Physicochemical Characterization and Phylogenetic Classification of the 2/2 Hemoglobins Family sheds light on their Molecular Functions.

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

Bariloche

Congreso; 5th Congress of the Asocación Argentina de Bioinformática y Biología Computacional; 2014

Asociación Argentina de Bioiniformatia y Biologia Computacional

Theglobinfamilyofhemeproteinsofferalarge,diverseandthoroughlystudiedsetofproteins,whosefunctionistightlyrelatedtosmallligand(mainlyO2butalsoNO,CO,andH2S)affinityandreactivity.Usually,thosedisplayinghighO2affinityfunctionasO2-redoxrelatedenzymes,likeNOdioxygenasefunctionofMycobacteriumtuberculosis2/2HbN.Moderateaffinityglobinsusuallyactasoxygencarriers,likemammalianmyoglobin,whilelowO2affinityglobinsareNOorCOsensors,likesolubleguanylatecyclase.Assumingthattheproteinfunctioniscodedinthestructurethroughthedeterminationofitschemicalproperties,wepresentastudyaimedtoclassifyingandcharacterizingthewhole2/2Hbsfamily,assigningtoeachproteinthusaputativeO2affinitybasedonligandentryandstabilization.Inthisworkweemployedacombinedbioinformatics,physicochemicalandphylogeneticapproachestodescribeandassignkey2/2HbsfeaturesthatinturndetermineO2affinity.Ourresultsconfirmandextendpreviousclassificationsandincludeacompletedescriptionofthedivergenceofdifferentsubgroupsatthemoleculalevel.PDF is not the exact since this concerned an Oral presentation,