Hemo
my G
Losin
of Enzymes They do
Hemoglory mod myoglobm
of A
Hemoglormot myogloss mo
The
R oles : Are Lower TS REACTron
Energy
we . Not
- OBIN RESPONSIBLE FOR FROM
G
Hemog
of Or TRANSPORT Of
O
THERROLES Are & THE THE
Storage
The Transport
LWGS
No COBA S O2 To
THE TISSUES AS WELL AS THE REMOVAL Of CO2 FROM My Resides THE TISSUES And ACTS As A
STORAGE PROJEN
TISSUES LOBM In
og
.
Cz
CH3
T~
enJJ HEME AS A COFACTOR : Order
·-
MANY PROTEMS REQUIREAdd row CHEMICAL ROS I
s g
To
CHz
-
C& ! -
&
I- %
-
7 S &G
2 3
-
&
- - HzC
yIY Z&( CoFACTORS ARE NON-PROTEM Compounds
-
For crow
2
T
't S
O E for
Required
· -
2)
THA Are
prote
~ 2
S
2
-
.
-
[I
Fe
-
N
v·
-
>
-
z.B
·
-
& C
23
·
K⑮
(
5 7
-
Error
2
of-X &
C THEY BE OR
ORGANI
COMPLEX MORECULES
MORGANIC
CAN METAL FONS
- I
2 .
% ..
1
>
Y
-
&O
↳I /
~...
23 &jJ& -
-
Y& C 8
S S
d&
-yY
HEME
THEY Car BE ASSOCIATED
Tightly TRAnsiently
ig
OR ACTS
gE-
CALLED
J Coenzymes
-
- . .
CH3
O -
I
HzS
-b
-
a
&
& 12 I
I
-
T
* &
Y
Y#&
&
·
-
↳ :
cofactor for
40S 8z &I& J Hemoglobm Myogasm
&
As Bot & ALMOST
TIgLy iRREVERSBBly
a
VERY
. d
C M S
C
2 ,
LG&
- .
& -
S E
S
-
S
& S
8 & I &
Borned (prosthetic HEMER
Group) Meag organic
A
If .
Coenzyme Is -
OH
& g O
Off O
STRUCTURE of Here : WHEN Felt is n o t Bound, M
myoglossme Hemogcosmo
- known HEME
As
protoporphyrin .
N S
only Once
Fet Has Bored Farture Heme
. to
properly SynthestE can
HETERGETRAMER ; And I BSUBUNDS (porphyria) Additon
·
MONOMERR RESULT no Vampires & WEREWOLVES
·
2X .
in
HighAffinery for O2 Lower
Affrmy for O2
· ·
WAffECTED PH, And
By PH 2 , 3-BPG SenstNE To CO2 BPG ComECTron To THE 4 HEME
·
CO, To MS Also is
neRogers
,
or ·
, ,
M
·
DOES NOT Bid BPG ·
Birds 4 O MOLECUTES
found
m Blood STABREED Brods
Ugand
His F8 And His E7 THE Or
By
·
no
TISSUES ·
.
Acids Are
Myoghosm
27 Amino THE SAME As
153 Acids only
·
·
Amino
·
77 % HELICAL
·
Enter Fully 14 Bound) BETWEEN Felt And His
Oxygenated
x Of or E7
.
·
8 & HELICES
ExtError Resides BOTH POLArt NONPOLAR Bound)
·
(no 02
Empty
Fet =
REDUCED
Febt =
OxidED
T Low
Mechanics of O2
Bindmy zog
HEME : of 2 On R= ACOSTERR EffECTORS
Binding
To morecues induces a such from H BNOS O2 WEARLY &
7 st re To rstre .
: HEME
REVERSUBLY COMPARED To Co
for HaS And CN These Are all Very Toxic
BeautyBlockBmdte
Bid,
HIGHER Affroty T(deoxy) State
THER AKA STATE HAS O2 Than WHE THE TWO Or Molecules
OXY The .
,
·
HETEROTROPIC NEGAINE EFFECTORS
Posne Effector !
ford ! DAN T EffECTORS of BPG of COz
AFFINERY O LOWER PH , And AccumATron
REMAMENG
THE MICREASES THE SuBrS As revel as 100 Stres NCLUDE All
PRESENCE ,
.
diffemby 150 from G , B, B2 from TTOR The of
These Are Effectors WHICH decrease Affrry They ALL STABrtE
TOGETHERA Megane
-
To To Submers
gET
C, . , CLOSER A r row Of .
felt
BANG Brody
Induces STRUCTURAL O2 THE THE T-STATE
CHANGES
THE CENTRAL OF THE HEME Wro
Group
TO
CAUY
Irgand
, -
Homeropre Effector-SAME
, ,
Substance as
LIES Outside of THE PLANE of THE HEME WHEN Of Brds , THE POLR Bond PULS Some of Feete-TOWAd THE MORE
LgONd
.
HETEROTROPRC EFFECTOR DIFFERENT SUBSTANCE
-
THEN
Effectunde
The ELECTROw Crowd of Felt fre
Bisphosphoglycerate Hemoglobi
2 3-
O
EFFECTRELY SARMORIG
Allowing
The makes
ELECTRONEGANE a
, ,
a to no the
plante , : More
of This Structural Affects THE OTHER Submers BPG feTR
drenyPregnancy
HAS Lower
the
H eme .
Change ProECTly , O un TISSUES . LEVELS ARE ElentED WHE
Hemoglobi
Affrry for MOTHER'S AfRMY FOR COMPAREd
HEMOGLOBM
BPG THOS THE A LOWER O WHEN
GNES
.
A *
SAL-T
La PH And Or
Affrry By IsaLtBridges of The Depends feral facilitates THE Transfer of From fetht
Hemoglobm
This
Bridges
: 7 Stre Is StaBratED .
One SaLy To .
O2 MATERIAL RBCs To
(SHJ Fetal Fetal Has an
US HIGH) Hemoglobno
HIS 146 HIS 146S PROTOMMED AND T roses
Hemoglobm
WHEN PHIS LOW also alts as X,
PROTONED
BENG
Or SO SINTE S STABMAE)
storage y,
. .
.
HCOntHt Conversely Bod DiffERENCE BSUBmNS
High Hemoglobi AKEY
RECALL 202tH0 When Phas is STMULATED To More Or Al Low pOr & CHAMS is THAT THE Ifis 143 on is SuSIMM
.
, ,
[Jz .
from
HYGENERATED By Bruding Reduci
WHME MOST of THE CO2
Charges
of The HCOn- Wi a Serve This Removes BPG
Hemaghorn pastne
Much THE iS Taken She ,
CO2 To up By 7 STE i n TISSUES . .
produced Bond for BPG
no THE TISSUES is CARRIED To THE
Lung
n The form of HCOs. Bus, some Con can
Contently to The
afferty [ His
Say THAT 10 TIMES FAST!
- TERMAS
N of EACH
Hemoglob supers to form
CARBAMAOHEMOGLOBA
.
THIS RAN PRODUCES H AS WELL . THE
VEGANELY NOTE BPG's
marry -p
CHARGED
CARBEMAE CAN FORM SALT
BRIDGES L
POSTINELY
CHARGED
STECHAMS On
HEMOGLABM ,
FURTHER
STABMAAOGY
STATE
vegame areages 0- [ His
> -
DECREASE IN Of AffrMY DUE TO INCREASE In CO2 & He is CALLED THE BOAR Effect ,
Lys
0
-
S His
P
Sickle
GENE EncodingHemoglo
CELL ANEMA : An Autosomal RECESSE MEXASTON N WHICH THE B CHAMS SUBSTrues a
Smughe - His
for Ver detrimental
negrinely Charged
62U6 . This is Because The Glu side Chamous WHE L is morpolar THES . CAUSES THE B CAS N THE
form FABRES
Long Becoming
I State THAT RESULT In THE RBCs STRETCHED & SreKLE SHAPED To
TOGETHERA
To Strk NO BPG = No
O2
TISSUEs & Too much
Hydrophore VAL PSe CO2
Resurtngm
Eri
HyperCapric Acidosis
=>
HydropHOBr PHEd LEr
my G
Losin
of Enzymes They do
Hemoglory mod myoglobm
of A
Hemoglormot myogloss mo
The
R oles : Are Lower TS REACTron
Energy
we . Not
- OBIN RESPONSIBLE FOR FROM
G
Hemog
of Or TRANSPORT Of
O
THERROLES Are & THE THE
Storage
The Transport
LWGS
No COBA S O2 To
THE TISSUES AS WELL AS THE REMOVAL Of CO2 FROM My Resides THE TISSUES And ACTS As A
STORAGE PROJEN
TISSUES LOBM In
og
.
Cz
CH3
T~
enJJ HEME AS A COFACTOR : Order
·-
MANY PROTEMS REQUIREAdd row CHEMICAL ROS I
s g
To
CHz
-
C& ! -
&
I- %
-
7 S &G
2 3
-
&
- - HzC
yIY Z&( CoFACTORS ARE NON-PROTEM Compounds
-
For crow
2
T
't S
O E for
Required
· -
2)
THA Are
prote
~ 2
S
2
-
.
-
[I
Fe
-
N
v·
-
>
-
z.B
·
-
& C
23
·
K⑮
(
5 7
-
Error
2
of-X &
C THEY BE OR
ORGANI
COMPLEX MORECULES
MORGANIC
CAN METAL FONS
- I
2 .
% ..
1
>
Y
-
&O
↳I /
~...
23 &jJ& -
-
Y& C 8
S S
d&
-yY
HEME
THEY Car BE ASSOCIATED
Tightly TRAnsiently
ig
OR ACTS
gE-
CALLED
J Coenzymes
-
- . .
CH3
O -
I
HzS
-b
-
a
&
& 12 I
I
-
T
* &
Y
Y#&
&
·
-
↳ :
cofactor for
40S 8z &I& J Hemoglobm Myogasm
&
As Bot & ALMOST
TIgLy iRREVERSBBly
a
VERY
. d
C M S
C
2 ,
LG&
- .
& -
S E
S
-
S
& S
8 & I &
Borned (prosthetic HEMER
Group) Meag organic
A
If .
Coenzyme Is -
OH
& g O
Off O
STRUCTURE of Here : WHEN Felt is n o t Bound, M
myoglossme Hemogcosmo
- known HEME
As
protoporphyrin .
N S
only Once
Fet Has Bored Farture Heme
. to
properly SynthestE can
HETERGETRAMER ; And I BSUBUNDS (porphyria) Additon
·
MONOMERR RESULT no Vampires & WEREWOLVES
·
2X .
in
HighAffinery for O2 Lower
Affrmy for O2
· ·
WAffECTED PH, And
By PH 2 , 3-BPG SenstNE To CO2 BPG ComECTron To THE 4 HEME
·
CO, To MS Also is
neRogers
,
or ·
, ,
M
·
DOES NOT Bid BPG ·
Birds 4 O MOLECUTES
found
m Blood STABREED Brods
Ugand
His F8 And His E7 THE Or
By
·
no
TISSUES ·
.
Acids Are
Myoghosm
27 Amino THE SAME As
153 Acids only
·
·
Amino
·
77 % HELICAL
·
Enter Fully 14 Bound) BETWEEN Felt And His
Oxygenated
x Of or E7
.
·
8 & HELICES
ExtError Resides BOTH POLArt NONPOLAR Bound)
·
(no 02
Empty
Fet =
REDUCED
Febt =
OxidED
T Low
Mechanics of O2
Bindmy zog
HEME : of 2 On R= ACOSTERR EffECTORS
Binding
To morecues induces a such from H BNOS O2 WEARLY &
7 st re To rstre .
: HEME
REVERSUBLY COMPARED To Co
for HaS And CN These Are all Very Toxic
BeautyBlockBmdte
Bid,
HIGHER Affroty T(deoxy) State
THER AKA STATE HAS O2 Than WHE THE TWO Or Molecules
OXY The .
,
·
HETEROTROPIC NEGAINE EFFECTORS
Posne Effector !
ford ! DAN T EffECTORS of BPG of COz
AFFINERY O LOWER PH , And AccumATron
REMAMENG
THE MICREASES THE SuBrS As revel as 100 Stres NCLUDE All
PRESENCE ,
.
diffemby 150 from G , B, B2 from TTOR The of
These Are Effectors WHICH decrease Affrry They ALL STABrtE
TOGETHERA Megane
-
To To Submers
gET
C, . , CLOSER A r row Of .
felt
BANG Brody
Induces STRUCTURAL O2 THE THE T-STATE
CHANGES
THE CENTRAL OF THE HEME Wro
Group
TO
CAUY
Irgand
, -
Homeropre Effector-SAME
, ,
Substance as
LIES Outside of THE PLANE of THE HEME WHEN Of Brds , THE POLR Bond PULS Some of Feete-TOWAd THE MORE
LgONd
.
HETEROTROPRC EFFECTOR DIFFERENT SUBSTANCE
-
THEN
Effectunde
The ELECTROw Crowd of Felt fre
Bisphosphoglycerate Hemoglobi
2 3-
O
EFFECTRELY SARMORIG
Allowing
The makes
ELECTRONEGANE a
, ,
a to no the
plante , : More
of This Structural Affects THE OTHER Submers BPG feTR
drenyPregnancy
HAS Lower
the
H eme .
Change ProECTly , O un TISSUES . LEVELS ARE ElentED WHE
Hemoglobi
Affrry for MOTHER'S AfRMY FOR COMPAREd
HEMOGLOBM
BPG THOS THE A LOWER O WHEN
GNES
.
A *
SAL-T
La PH And Or
Affrry By IsaLtBridges of The Depends feral facilitates THE Transfer of From fetht
Hemoglobm
This
Bridges
: 7 Stre Is StaBratED .
One SaLy To .
O2 MATERIAL RBCs To
(SHJ Fetal Fetal Has an
US HIGH) Hemoglobno
HIS 146 HIS 146S PROTOMMED AND T roses
Hemoglobm
WHEN PHIS LOW also alts as X,
PROTONED
BENG
Or SO SINTE S STABMAE)
storage y,
. .
.
HCOntHt Conversely Bod DiffERENCE BSUBmNS
High Hemoglobi AKEY
RECALL 202tH0 When Phas is STMULATED To More Or Al Low pOr & CHAMS is THAT THE Ifis 143 on is SuSIMM
.
, ,
[Jz .
from
HYGENERATED By Bruding Reduci
WHME MOST of THE CO2
Charges
of The HCOn- Wi a Serve This Removes BPG
Hemaghorn pastne
Much THE iS Taken She ,
CO2 To up By 7 STE i n TISSUES . .
produced Bond for BPG
no THE TISSUES is CARRIED To THE
Lung
n The form of HCOs. Bus, some Con can
Contently to The
afferty [ His
Say THAT 10 TIMES FAST!
- TERMAS
N of EACH
Hemoglob supers to form
CARBAMAOHEMOGLOBA
.
THIS RAN PRODUCES H AS WELL . THE
VEGANELY NOTE BPG's
marry -p
CHARGED
CARBEMAE CAN FORM SALT
BRIDGES L
POSTINELY
CHARGED
STECHAMS On
HEMOGLABM ,
FURTHER
STABMAAOGY
STATE
vegame areages 0- [ His
> -
DECREASE IN Of AffrMY DUE TO INCREASE In CO2 & He is CALLED THE BOAR Effect ,
Lys
0
-
S His
P
Sickle
GENE EncodingHemoglo
CELL ANEMA : An Autosomal RECESSE MEXASTON N WHICH THE B CHAMS SUBSTrues a
Smughe - His
for Ver detrimental
negrinely Charged
62U6 . This is Because The Glu side Chamous WHE L is morpolar THES . CAUSES THE B CAS N THE
form FABRES
Long Becoming
I State THAT RESULT In THE RBCs STRETCHED & SreKLE SHAPED To
TOGETHERA
To Strk NO BPG = No
O2
TISSUEs & Too much
Hydrophore VAL PSe CO2
Resurtngm
Eri
HyperCapric Acidosis
=>
HydropHOBr PHEd LEr
