Metals in bislegical systema (A) Scopes: —Undicstond thet tome metals are esoenttod do life amok chle ty explacn the Chetty invevecl , ~ Feeegnise thet Sohne mtale ore foxte ancl discuse, 1h Chemical terms, tha prhkins associated With heavy natal ih the ehyivonin ent entering the food chara — For ty. Mercury ,Scoma mtal Ort eassrtiol to life Mansy meatal fena plo vital reles ih bactabotism Some ave Prumel naturally jn ovr bookies anol arte pasintial Por Aeodth . I. [ron (II) tone, Fe? are a component of -hatinoglobin Iron is also involved in Ha function of egfochromea, whieh cre Linked to ATP production ih oxidechive phosphorylation is Zine fom, Zn*t act 23 cofactors 1h many engyme coclycect react ong, | Sodkium and potassinin (ong areihvelved in maintening cheetolyte balance fh our Colle and jh generating Marve ineprate .Lon and ~hesmoglobin, Hoamoglebin i an enya oncoming. postisn prasocl jr rect blooedl celle , Haemoglobin conadts oa Awe pairs of potypaptide. subunits % an B. fy hasin group, which contacts Fa’ * Jona is bonctect to each subunit: ee a. The structure of hashoglobin showing Lovip chanins b. The stracture of Aecin when nat hovel to a protech. Each ~hasm group com binel one oxygen molecule . Each of the fur chasm grasps com binel oke ory prclecute at the Same Hie So the ovsratl reaction for a complete molecule of rheaimoglobin CHb) i$: He + 40, <== HbOs oxyhac imo globinEach Fation acts a0 the contra of a compdar jon. The ligands are the four A) axtoma of the hasin, the N ecm of @h ainche acc Chestielive) sitle -chach on the potypypticte ancl an onygin molrcle . protein chain Tha complex (on th Passes globch As the equecion Hb +40, Hb, show, the bewding cf oxygen fo hatinoglabeh it om eguiléhiiiom proces In The lungs , Where the oxygen concentration 1S high, the pesition ft librium movsrte the nght, Se oxygen is bound to haciegloben , In mmuacle -Fissucs, Where the oxygen conton traction 44 fow, the position of equclibrlum Moves to the Left, Se orygen 2 releasect for cellular rupiration ,The oxygen 13 dose shongly browdk 4o tHe Fe2 con than the other ligonols . HH ts remove when the ved blevd bls reach the Hissues whore otygen iS reputvact . The orygen Iigond con be viplaced by another Higancl thet binds move Stromaly to the Fe2t ton, Carbon hohexida Imolreutes will aloo berel te hachoglobin , occupychy ths site morimallg occapiect by oxygen. Carbon monoxide mo lreler are bone 200 Hikes more, chong ly than oxygen ih an irreversthle reaction, Thay Corben bohoricla i$ Vig Peisencua beacause. it com comme haemoglobin fo lose its eKYgen — comycng function .Exerecse | Harm is an impertont prosthactie rp whech contacha jren at its Contre & Ppsthehic groups endl comsymas are What isthe difference betwen a prosthetic and & coenzyme ? 6. Give two important feature about the attach mend of oxygen fo ach hasta globin bao lrente, C. Name another important group of protecua thet contin the hacen grep - Where Ore thea protecns locatrcl in the coll . Workchas Q. Prosthetic pops Ore Permanent ty bound to @ porticrlan 23 yy me Coamsyinea are ret permanently ound te ar mi yins , b, The oxygen Molecule is a bijond and if eHackas fo on Fe*f ion at the Contre of a hasin rp. The bonding of cry gin molecale to Fie ron, 's sthorg erengh for if to travel ih the blood witheut beeing displacat eauly by other ligands TH is removed whin the ved bloccl all reach the Aissuss whore onygon 's regina, C, myoglobin in muscle ASS Ke, both cofactors ay