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Table Table 1. O 2 binding to insect Hbs and sperm whale Mb Ligands O 2 k on ×10 −7 (M −1 s −1) k off (s −1) P 50 (torr) P 50* (torr) HisE7 K a Heme Fe atom HisE7 conformation • a a P 50* = P 50/(1 + K a) (Hankeln et al. • b b From Burmester et al.. • c c From Hankeln et al.. • d d From Dewilde et al..
• e e From Antonini and Brunori. Thummi HbIII 30 218 0.46 — — Penta-coordinate Open gate D. Melanogaster Hb 6.4 1.0 0.12 0.0063 18 Hexa-coordinate — G. Intestinalis Hb1 1.0 2.4 0.15 — — Penta-coordinate Closed gate Sperm whale Mb 1.9 10 0.33 — — Penta-coordinate Closed gate. Figure Figure 2.
• • Overall views of GiHb1 quaternary and tertiary structures. ( A) The C trace of both GiHb1 subunits A (cyan) and B (yellow), building up the observed homodimer. For each subunit the heme group is drawn in red, and the dimerization interface -helices are labeled. Some of the key residues building up salt bridges stabilizing the quaternary association are drawn. ( B) Display of the structural overlay of GiHb1 and DmHb. The two proteins (A subunit for GiHb1, cyan ribbon; DmHb, magenta skeleton, PDB entry code 2BK9) are overlaid based on their C backbones.
The figure shows the location adopted by the two heme groups following overlay of the penta-coordinate GiHb1 on the hexa-coordinate DmHb. The proximal HisF8 and distal HisE7 residues are shown to highlight the different distal site stereochemistry in the two cases (GiHb1 distal site includes the Fe-coordinated O 2 molecule, in orange).
Helices E and F, distal and proximal to the heme, are labeled. Note the subtle structural shifts that allow heme distal and proximal backbone readjustments supporting hexa- versus penta-coordination. Drawn with MOLSCRIPT (Kraulis ). Figure Figure 3. • • Stereo views of the closed and open HisE7 gate conformations in GiHb1 and in CttHbIII. ( A) Details of the heme distal site structure adopted by GiHb1 in its oxygenated form (present report; the O 2 molecule is shown in orange), where the distal HisE7 is in the “closed gate” conformation. ( B) The “open gate” conformation of HisE7, swung out of the heme distal pocket, is shown for CttHbIII deoxygenated form (PDB entry code 1ECD; a water molecule, not bound to the heme Fe atom, at the entrance of the distal pocket is shown in magenta).