Physicochemical and Phylogenetic Approaches shed Light on complete 2/2 Hemoglobins Family Classification and Characterization.

BUSTAMANTE JP; BOECHO L; RADUSKY L; ARJEN TEN HAVE; ESTRÍN DA; MARTÍ MA

Sheffield

Conferencia; XVIII International Conference on ?Oxygen-binding and sensing proteins?; 2014

Theglobinfamilyofhemeproteinsofferalarge,diverseandthoroughlystudiedsetofproteins,whosefunctionistightlyrelatedtosmallligand(mainlyO2butalsoNO,CO,andH2S)affinityandreactivity.Usually,thosedisplayinghighO2affinityfunctionasO2-redoxrelatedenzymes,likeNOdioxygenasefunctionofMycobacteriumtuberculosis2/2HbN.Moderateaffinityglobinsusuallyactasoxygencarriers,likemammalianmyoglobin,whilelowO2affinityglobinsareNOorCOsensors,likesolubleguanylatecyclase.Assumingthattheproteinfunctioniscodedinthestructurethroughthedeterminationofitschemicalproperties,wepresentastudyaimedtoclassifyingandcharacterizingthewhole2/2Hbsfamily,assigningtoeachproteinthusaputativeO2affinitybasedonligandentryandstabilization.Inthisworkweemployedacombinedbioinformatics,physicochemicalandphylogeneticapproachestodescribeandassignkey2/2HbsfeaturesthatinturndetermineO2affinity.Ourresultsconfirmandextendpreviousclassificationsandincludeacompletedescriptionofthedivergenceofdifferentsubgroupsatthemoleculalevel.