Cover Image, Volume 38, Issue 17

The figure depicts the dominant electron transfer pathways between the two tryptophan residues and the heme in the protein myoglobin. Nicholas A. Besley and colleagues' calculations find the relaxation times for electron transfer to be 42 ps and 12000 ps for the two tryptophan residues in agreement with experimental measurements of 34 ps and 40000 ps. The electron transfer rates are dictated by the distance between the heme and tryptophan residues, while the orientation of the tryptophan residues relative to the heme is important for excitation energy transfer. (DOI: 10.1002/jcc.24793 )