic, and fluorescence emission spectroscopy of hemerythrins from four species of sipunculids (Phascolopsis gouldii, Phascolosoma agassizii, Themiste dyscritium, and Themiste pyroides) reveals no major differences in their active site or tertiary structures. This precludes any change in iron ligands or(More)
 Ribonucleotide reductase protein R2 contains a diiron-oxo center with the ability to generate and stabilize a catalytically essential tyrosyl radical. The six protein-derived ligands (four carboxylates and two histidines) of the diiron site were, in separate experiments, mutated to alanines and in two cases also to histidines. We found that removal or(More)