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
the protein in the oxyhemoglobin is in the — sate since there are few — present in the haemoglobin
- R-state , relaxed
- few salt linkages
— protein is one which interaction at one site in the molicule affects interaction of the remote site
- allosteric protein
which of those are allosteric protein: - haemoglobin
- myoglobin
- both
- none
- haemoglobin
allosteric effects in haemoglobin includes:
- 02 binding in one site will help the 02 binds in the remote site in the same molecule
- binding of h+ and c02 in a site results in charged groups being formed which promotes the formation of salt bridges ( ie. t state ) which squeeze the 02 out
- binding of 02 to haemoglobin in alveolar capillaries of the the lungs causes the breaking of salt bridges and releasing of c02 and h+
the inter relationship between h+ , co2, and 02 is known to be:
bohrs effect
— is produced when c is burned in the presence of 02 and the properties are —
carbon monoxide
- 2c + 02 –> 2co
- colorless , ouderwets cab ve found in the vehicles of the exhaust fumes , house fires or poorly maintained oil and gas hearers. also known as the: silent killer
why is CO toxic?
- the affinity of haemoglobin to co is 225 times greater than its affinity for 02
- binding is string and is irrversable
- affinity of myoglobin for co is 25 times greater than 02
hb + 4 co –> hb ( co) 4 is known as
carbomoxoheamomyglobin
If the fe-c trible bond 0 was – no — would be involved in the affinity for haemoglobin for c trible bond 0 and it would be —- times greater than affinity for — which means any exposure would kill us
- linear
- no hydrogen bonding
- 25,000 greater
- 02
affinity of haemoglobin for co is only — than 02 because of the —- of stability of the co complex increases the stability for —
- 225
- reduction of stability
- 02
— is located close to 02 and co binding site forces the co to bind in an — which — the complex which is considered to be a —-
- distal histadine ( no fe coordinated unlike proximal )
- angle
- destabilises
- steric effect
02 is stabilised by the presence of —- between partially — on non bridging oxygen and the distal histadine
-strong h+
- negative
—- stabilises the oxyhemaoglobin by — more than it does in —-
which is the most important thing.
- distal histadine
- hydrogen bonding
- carbinmonxohymoglobin
AGAIN LOL: why is it toxic:
- hydrogen bonding between – and — stabilises the — of haemoglobin much more than —
- 02
- distal histadinbe
- 02 complex
- ( the poison is treated by administering 02 under high pressure 2 or 3 atm as in hyperbaric )
