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    Hemoglobin and Myoglobin (2012)

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    Dr. Atif Hassan Khirelsied
    Myoglobin and Hemoglobin Atif H. Khirelsied, Ph.D.   Atif H. Khirelsied, Ph.D. Department of Biochemistry Faculty of Medicine International University of Africa, Khartoum, Sudan Myoglobin and Haemoglobin • M l bi Myoglobin and hemoglobin are hemeproteins. dh l bi h i • They are principally involved in binding molecular  oxygen.  Myoglobin • Is a monomeric hemoprotein.  • An intracellular storage for oxygen in muscle tissue.  • Releases its bound oxygen during periods of oxygen  deprivation.

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    Hemoglobin and Myoglobin (2012)

    Uploaded by

    Dr. Atif Hassan Khirelsied
    147 views29 pages
    Myoglobin and Hemoglobin Atif H. Khirelsied, Ph.D.   Atif H. Khirelsied, Ph.D. Department of Biochemistry Faculty of Medicine International University of Africa, Khartoum, Sudan Myoglobin and Haemoglobin • M l bi Myoglobin and hemoglobin are hemeproteins. dh l bi h i • They are principally involved in binding molecular  oxygen.  Myoglobin • Is a monomeric hemoprotein.  • An intracellular storage for oxygen in muscle tissue.  • Releases its bound oxygen during periods of oxygen  deprivation.

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    Hemoglobin and Myoglobin [2012]

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    Myoglobin and Hemoglobin Atif H. Khirelsied, Ph.D.   Atif H. Khirelsied, Ph.D. Department of Biochemistry Faculty of Medicine International University of Africa, Khartoum, Sudan Myoglobin and Haemoglobin • M l bi Myoglobin and hemoglobin are hemeproteins. dh l bi h i • They are principally involved in binding molecular  oxygen.  Myoglobin • Is a monomeric hemoprotein.  • An intracellular storage for oxygen in muscle tissue.  • Releases its bound oxygen during periods of oxygen  deprivation.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    147 views29 pages

    Hemoglobin and Myoglobin (2012)

    Uploaded by

    Dr. Atif Hassan Khirelsied
    Myoglobin and Hemoglobin Atif H. Khirelsied, Ph.D.   Atif H. Khirelsied, Ph.D. Department of Biochemistry Faculty of Medicine International University of Africa, Khartoum, Sudan Myoglobin and Haemoglobin • M l bi Myoglobin and hemoglobin are hemeproteins. dh l bi h i • They are principally involved in binding molecular  oxygen.  Myoglobin • Is a monomeric hemoprotein.  • An intracellular storage for oxygen in muscle tissue.  • Releases its bound oxygen during periods of oxygen  deprivation.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    of 29

    MyoglobinandHemoglobin

    AtifH.Khirelsied,Ph.D. Atif H. Khirelsied, Ph.D.


    DepartmentofBiochemistry

    FacultyofMedicine
    InternationalUniversityofAfrica,Khartoum,Sudan

    Myoglobin andHaemoglobin
    M l bi Myoglobinandhemoglobinarehemeproteins. dh l bi h i Theyareprincipallyinvolvedinbindingmolecular oxygen.

    Myoglobin
    Isamonomerichemoprotein. Anintracellularstorageforoxygeninmuscletissue. Releasesitsboundoxygenduringperiodsofoxygen deprivation. d i i

    Myoglobin structure
    Thetertiarystructureofmyoglobinisatypicalglobular protein. protein It h Ithasaveryhighproportion(75%)ofhelix. hi h ti (75%) f h li Comprises8helices,designatedAtoH,connectedby i 8 h li d i d db shortnonhelicalregions.

    Myoglobin peptide

    Myoglobin structure
    Aminoacidpackedintotheinteriorofthemoleculeare predominantlyhydrophobic whilethoseonthesurface arehydrophilic. h d hili

    Eachmyoglobinmoleculecontainsonehemeprosthetic groupinsertedintoahydrophobiccleftintheprotein.

    Myoglobin structure
    Eachhemeresiduecontainsonecentralcoordinately boundironatomintheFe2+ (ferrous)state.

    Th Theoxygenisbounddirectlytotheferrousironatom. i b d di tl t th f i t

    OxidationoftheirontotheFe3+(ferric)staterendersthe moleculeincapableofnormaloxygenbinding.

    Myoglobin structure
    Hydrophobicinteractionsbetweenthetetrapyrrolering andhydrophobicaminoacidontheinteriorofthecleft stronglystabilizethehemeproteinconjugate. t l t bili th h t i j t

    AnitrogenatomfromahistidineR grouplocatedabove theplaneofthehemeringiscoordinatedwiththeiron atomprovidesfurtherstabilization. f

    Porphyrin ring

    Heme

    Myoglobin
    Inoxymyoglobin the6thcoordinatepositionisoccupied bytheoxygen,whosebindingisstabilizedbyasecond histidineresidue. histidine residue.

    CObindscoordinatelytohemeironinamannersimilar tothatofoxygen,butismuchstronger.

    Haemoglobin
    Hemoglobinisatetrameric hemeproteinfoundinRBCs g p Each subunit of a hemoglobin has a heme prosthetic Eachsubunitofahemoglobinhasahemeprosthetic group. Thepeptidesaredesignated,,,and whichare arrangedintovariousformsoffunctionalhemoglobins. g g

    Developmentalpatternofthequaternarystructureoffetal andnewbornhemoglobins g

    Haemoglobin
    ThesecondaryandtertiarystructureofHb.subunits aresimilar,withextensivehomologyinaminoacid composition.

    ThequaternarystructureofHb.yieldstophysiologically importantallostericinteractionsbetweenthesubunits,

    Myoglobin

    Th ThecurveofoxygenbindingtoHbissigmoidal f bi di t Hb i i id l typicalofallosteric. When oxygen binds to the first subunit of Whenoxygenbindstothefirstsubunitof deoxyhemoglobinitincreasestheaffinityofthe remainingsubunitsforoxygen. remaining subunits for oxygen

    ThecurvesofoxygenbindingtoHb andMb

    TheeffectofoxygenbindingtoHb.
    Binding of oxygen to iron of deoxyHb pulls the iron BindingofoxygentoironofdeoxyHbpullstheiron atomintotheplaneoftheheme. SincetheironisalsoboundtohistidineF8,this residueisalsopulledtowardtheplaneoftheheme ring. i The resulting conformational change is transmitted Theresultingconformationalchangeistransmitted throughoutthepeptidebackbonecausingasignificant changeintertiarystructureofHb. g y

    TheeffectofoxygenbindingtoHb.
    The conformation of the low affinity, deoxygenated Theconformationofthelowaffinity,deoxygenated hemoglobin(Hb)isknownasthetaut(T)state. Theconformationofthefullyoxygenatedhighaffinity formofhemoglobinisknownastherelaxed(R)state. form of hemoglobin is known as the relaxed (R) state

    TheconformationalchangesduringoxygenbindingtoHb.

    Deoxygenated D t d

    Oxygenated

    The regulation of oxygen binding to Hb

    InthecontextoftheaffinityofHb foroxygenthereare fourprimaryregulators,eachofwhichhasanegative p y g , g effect.Theseare o CO2, o hydrogen ion (H+), hydrogenion(H ), o chlorideion(Cl), o 2,3bisphosphoglycerate.

    TheregulationofoxygenbindingtoHb
    InthehighpO2 ofthelungsthereissufficientO2 to g p g overcometheinhibitorynatureoftheTstate. TheO2 bindinginducesalterationfromtheTformto theRform.

    TheregulationofoxygenbindingtoHb

    Whenoxyhemoglobinreachesthetissuesthe pO2issufficientlylow,aswellasthepH( 7.2), pO2 is sufficiently low as well as the pH (~7 2) thattheTstateisfavoredandtheO2 released. 4O2 +Hb<>nH++Hb(O2)4

    TheregulationofoxygenbindingtoHb
    Inthetissues,CO2,H+andCl exerttheirnegativeeffects onHbbindingofO2 MetabolizingcellsproduceCO2 whichdiffusesintothe bloodandentersthecirculatingRBCs. WithinRBCstheCO2israpidlyconvertedtocarbonic acidthroughtheactionofcarbonicanhydrase.

    TheregulationofoxygenbindingtoHb
    TheHCO3 ionproducedinthisdissociationreactiondiffuses outoftheRBCandiscarriedinthebloodtothelungs. t f th RBC d i i d i th bl d t th l This effective CO2 transport process is referred to as ThiseffectiveCO transportprocessisreferredtoas isohydric transport. Approximately80%oftheCO2 producedinmetabolizingcells istransportedtothelungsinthisway. AsmallpercentageofCO2istransportedinthebloodasa dissolvedgas. dissolved gas

    Theroleof2,3bisphosphoglycerate
    2,3bisphosphoglycerate derivedfromtheglycolysis. It is a potent allosteric effector on the oxygen binding Itisapotentallostericeffectorontheoxygenbinding propertiesofHb. 2,3BPGbindstoacavityinthecenterofthe deoxygenatedTformofHb. d t dTf f Hb

    Theroleof2,3bisphosphoglycerate
    Increased2,3BPGconcentrationfavorsconversion , ofRformHbtoTformHbanddecreasesthe amountofoxygenboundbyHbatanyoxygen concentration. concentration

    HBFbindingaffinity
    Hb molecules differing in subunit composition have Hb.moleculesdifferinginsubunitcompositionhave different2,3BPGbindingproperties. Forexample,HbF binds2,3BPGmuchlessavidlythan HbA. HbFinfetusesbindsoxygenwithgreateraffinity than themothersHbA. the mothers HbA

    HBalsotransposrts CO2 andprotonstolungs


    HemoglobincarriesCO2 ascarbamatesformedwith theaminoterminalnitrogensofthepolypeptide chains.

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