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COBALT AS AN ENZYME.??
Somemetalsdirectlyexistasenzymesandinsomecasesthese setofenzymesrequireacoenzymeoracofactorfortheiractivity coenzymedependent. Theenzymebecomesfunctionalonlywhenthecoenzymebindsto them. Thecobaltispresentasalinkageinthecorrinringinthese coenzymeandactsasanenzyme,hencecalledascobaltenzyme. Example:B12 (withcorrinring) Thereareseveralenzymescontainingcobaltinaformotherthan thatinthecorrinringofvitaminB12.
COBALAMINE-
VITAMIN B12
VitaminB12 anditscoenzymeformsareprominentcobaltcontaining cofactors. Theyarepartofthelargerclassofthenaturaltetrapyrrolicmetal complexes. Ithasagroupofcobaltcontainingvitamercompoundswhichinclude: cyanocobalamin(anartifactformedfromusingactivatedcharcoal, whichalwayscontainstracecyanide,topurifyhydroxycobalamin) hydroxocobalamin(anothermedicinalform,producedbybacteria) thetwonaturallyoccurringcofactorformsofB12 :adenosylcobalamin andmethylcobalamin. B12 isthemostchemicallycomplexofallthevitamins. ThestructureofB12 isbasedonacorrinring.
STRUCTURE
ItisaCOENZYMECOBALTCOMPLEXwherethemetalion issituatedatthecentreofthemacrocyclicplanarringcompound of4(four)pyrrolederivatives. Cobaltmetalionisdirectlybondedtothe5 carbonatomof thedeoxyribosemoiety.
Thisfurherbondedtoadenine.
Ontheothersideofthering,cobaltisattachedtothe dimethylbenzimidazolebase.
Thisinturnislinkedtothesidechainofapyrrolering throughriboseandphosphatemoieties.
COBALAMINE
Formula:C63 H88 CoN14 O14 P Mol.Mass:1355.37g/mol Colinkedto5deoxyadenosyl AgainCoattachedtodimethyl benzimidazolebase. Inturnlinkedtosidechainof pyrrole ringthroughriboseandphosphate moieties.
MAINSOURCES COBALTENZYMES.
Source
Animals, yeast, bacteria Archae Actinomycetes and bacteria Actinomycetes Actinomycetes and yeast
Cofactor content
2 Co per subunit 12 Co per subunit 1 Co in each -subunit 1 Co per 4 subunits
Methylmalonyl-CoA Bacteria carboxytransferase Aldehyde decarbonylase Algae Lysine-2,3aminomutase Bromoperoxidase Cobalt-porphyrincontaining protein Bacteria Bacteria Bacteria
1 Co, 1 Zn per subunit 1 Co- porphyrin per subunit 0.51 Co per subunit
Itisusedasaconcentratedsourceofradiationincancer therapyandfoodsterilization,andasaradioactivetracerin biologicalandindustrialapplications. Ithasalsoservedasaspectroscopicprobeinmetalloenzymes. Substitutingcobaltforzinchasoftenbeenausefultoolto investigatethestructuralbasisofcatalyticpropertiesinzinc enzymes. B12 isnormallyinvolvedinthemetabolismofeverycellofthebody, especiallyaffectingtheDNAsynthesisandregulationbutalsofatty acidsynthesisandenergyproduction.
CoenzymeB12 'sreactiveCCobondparticipatesinthreemain typesofenzymecatalyzedreactions.Theyareasfollows: Isomerases:Rearrangementsinwhichahydrogenatomis directlytransferredbetweentwoadjacentatomswith concomitantexchangeofthesecondsubstituent,X,whichmay beacarbonatomwithsubstituents,anoxygenatomofan alcohol,oranamine. Methyltransferases:Methyl(CH3)grouptransfers betweentwomolecules. Dehalogenases:Reactionsinwhichahalogenatomis removedfromanorganicmolecule.Enzymesinthisclasshave notbeenidentifiedinhumans.
Conclusion:
Although metal ions play a variety of roles in natural proteins, including nucleophilic catalysis, electron transfer, and the stabilization of protein structure, the functions of cobalt have rarely been studied. Cobalt is used in a limited number of enzymes, unlike iron and zinc.
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