HemoglobinandtheMovementof*Oxygenoregonstate.edu/instruct/bb450/450material/Keynotes... ·...

Hemoglobin and the Movement of Oxygen

Hemoglobin and the Movement of Oxygen• Introduction

Animals Have Widely Varying Needs for OxygenDemand for Oxygen Can Change in SecondsBasal Needs are Significant - Diffusion not Enough

Animals Have Widely Varying Needs for OxygenDemand for Oxygen Can Change in SecondsBasal Needs are Significant - Diffusion not EnoughExercise, Fight/Flight Add to the Need

Animals Have Widely Varying Needs for OxygenDemand for Oxygen Can Change in SecondsBasal Needs are Significant - Diffusion not EnoughExercise, Fight/Flight Add to the NeedATP Energy Produced Aerobically 15 Times More Efficiently Than Anaerobically

Respiration versus Fermentation

Respiration versus FermentationEfficient, Adaptable Oxygen Delivery is Necessary

Quaternary Structure• Interaction of multiple protein subunits

Hemoglobin - 4 Subunits (α2β2), 1 Heme Each, 1 O2 Each, 1 “Donut Hole”Myoglobin - 1 Subunit, 1 Heme, 1 O2 Each

Hemoglobin and the Movement of Oxygen• Structure and Function

Heme Prosthetic GroupFerrous Iron - Methemoglobin Won’t WorkOnly Fe++ Binds Oxygen

Edge-on View

Attached to Remainder of Global Subunit

Edge-on View

Histidine’s Movement Changes

Global Unit’s Shape

Hemoglobin and the Movement of Oxygen• Cooperativity

Exiting Lungs

Entering Lungs

Exiting Lungs

No Oxygen (T-State)

Entering Lungs

Exiting Lungs

No Oxygen (T-State)

Oxygen Bound

Entering Lungs

Exiting Lungs

No Oxygen (T-State)

Oxygen Bound

Affected by O2 Binding (R-State)

Entering Lungs

Exiting Lungs

No Oxygen (T-State)

Oxygen Bound Affected by O2 Binding

R-State

Entering Lungs

Exiting Lungs

No Oxygen (T-State)

R-State

Entering Lungs

Exiting Lungs

Fully Oxygenated (R-State)

No Oxygen (T-State)

R-State

Binding of the first O2 favors binding of second, etc. - CooperativelyCooperatively Important as Hemoglobin Rapidly Passes Through Lungs

Entering Lungs

Exiting Lungs

Fully Oxygenated (R-State)

At Low O2, Myoglobin Holds More than Hemoglobin

At High O2, Both Hold 100%

Hyperbolic Binding Curve

Sigmoidal Binding Curve

Hyperbolic Binding Curve

As Curves Move to Right Less Affinity for Oxygen

Myoglobin Better for Storing OxygenHemoglobin Better at Delivering Oxygen

As Curves Move to Right Less Affinity for Oxygen

Hemoglobin and the Movement of Oxygen• Bohr Effect

Less Oxygen Bound at Same Pressure

More O2 Required To Have Same Fraction Bound

More Affinity

Less Affinity

Protons Can Bind to HemoglobinProtons Change Hemoglobin’s Shape Reshaped Hemoglobin Loses Oxygen

Rapidly Metabolizing Tissues Release Protons

Rapidly Metabolizing Tissues Release ProtonsRapidly Metabolizing Tissues Get More Oxygen From Hemoglobin

Hemoglobin and the Movement of Oxygen• Bohr Effect & CO2

Acid Favors Release of O2 From HemoglobinCO2 Favors Release of O2 From Hemoglobin

Hemoglobin and the Movement of Oxygen• Bohr Effect & CO2

Acid Favors Release of O2 From HemoglobinCO2 Favors Release of O2 From Hemoglobin

Acid and CO2 are Released by Rapidly Metabolizing Tissues

Hemoglobin and the Movement of Oxygen• 2,3 BPG

2,3 Bisphosphoglycerate

Byproduct of GlycolysisExercising Muscle Cells Rapid Use GlycolysisExercising Muscle Cells Produce Acid, CO2, and 2,3 BPG

Byproduct of GlycolysisExercising Muscle Cells Rapid Use GlycolysisExercising Muscle Cells Produce Acid, CO2, and 2,3 BPGBinds in Hole of Donut

Byproduct of GlycolysisExercising Muscle Cells Rapid Use GlycolysisExercising Muscle Cells Produce Acid, CO2, and 2,3 BPGBinds in Hole of DonutLocks Hemoglobin in T-State

Hemoglobin and the Movement of Oxygen• 2,3 BPG and Oxygen Binding

Slow Metabolic Rate

Fast Metabolic Rate

Rapidly Metabolizing Cells Produce AcidRapidly Metabolizing Cells Release CO2

Rapidly Metabolizing Cells Release 2,3 BPG

All Favor O2 Release from Hemoglobin

All Favor O2 Release from Hemoglobin So

Rapidly Metabolizing Cells Get More O2

Hemoglobin and the Movement of Oxygen• 2,3 BPG and Smoking

2,3 BPG Big Concern for SmokersBlood of Smokers has High Levels of 2,3 BPGHemoglobin Gets Locked in T-state in Passage Through Lungs

2,3 BPG Big Concern for SmokersBlood of Smokers has High Levels of 2,3 BPGHemoglobin Gets Locked in T-state in Passage Through LungsOxygen Carrying Capacity of Blood Reduced

2,3 BPG Big Concern for SmokersBlood of Smokers has High Levels of 2,3 BPGHemoglobin Gets Locked in T-state in Passage Through LungsOxygen Carrying Capacity of Blood ReducedCarbon Monoxide Levels Also Higher in Smokers

Hemoglobin and the Movement of Oxygen• Movement of CO2

Rapidly Metabolizing Tissue

HbO + H+ O2 Blood

H+:Hb-CO2

HbO + H+ O2 Blood

Rapidly Metabolizing Tissue Some

H+:Hb-CO2

HbO + H+ O2 Blood

H+:Hb-CO2

RemainderH2O

HbO + H+ O2 Blood

H+:Hb-CO2

RemainderH2O

HbO + H+ O2 Blood

H+:Hb-CO2

LungsO2 + H+:Hb-CO2

H+:Hb-CO2

RemainderH2O

HbO + H+ O2 Blood

H+:Hb-CO2

LungsO2 + H+:Hb-CO2

H+:Hb-CO2

RemainderH2O

HbO + H+ O2 Blood

H+:Hb-CO2

HbO HbO

LungsO2 + H+:Hb-CO2

H+:Hb-CO2

RemainderH2O

HbO + H+ O2 Blood

H+:Hb-CO2

HbO HbO

H2O + CO2 LungsO2 + H+:Hb-CO2

H+:Hb-CO2

RemainderH2O

HbO + H+ O2 Blood

H+:Hb-CO2

HbO HbO

H2O + CO2 LungsO2 + H+:Hb-CO2

H+:Hb-CO2

RemainderH2O

HbO + H+ O2 Blood

H+:Hb-CO2

HbO HbOExhaled

Hemoglobin and the Movement of Oxygen• Carbon Monoxide and Heme

An Additional Histidine is Present at the Heme Iron SiteReduces Affinity to CO, but Does Not Eliminate itCarbon Monoxide in Cigarette Smoke

Hemoglobin and the Movement of Oxygen• Carbon Monoxide and Heme

An Additional Histidine is Present at the Heme Iron SiteReduces Affinity to CO, but Does Not Eliminate itCarbon Monoxide in Cigarette SmokeNote That CO2 Does Not Bind to Heme, nor do Protons

Hemoglobin and the Movement of Oxygen• Fetal Hemoglobin

The Body Makes Different Globins Over TimeMost Variations Centered on BirthFetal Hemoglobin Mostly α2γ2

High Most of Life

Highest in Fetus

High Most of Life

Highest in Fetus At Adult Levels by 24 Weeks

Increasing Affinity

Fetal Hemoglobin Can’t Bind to 2,3 BPG Mostly Remains in R-state

Hemoglobin and the Movement of Oxygen• Sickle Cell Anemia

Sickle Cell Anemia is a Genetic Disease Affecting HemoglobinMultiple Forms - Mutation of Glu to Val at Position #6 Most CommonRed Blood Cells Lose Rounded Shape and Form Sickles

Sickle Cell Anemia is a Genetic Disease Affecting HemoglobinMultiple Forms - Mutation of Glu to Val at Position #6 Most CommonRed Blood Cells Lose Rounded Shape and Form SicklesShape Change Happens in Low O2 Conditions - Exercise

Sickle Cell Anemia is a Genetic Disease Affecting HemoglobinMultiple Forms - Mutation of Glu to Val at Position #6 Most CommonRed Blood Cells Lose Rounded Shape and Form SicklesShape Change Happens in Low O2 Conditions - ExerciseChange Caused by Polymerization of Hemoglobin

Sickled Cells

Rounded Cells Move Easily Through Capillaries

Sickled Cells Get Stuck

Sickled Cells Get StuckSickled Cells Removed by Spleen

Why is Sickle Cell Anemia so Widespread?Why Has it Not Been Selected Against?

Greatest Incidence of Sickle Cell Anemia

Greatest Incidence of MalariaGreatest Incidence of Sickle Cell Anemia

Benefit of Sickle Cell Mutation for Heterozygotes No Benefit to Homozygous Recessive or Dominant

Hemoglobin and the Movement of Oxygen• Summary

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different Functions

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of Each

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s Shape

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-state

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 Better

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 Release

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 ReleaseThe Bohr Effect Explains How Oxygen and CO2 Exchanged in Lungs

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 ReleaseThe Bohr Effect Explains How Oxygen and CO2 Exchanged in Lungs2,3 BPG is Produced by Rapidly Metabolizing Cells. It too Favors O2 Release

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 ReleaseThe Bohr Effect Explains How Oxygen and CO2 Exchanged in Lungs2,3 BPG is Produced by Rapidly Metabolizing Cells. It too Favors O2 ReleaseFetal Hemoglobin Can’t Bind 2,3 BPG and has Greater O2 Affinity Than Adult Hemoglobin

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 ReleaseThe Bohr Effect Explains How Oxygen and CO2 Exchanged in Lungs2,3 BPG is Produced by Rapidly Metabolizing Cells. It too Favors O2 ReleaseFetal Hemoglobin Can’t Bind 2,3 BPG and has Greater O2 Affinity Than Adult HemoglobinSickle Cell Anemia (SCA) is a Genetic Disease of Hemoglobin

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 ReleaseThe Bohr Effect Explains How Oxygen and CO2 Exchanged in Lungs2,3 BPG is Produced by Rapidly Metabolizing Cells. It too Favors O2 ReleaseFetal Hemoglobin Can’t Bind 2,3 BPG and has Greater O2 Affinity Than Adult HemoglobinSickle Cell Anemia (SCA) is a Genetic Disease of HemoglobinIn Low O2 Concentration, Red Blood Cells of SCA Sufferers Form Sickle Shapes

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 ReleaseThe Bohr Effect Explains How Oxygen and CO2 Exchanged in Lungs2,3 BPG is Produced by Rapidly Metabolizing Cells. It too Favors O2 ReleaseFetal Hemoglobin Can’t Bind 2,3 BPG and has Greater O2 Affinity Than Adult HemoglobinSickle Cell Anemia (SCA) is a Genetic Disease of HemoglobinIn Low O2 Concentration, Red Blood Cells of SCA Sufferers Form Sickle ShapesSickled Cells Stick in Capillaries and Can be Fatal

Animals Have Widely Varying O2 NeedsATP Generated Much More Efficiently in Presence of O2Hemoglobin and Myoglobin are Related, but Have Different FunctionsHemoglobin has Four Subunits and Hemes. Myoglobin has One of EachBind of O2 by Heme’s Iron Pulls up on a Histidine and Change’s Hemoglobin’s ShapeChanging Hemoglobin’s Shape Converts Hemoglobin from T-state to R-stateR-state Binds Oxygen Better. T-state Releases O2 BetterIn the Bohr Effect, Binding of CO2 and H+ Favors O2 ReleaseThe Bohr Effect Explains How Oxygen and CO2 Exchanged in Lungs2,3 BPG is Produced by Rapidly Metabolizing Cells. It too Favors O2 ReleaseFetal Hemoglobin Can’t Bind 2,3 BPG and has Greater O2 Affinity Than Adult HemoglobinSickle Cell Anemia (SCA) is a Genetic Disease of HemoglobinIn Low O2 Concentration, Red Blood Cells of SCA Sufferers Form Sickle ShapesSickled Cells Stick in Capillaries and Can be FatalPeople Heterozygous for the Mutated Gene Survive Malaria Better Than Others

Protein Structure

Primary -‐ Sequence of amino acidSecondary -‐ Interaction of amino acids close in primary sequenceTertiary -‐ Interaction of amino acids distantly located

Protein Structure

Primary -‐ Sequence of amino acidSecondary -‐ Interaction of amino acids close in primary sequenceTertiary -‐ Interaction of amino acids distantly locatedQuaternary -‐ Interaction of protein subunits

Protein Structure

Metabolic Melody

Oh isn't it greatWhat proteins can do

Especially ones that bind to O2Hemoglobin's moving around

Inside of the lungs It picks up the bait

And changes itself from T to R state Hemoglobin's moving around

The proto-porphyrin system Its iron makes such a scene Arising when an O2 binds

Pulling up on histidine

The binding occurs Cooperatively

Thanks to changes qua-ter-nar-y Hemoglobin's moving around

It exits the lungs Engorged with O2

In search of a working body tissue Hemoglobin's moving around

Hemoglobin's Moving Around (To the tune of "Santa Claus is Coming to Town")

Oh isn't it greatWhat proteins can do

Especially ones that bind to O2Hemoglobin's moving around

Inside of the lungs It picks up the bait

And changes itself from T to R state Hemoglobin's moving around

The proto-porphyrin system Its iron makes such a scene Arising when an O2 binds

Pulling up on histidine

The binding occurs Cooperatively

Thanks to changes qua-ter-nar-y Hemoglobin's moving around

It exits the lungs Engorged with O2

In search of a working body tissue Hemoglobin's moving around

Hemoglobin's Moving Around (To the tune of "Santa Claus is Coming to Town")

The proton concentration Is high and has a role

Between the alpha betas It finds imidazole

To empty their loads The globins decree

"We need to bind 2,3BPG" Hemoglobin's moving around

The stage is thus setFor grabbing a few

Cellular dumps of CO2Hemoglobin's moving around

And then inside the lungs it Discovers ox-y-gen

And dumps the CO2 off To start all o'er again

So see how this works You better expect

To have to describe the Bohr effect Hemoglobin's moving around

Metabolic Melody

The Bloody Things(To the tune of “Coke ® It's The Real Thing”)

I’m gonna put some oxygensbeside my porphyrin rings

To nudge the irons up a notchand yank on histidines

The globins’ shapes will change a bit,oh what a sight to see

The way they bind to oxygenco-op-er-AH-tive-ly

And as I exit from the lungsto swim in the bloodstreamMetabolizing cells they allexpress their needs to meTo them I give up oxygenand change from R to T

While my amines, they hang ontothe protons readily

I’m gonna put some oxygensbeside my porphyrin rings

To nudge the irons up a notchand yank on histidines

The globins’ shapes will change a bit,oh what a sight to see

The way they bind to oxygenco-op-er-AH-tive-ly

And as I exit from the lungsto swim in the bloodstreamMetabolizing cells they allexpress their needs to meTo them I give up oxygenand change from R to T

While my amines, they hang ontothe protons readily

But that's not all the tricks I know,there's more that’s up my sleeve

Like gaps between sub-U-nits thathold 2,3-BPG

When near met-a-bo-LI-zing cells,I bind things that diffuse

The protons and bicarbonatesfrom lowly cee oh twos

CHORUS

That’s the way it isWhen your cells are at play

Go say hip hip hoorayFor the bloody things

HemoglobinandtheMovementof*Oxygenoregonstate.edu/instruct/bb450/450material/Keynotes... ·...

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Hemoglobin*and*the*Movement*of*Oxygenoregonstate.edu/instruct/bb450/450material/Keynotes... ·...

HemoglobinandtheMovementof*Oxygenoregonstate.edu/instruct/bb450/450material/Keynotes... ·...