Transport Oxygen

Oxygen
Sel atau jaringan: butuh O2 untuk
metabolisme
Hemoglobin & myoglobin :
transporter
O2 kurang : Hypoxia atau anoxia
Mutasi struktur Hb and myoglobin :
sickle cell, thalassemia.

O2 CO2

OXYGEN
Sedikit larut dalam air: 3.2 mL O2 /1 L
blood plasma
Transporter: protein
hemoglobin (erytrocyte)
Myoglobin (muscle)

Tissue: oxidative metabolism

Electron acceptor
Molecular oxygen : oxidize metal ions,
Iron-containing enzymes dan protein :
iron, Fe(II) atau Fe(I) .
Fe(III) tidak berfungsi

Hemoglobin (Hb)
Empat Heme + Globin
Heme: porfirin dengan 4 bh cincin pirol dan 1
Fe
porphyrin ring : Fe dan globin
Oxygen terikat dengan Fe ( fero)
Hemoglobin (HHgb) basa lemah (K = 1.4 x 10 ; pKa
= 7.85). Oxyhemoglobin (HHgbO 2) asam
lemah
-8

(K = 2.5 x 10-7; pKa = 6.6)

Hb diatur oleh H+ dan CO2

Hemogl...

Hemogl...
Tetramers: pairs of two different
polypeptide subunits
2b2 (HbA; normal adult hemoglobin)
22 (HbF; fetal hemoglobin)
2bS2 (HbS; sickle cell hemoglobin)
22 (HbA2; a minor adult hemoglobin).

Heme

methyl (M)
vinyl (V)
(Pr)
propionate

Heme

Heme..

Oxyhemoglobin Deoxyhemoglobin

Pertukaran O2 CO2
Jaringan

Chliride shift

Pertukaran CO2 O2 Alveoli

Hb O2
Fe moves in plane,
pulling proximal His
and Helix F

T state (tense) and R state (relaxed) represent two

different conformations of the tetramer
Both bind O2 but R state binds it more strongly

Oxygenation hemoglobin: iron atom

moves into the plane of the heme
1 molecule Hb can
bind 4 molecules of O2
(Heme) and 1
molecule of CO2
(globin)
100 ml of blood has
about 15 gr of Hb, at
Hct = 0.45
Each gram of Hb can
store about 1.34 ml of
O2

Dissosiasi OksiHb
,
1. Suhu : afiinitas O2-Hb

2. pH : afiinitas O2-Hb

3. CO2 : afiinitas O2-Hb

Suhu- saturasi o2

Bohr Effect
Competition between oxygen and H+
Effect of pH and CO2 on the binding
and release of oxygen to Hb
Discovered by Christian Bohr
Binding of protons diminishes
dioxygen binding

Haemoglobin Saturation at High

Values
Permukaan laut : PO2 (100mmHg)
haemoglobin : 98% SATURATED
PO2 < permukaan laut : Afinitas O2Hb saturasi dipertahankan
Tempat tinggi: PO2 (80mmHg),
haemoglobin 95% saturated

2,3,-DPG (2,3-diphosphoglycerate)

Glikolisis an-aerob
Afinitas O2-Hb berkurang
Hemoglobin tetramer mengikat satu BPG
BPG stabilizes deoxygenated hemoglobin:
BPG , afinitas dg O2 sehingga O2 jaringan
Adaptasi High Altitude : Erytrosit (Hb )
Fetal Hb - lower affinity for 2,3-BPG, higher
affinity for oxygen, so it can get dioxygen from
mother

DPG..
Chronic hypoxia :
increase 2,3-DPG in
RBCs
2,3-DPG affinity O2 for
hemoglobin < : this
shifts the curve to the
right.

DPG..

Carbon Monoxide (CO)

Berikatan dengan O2 pada tempat
yang sama
Affinitas: 200 X O2

PCO >0.4 mmHg ; lethal.

Transport CO2
Larut dlm plasma (7 10%, )
Ion bicarbonat:
CO2+ H20 H2CO3 HCO3 + H ion

Berikatan dengan haemoglobin:

Carbaminohemoglobin / Hemoglobin
carbamates :15% of the CO2 in venous
blood.
>> CO2 : bicarbonate, (eritrocyte), hidrasi
CO2 menjadi (H2CO3), dibantu carbonic
anhydrase.
.

Transport..
CO2 + Hb

HbCO2

Hypoxia

This is Fatal

Methemoglobin
Fe heme : feri (+3)
O2 tidak bisa diikat
Enzyme methemoglobin reductase :
merubah ion Feri menjadi Fero

Methemoglobin
Oxidation of iron within heme from
Fe2+ to Fe 3+

Met Hb
Autooxidation of Hb
0.5 - 3% Hb converted to MHb each
day

Autoreduction of MHb
99% occurs via NADH-dependent
cytochrome b5 reductase (b5r)
pathway
Ascorbic acid, glutathione minor role
in reduction
Conversion of MHb to Hb is 15% per

Myoglobin
Mb + O2 --- MbO2
Each myoglobin : capable of binding
one oxygen (one heme per molecule)
. with the oxygen in solution.
The titration curve of myoglobin with
oxygen is a hyperbola

Hemoglobin - Myoglobin
Beda pada quaternary structure.
Hemoglobin : tetramer (2 )
Myoglobin : monomer (quaternary
structure tidak ada).
Myoglobin - oxygen lebih kuat dari
Hb
Perpindahan Oxygen sirkulasi ke cell
lebih mudah

myoglobin

Hb sigmoidal (S-shaped
curve)
This permits the blood to
deliver much more O2 to
the tissue than if Hb had a
hyperbolic curve with the
same P50

BIOMEDICAL IMPLICATIONS

Hemoglobinopathy: mutasi
Myoglobinuria : infark myocard
Anemia : jumlah Hb <
Thalassemia : genetic defect
(absence or b chains)
Glycated Hemoglobin (HbA1c):
glucose glycates the-amino group of
lysyl residues.

Referensi
MURRAY, R. K., BENDER, D. A., BOTHAM, K. M., J, P.,
KENNELLY, RODWELL, V. W. & WEIL, P. A. (2009) Harpers
Illustrated Biochemistry, The McGraw-Hill Companies, Inc
VOET, D., G.VOET, J. & PRATT, C. W. (2008) FUNDAMENTALS
OF Biochemistry :LIFE AT THE MOLECULAR LEVEL, John
Wiley & Sons, Inc.
KOOLMAN, J. & ROEHM, K.-H. (2005) Color Atlas of
Biochemistry, New York, Thieme.
JAIN, J. L., JAIN, S. & JAIN, N. (2005) FUNDAMENTALS OF
BIOCHEMISTRY, NEW DELHI, S. CHAND & COMPANY LTD.
Rodwell Victor W. Bender D. A. Botham K. M. Kennelly P. J.
Anthony W P. (2015) Harpers Illustrated Biochemistry, The
McGraw-Hill Companies, Inc
Michal Gerhard and Dietmar Schomburg (ed), 2012,
Biochemical Pathways: An Atlas of Biochemistry and
Molecular Biology, Second Edition, John Wiley & Sons, Inc.