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$:
He + 40, <== HbOs
oxyhac imo globinEach Fation acts a0 the contra of a compdar jon.
The ligands are the four A) axtoma of the hasin,
the N ecm of @h ainche acc Chestielive) sitle -chach
on the potypypticte ancl an onygin molrcle .
protein chain
Tha complex (on th Passes globch
As the equecion Hb +40, Hb, show, the bewding
cf oxygen fo hatinoglabeh it om eguiléhiiiom proces
In The lungs , Where the oxygen concentration 1S high,
the pesition ft librium movsrte the nght, Se
oxygen is bound to haciegloben ,
In mmuacle -Fissucs, Where the oxygen conton traction 44
fow, the position of equclibrlum Moves to the Left,
Se orygen 2 releasect for cellular rupiration ,The oxygen 13 dose shongly browdk 4o tHe Fe2 con
than the other ligonols .
HH ts remove when the ved blevd bls reach the
Hissues whore otygen iS reputvact .
The orygen Iigond con be viplaced by another
Higancl thet binds move Stromaly to the Fe2t ton,
Carbon hohexida Imolreutes will aloo berel te
hachoglobin , occupychy ths site morimallg occapiect
by oxygen.
Carbon monoxide mo lreler are bone 200 Hikes
more, chong ly than oxygen ih an irreversthle
reaction,
Thay Corben bohoricla i$ 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