Hemoglobin: Difference between revisions

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Eran Hodis, Joel L. Sussman, Marc Gillespie, Eric Martz, Jaime Prilusky, Alexander Berchansky, Karl Oberholser, Michal Harel, Ann Taylor, Mark Hoelzer, Karsten Theis, Tihitina Y Aytenfisu, Hannah Campbell

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 The three-dimensional structure of an <scene name='Journal:JBIC:8/Trhb/2'>Fe(II)-O2 complex of Tp trHb</scene> was determined at 1.73 Å resolution ([[3aq9]]). <scene name='Journal:JBIC:8/Trhb/3'>Tyr25 (B10) and Gln46 (E7) were hydrogen-bonded to a heme-bound dioxygen molecule</scene>. Tyr25 donated a hydrogen bond to the terminal oxygen atom, whereas Gln46 hydrogen-bonded to the proximal oxygen atom. Furthermore, <scene name='Journal:JBIC:8/Trhb/4'>Tyr25 was hydrogen-bonded to the Gln46 and Gln50 (E11) residues</scene>.
-The O<sub>2</sub> association and dissociation rate constants of ''T. pyriformis'' trHb were 5.5 μM<sup>-1</sup> s<sup>-1</sup>, and 0.18 s<sup>-1</sup>, respectively. The oxygen affinity was determined to be 33 nM. The autooxidation rate constant was 3.8 x 10<sup>-3</sup> h<sup>-1</sup>. These values are similar to those of <scene name='Journal:JBIC:8/Hbn/3'>HbN from Mycobacterium tuberculosis</scene>. Mutations at <scene name='Journal:JBIC:8/As/2'>Tyr25</scene>, <scene name='Journal:JBIC:8/Ad/2'>Gln46</scene>, and <scene name='Journal:JBIC:8/Trhb/11'>Gln50</scene> increased the O<sub>2</sub> dissociation and autooxidation rate constants, and partly disrupted the hydrogen-bonding network.
+The O<sub>2</sub> association and dissociation rate constants of ''T. pyriformis'' trHb were 5.5 μM<sup>-1</sup> s<sup>-1</sup>, and 0.18 s<sup>-1</sup>, respectively. The oxygen affinity was determined to be 33 nM. The autooxidation rate constant was 3.8 x 10<sup>-3</sup> h<sup>-1</sup>. These values are similar to those of <scene name='Journal:JBIC:8/Hbn/3'>HbN from Mycobacterium tuberculosis</scene>.
+'''Mutations:'''
+*Mutation at Tyr25: <scene name='43/435485/As/6'>Wildtype Y25 and mutant Y25F together</scene> and <scene name='43/435485/As/5'>animation of this scene</scene>. <jmol><jmolButton>
+<script>if (_animating); anim pause;set echo bottom left; color echo white; font echo 20 sansserif;echo Animation Paused; else; anim resume; set echo off;endif;</script>
+<text>Toggle Animation</text>
+</jmolButton></jmol>
+*Mutation at Gln46: <scene name='43/435485/Ad/4'>Wildtype Q46 and mutant Q46E together (animation)</scene> <jmol><jmolButton>
+<script>if (_animating); anim pause;set echo bottom left; color echo white; font echo 20 sansserif;echo Animation Paused; else; anim resume; set echo off;endif;</script>
+<text>Toggle Animation</text>
+</jmolButton></jmol>
+*Mutation at <scene name='Journal:JBIC:8/Trhb/11'>Gln50</scene> increased the O<sub>2</sub> dissociation and autooxidation rate constants, and partly disrupted the hydrogen-bonding network.
 An <scene name='Journal:JBIC:8/Ag/4'>Fe(III)-H2O complex of Tp trHb was formed following reaction of the Fe(II)-O2 complex of Tp trHb</scene>, in a crystal state, with nitric oxide. This suggests that ''Tp'' trHb functions in nitric oxide detoxification.