hameproteins 2 Flashcards
left shift has : — affinity for 02
right shift has: — of o2 due to the – of ph and – of h+ concentration. The h+ and 02 both compete for the binding to —
- high
- low
- decrease ph
- increased H
- hemaoglobin
if we — the acidity and — h+ the haemoglobin will becomes less likely to bind to 02 for a given po2
- increased , increased
at 40mmhg of 02 — % ~ to haemoglobin at ph — saturated
at 40mmgh > of 02 > – of haemoglobin at ph – saturated w/ o2
- 45% , 6.8
- 80% , 7.6
oxygenation occurs in the
lungs
at the lungs 02 levels are —
high
02 levels in the muscles are — and ph is — due to —-
- low
- low
-respiration
the affinity of myoglobin for o2 is — than haemoglobin and 02 will be transferred from – to —-
- higher
- oxyhemoglobin
-myoglobin - fromula: hb+ (02)4 equilibrum hb+ 4 02 equilibrum 4 Mb02
at the muscles — occurs by using — to produce — hence muscle’s ph is — and 02 levels are —
- respiration
- 02
-co2
low - low
H+ is produced in the — by —–
muscles , metabolism
haemoglobin also transports — and — . Free — at the muscles will bind to — and — and transports it to the —
- co2 and h+
- heamoglobin
- c02 and h+
- lungs
most co2 produced in — reacts with — by the catalyst — and is converted into —- in erythrocytes
- respiration
- water
- carbonic anhydrase
- bicarbonate ( HCO3-)
- formula: co2 + h20 —> <— hco3- + h+
some co2 will react with haemoglobin to form — which is — and —
- haemoglobin
- carbomate
- carboxylic acid with an animo group
- fromula: c02 + R-NH2 equilibrum crabomate + h+
h+ are transported by – to the side chains of the number of amino acids risidues and produces — charged groups
- binding
- positive
- ( the amino acid residues in proteins are numbered, so histadine 122 alpha is 122nd amino acid residue from the end of the alpha chain )
— is a compact tense structure which the globin chains interact with —- so haemoglobin is said to be in a — state
- haemoglobin
- salt linkages/ electrostatic
- t- state ( tense , taut )
the process of cooperative oxygen binding aka cooperativity :
- addition of the first 02 to haemoglobin is difficult
- when this happens the fe II will be converted from high spin to low spin
- this causes the fe II to shrink and moves into the porphyrin plane
- proximal histadine attached to iron moves w/ it
- globin chain which histadine belongs to also moves
- causes breakage in the salt bridges and the whole structure will relax and opens
- the other heam group becomes exposed and 2nd,3d,4th 02 molecule can be added
