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What is the Function of Hemoglobin in the Human Body

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Home»Science»Biology»CellBiology»WhatistheFunctionofHemoglobinintheHumanBody
WhatistheFunctionofHemoglobininthe
HumanBody
February19,2017 •byLakna •5minread
2
Hemoglobin(Hb)isametalloproteinfoundinredbloodcells.
Red blood cells transport Oxygen throughout the body. All
vertebratesexceptfish,havehemoglobinintheredbloodcells
asthe oxygen carrier.Hemoglobin makes up the 96% of dry
weight of the red blood cell and contains iron. All human
bodiescontainhemoglobin.Thenormalhemoglobinlevelofa
normal male adult is 13.8 – 17.2 g/dL. Adult female (non
pregnant)shouldhave12.1–15.1g/dLofhemoglobin.
Thisarticlewilllookat,
1.WhatisthestructureofHemoglobin
2.WhatistheFunctionofHemoglobinintheHumanBody
WhatistheStructureofHemoglobin
Hemoglobinisamultisubunitglobularprotein,whichhasaquaternary structure– fourglobin subunitsarearranged
inatetrahedralstructure.Eachglobularproteinsubunitcontainsaproteinchainwhichisassociatedwithnonprotein,
prosthetichemegroup.Thealphahelixstructureoftheglobinproteinscreatesapocketwhichbindsthehemegroup.
Globinproteins are synthesized by ribozymes in thecytosol. The Heme part is synthesized inthe mitochondria. A
chargedironatomisheldintheporphyrinringbycovalentbindingofironwithfournitrogenatomsinthesameplane.
These N atoms belong to the imidazole ring of the F8 histidine residue of each of the four globin subunits. In
hemoglobin,ironexistsasFe .
Thehumanbodycontainsthreehemoglobintypes:HemoglobinA,HemoglobinA ,andHemoglobinF.Hemoglobin
A is the most common type. Hemoglobin A is encoded by HBA1, HBA2, and HBB genes. The four subunits of
Hemoglobin A consist of two α and two β subunits (α β ).Hemoglobin A2 and Hemoglobin F are rare, and they
consistoftwoαandtwoδsubunitsandtwoαandtwoγsubunitsrespectively.Ininfants,thehemoglobintypeisHbF
(α γ ).
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Figure1:StructureofHemoglobin
WhatistheFunctionofHemoglobinintheHumanBody
1.Hemoglobinisanoxygencarrier.
2.Hemoglobinisacarbondioxidecarrier.
3.Hemoglobingivestheredcolortoblood.
4.Hemoglobinmaintainstheshapeoftheredbloodcells.
5.Hemoglobinactsasabuffer.
6.Hemoglobininteractswithotherligands.
7.Hemoglobindegradationaccumulatesphysiologicallyactivecatabolites.
OxygenCarrier
The major function of hemoglobin is the transportation of oxygen from lungs to all the tissues of the body. The
oxygenbindingcapacityofhemoglobinis1.34mLO pergram.Eachglobinsubunitofthehemoglobinmoleculecan
bindwithoneFe ion.TheaffinityofhemoglobintowardsoxygenisgainedbytheFe ion.EachFe canbindwith
oneoxygenmolecule.ThebindingofoxygenoxidizesFe intoFe .Oneatomoftheoxygenmolecule,whichbinds
toFe becomesasuperoxide,wheretheotheroxygenatomprotrudesatanangle. Theoxygenboundhemoglobinis
referred to as oxyhemoglobin. When blood reaches an oxygen deficient tissue, oxygen is dissociated from
hemoglobin and diffused into the tissue. The O is the terminal electron acceptor in the process called oxidative
phosphorylation in the production of ATP. The removal of O turns the iron into its reduced form. The oxygen
unboundhemoglobin is referredtoas deoxyhemoglobin.Oxidationof Fe intoFe creates methemoglobin which
cannotbindwithO .
CarbonDioxideCarrier
Hemoglobinalsotransportscarbondioxidefromtissuestolungs.80%ofthecarbondioxideistransportedviaplasma.
Carbondioxide doesnotcompete withtheoxygenbindingsiteof hemoglobin.Itbinds totheprotein structureother
thanironbindingposition.Thecarbondioxideboundhemoglobinisreferredtoascarbaminohemoglobin.
InfluenceonRedBloodCells
Hemoglobingivesared color to red bloodcellsbyFe ions.Withred bloodcells,bloodreachestoitsunique red
color.Plasma, without red blood cells, has a pale yellow color. The shape of the red blood cells is maintained by
hemoglobin. Red blood cells are biconcave disks which are flattened and depressed in the center. They have a
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dumbbellshapedcrosssection.Hemoglobingenealsoconsistsofvariousalleles.Mostmutantsmaycausenodisease.
Butsomemutantsmaycausehereditarydiseaseslikehemoglobinpathesis.
Figure2:Redbloodcells
BufferingAction
HemoglobinmaintainsthebloodpHat 7.4.Accumulation ofcarbondioxideintheblooddecreasesthepHfrom7.4.
Thechangeof the pH canbereversedby ventilation. Due tothisbufferingaction of hemoglobin,alltheenzymatic
reactionsinthebody,whichprefersthispH,cantakeplacewithoutanydisturbance.
InteractionwithLigands
Hemoglobinsalso bindtootherligandssuchascarbonmonoxide,nitrogenoxide,cyanide,sulfur monoxide,sulfide,
and hydrogen sulfide. Binding of carbon monoxide may sometimes be lethal because the binding is irreversible.
Hemoglobincanalsotransportdrugstotheirsiteofaction.
ProductionofPhysiologicalActiveCatabolites
Aging and defects in the cell can kill the red blood cells, accumulating various physiologically active catabolites.
Hemoglobinof thedeadred bloodcellsisclearedfrom thecirculationby thehemoglibintransporter,CD163.Heme
degradation, which occurs in monocytes and macrophages, is a natural source of the carbon monoxide generation.
Bilirubin is the final product of heme degradation. It is secreted as bile into intestine. Bilirubin is converted into
urobilinogenwhichisfoundinfeces,givingtheuniqueyellowcolor.Ontheotherhand,iron,whichisremovedfrom
hemeisconvertedtoferritinandstoredintissuesforthelateruse.
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AbouttheAuthor:Lakna
Lakna,agraduateinMolecularBiology&Biochemistry,isaMolecularBiologistandhasa
broadandkeeninterestinthediscoveryofnaturerelatedthings
Hemoglobincanalsobefound in other cells of the body than red blood cells. Other hemoglobin carrying cells are
macrophages,alveolarcells in lungs and mesangialcellsinthe kidney.Hemoglobinfunctions as a regulatorofiron
metabolismandanantioxidantinthesecells.
Reference:
1.“Hemoglobin”.Wikipedia,thefreeencyclopedia.2017.Accessed15Feb.2017
2.DavisC.P.andShielW.C.“Hemoglobin”.MedicineNet,2015.htm.Accessed15Feb.2017
3.“StructureandFunctionsofhemoglobin”.AllMedicalstuff,2017.Accessed15Feb.2017
ImageCourtesy:
1.“1904Hemoglobin”ByOpenStaxCollege–Anatomy&Physiology,ConnexionsWebsite.Jun19,2013.(CCBY
3.0)viaCommonsWikimedia
2.“Redbloodcells”ByJessicaPolka–Ownwork(CCBYSA4.0)viaCommonsWikimedia
2
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... 6 Hemoglobin F (HbF), also known as fetal hemoglobin, is usually present at levels of 65 to 90% in a newborn baby but drops in concentration to less than 2% when the baby is 6 months to 12 months of age. 6,7,8 It consists of two α and two gamma γ) subunits. The two gamma subunits enable HbF to have higher affinity for oxygen compared to the other two types of Hb, HbA and HbA2. ...
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Structure and Functions of hemoglobin
  • Feb 2015
  • C P Davis
  • W Shiel
Davis C. P. and Shiel W. C. "Hemoglobin". MedicineNet, 2015.htm. Accessed 15 Feb. 2017 3. "Structure and Functions of hemoglobin". All Medical stuff, 2017. Accessed 15 Feb.2017
By OpenStax College-Anatomy & Physiology, Connexions Web site
  • Jun 2013
  • HEMOGLOBIN
Hemoglobin" By OpenStax College-Anatomy & Physiology, Connexions Web site. Jun 19, 2013. (CC BY