Sulfide-Binding Hemoglobins: Effects of Mutations on Active-Site Flexibility Export

@article{citeulike:4172405, abstract = {The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata , from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H 2 S), have been studied in molecular dynamics simulations. Features that account for differences in H 2 S affinity among the three have been examined. Our results verify the existence of an unusual heme rocking motion in unligated HbI that can promote the entrance of large ligands such as H 2 S. The FQF-mutant partially reproduces the amplitude and relative orientation of the motion of HbI's heme group. Therefore, besides introducing favorable electrostatic interactions with H 2 S, the three mutations in the distal pocket change the dynamic properties of the heme group. The active-site residues Gln-64(E7), Phe-43(CD1), and His-93(F8) are also shown to be more flexible in unligated HbI than in FQF-mutant and SW. Further contributions to H 2 S affinity come from differences in hydrogen bonding between the heme propionate groups and nearby amino acid residues.}, author = {Fernandezalberti, S. and Bacelo, D. and Binningjr, R. and Echave, J. and Chergui, M. and Lopezgarriga, J.}, citeulike-article-id = {4172405}, citeulike-linkout-0 = {http://dx.doi.org/10.1529/biophysj.106.081646}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0006349506718835}, day = {01}, doi = {10.1529/biophysj.106.081646}, issn = {00063495}, journal = {Biophysical Journal}, keywords = {flexibility, md}, month = {September}, number = {5}, pages = {1698--1709}, posted-at = {2009-03-13 18:38:22}, priority = {2}, title = {Sulfide-Binding Hemoglobins: Effects of Mutations on Active-Site Flexibility}, url = {http://dx.doi.org/10.1529/biophysj.106.081646}, volume = {91}, year = {2006} }

TY - JOUR ID - citeulike:4172405 L3 - citeulike-article-id:4172405 N2 - The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata , from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H 2 S), have been studied in molecular dynamics simulations. Features that account for differences in H 2 S affinity among the three have been examined. Our results verify the existence of an unusual heme rocking motion in unligated HbI that can promote the entrance of large ligands such as H 2 S. The FQF-mutant partially reproduces the amplitude and relative orientation of the motion of HbI’s heme group. Therefore, besides introducing favorable electrostatic interactions with H 2 S, the three mutations in the distal pocket change the dynamic properties of the heme group. The active-site residues Gln-64(E7), Phe-43(CD1), and His-93(F8) are also shown to be more flexible in unligated HbI than in FQF-mutant and SW. Further contributions to H 2 S affinity come from differences in hydrogen bonding between the heme propionate groups and nearby amino acid residues. IS - 5 JF - Biophysical Journal SN - 00063495 EP - 1709 TI - Sulfide-Binding Hemoglobins: Effects of Mutations on Active-Site Flexibility VL - 91 SP - 1698 KW - flexibility KW - md AU - Fernandezalberti, S AU - Bacelo, D AU - Binningjr, R AU - Echave, J AU - Chergui, M AU - Lopezgarriga, J PY - 2006/09/01/ UR - http://dx.doi.org/10.1529/biophysj.106.081646 ER -