Dioxygen Transport
Transcript of Dioxygen Transport
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Dr. Shubhra Bikash MaityDepartment of ChemistryCV Raman Global University
Bioinorganic Chemistry
Dioxygen Transport
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Structures of Amino Acids
H2N COOH
H
H2N COOH
CH3
H2N COOH H2N COOH H2N COOH
HOH OH SH
H2N COOH H2N COOH H2N COOH H2N COOH
H2N COOHH2N COOH H2N COOH H2N COOH H2N COOH
H2N COOH H2N COOH H2N COOH H2N COOH H2N COOH
S
NH
COOH
OHNH
OH
OOHO
NH2
OO NH2
NHHN
NH3
NH
NH2H2N
Glycine (Gly) G Alanine (Ala) A Serine (Ser) S Threonine, Thr (T) Cysteine (Cys) C
Small Nucleophile
Hydrophobic
Aromatic Acidic
Amide Basic
Phenylalanine (Phe) F Tyrosine (Tyr) Y Tryptophan (Trp) W Aspartic Acid (Asp) D Glutamic Acid (Glu) E
Valine (Val) V Leucine (Leu) L Isoleucine (Ile) I Methionine (Met) M Proline (Pro) P
Asparagine (Asn) N Glutamine (Gln) Q Histidine (His) H Lysine (Lys) K Arginine (Arg) R
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The Primary Structure of a Protein
Primary Protein Structure: Sequence of a chain of amino acids
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The Secondary Structure of a Proteins
Hydrogen bonds can form betweennearby amino and carbonyl groupson the same polypeptide chain.
Left: an �-helix (alpha-helix), in which the polypeptide’s backbone is coiledRight: a �-pleated sheet (beta-pleated sheet), in which segments of a peptide chain bend 180° and then fold in the same plane
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Tertiary & Quaternary Structure of Proteins
Interactions that determinethe tertiary structure ofproteins
TERTIARY STRUCTURES
QUATERNARY STRUCTURES
The Cro protein is a dimer—it consists of twoidentical polypeptide subunits
Hemoglobin is a tetramer—it consists of four polypeptide subunits. two identical α subunits and
two identical β subunits
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Summary: Protein Structure
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NON-PROTEINSPROTEINS
ELECTRON TRANSPORT
DIOXYGEN MANAGEMENT
METAL MANAGEMENT
PHOTOREDOX
METAL STORAGE & TRANSFER
Iron-sulfur (Fe), Blue copper (Cu),& Cytochromes (Fe)
Hemoglobin (Fe), Myoglobin (Fe), Hemocyanin (Cu), & Hemerythrin (Fe)
Ferritin (Fe), Transferrin (Fe),& Ceruloplasmin (Cu)
MetalloenzymesTRANSPORT & STORAGE
HydrolasesePhosphatases (Mg, Zn, Cu)Aminopeptidases (Mg, Zn)Carboxypeptidases (Zn)
Oxidoreductases
Oxidases (Fe, Cu), Reductases (Fe, Cu, Mo)Superoxide dismutases (Cu, Zn, Mn)
Isomerases and synthetases
Vitamin B12 coenzyme (Co)
Transferases Kinases (Mg)
METALLOBIOMOLECULES
Lyases
Lygases Glutamin synthetase (Mg, Mn)
Enolases (Mg)
Chlorophyll (Mg)
Siderophores (Fe)
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Porphyrin and Metalloporphyrin22π electrons but only 18 are delocalized (n= 4 in Hückel’s rule)
Hans Fischer (1881-1945)Nobel Prize in Chemistry (1930)
NH
NH HN
HN NH
N HN
N
Porphyrinogens Porphyrins/Porphinshighly colored
(purple)Colorless
Pyrrole ring
h O2N
N N
N
Mn+
Metalloporphyrins
Mn+
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NH
N HN
NA B
CD
1
2 3
4
567
8
2.05
How to draw Porphyrin molecule??
NH
NH HN
HN
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Hemoglobin: A Protein that transports O2 to all organs of the body though blood
Oxygen Carrying & Storage Proteins….
Heme
Myoglobin: A Protein thatstores O2
PDB ID: 1GZX PDB ID: 3RGK
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Some Properties of Oxygen Carrying Proteins
Property Myoglobin (Mb) Hemoglobin (Hb)
Metal Fe Fe
Oxidation state of metal in deoxyprotein
(II) (II)
Metal:O2 Fe:O2 Fe:O2
Oxidation state of metal in oxy protein
(III) (III)
Color, deoxy state Red-purple Red-purple
Color, oxy state Red Red
Environment around Metal centre Porphyrin ring Porphyrin ring
Molecular weight (Da) 17,100 65,000
Number of subunit(s) 1 (α = 161 residues) 4 (2α + 2: α = 141 residues& = 146 residues)
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Deoxy-Hb/Mb Oxy-Hb/Mb
Oxygen Binding Changes the Position of Iron Ion in Hb/Mb
High spin Fe(II) Low spin Fe(III)
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Dioxygen and its Reduced Species
Species νO-O (cm-1) dO-O (Å)
O2+ 1905 1.12
O2 1580 1.21
O2- 1097 1.33
O22- 802 1.49
From resonance Raman spectroscopy the O-O stretch in oxy-Mb is measured to be ̴1105 cm-1. The protein is also diamagnetic (d5, FeIII and O2
- couple)
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Oxygen Binding to Hb: Statistical Probability
Musical Chair!!
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Oxygen Binding to Hb: In RealityIn reality the successive O2 binding constants of Hb gradually increases, i.e.K1 < K2 < K3 < K4 . This is due to cooperative binding of O2 with Hb.
This happens like chain and pulley. Thepulling of the proximal histidine alongwith the activity of Fe getting into theplane of the porphyrin triggers thisactivity
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Cooperativity in O2 Binding & Release in Hb
Oxygen binds to one Hb sub-unit
Fe(II) contracts & moves into plane of porphyrin ring
Moves the histidineattached to it
Triggers conformational changes in the globin chain
Translated through H-bond network
Enhances the ability of other three units to bind O2
NB: Due to MONOMERIC in nature Mb does not possess such cooperative interactions.
In a similar way when blood reaches the muscle, only one O2 is released , the others arereleased even more easily due to the cooperative effect in reverse way.
The Phenomenon is called Cooperative Effect
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O2 Affinity of Mb & Hb: Hill PlotDue to monomeric in nature & absence of cooperative interaction Mb takes up O2 in
1:1 ratio. The equilibrium expression is therefore expressed as
On the other hand due to tetrameric nature & cooperative interaction oxygenation of Hb may be expressed as
Fraction (f) of Mb & Hb oxygenated could be expressed as
Similarly for Hb -
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Which gives the Hill equation for oxygenation of Mb and Hb respectively -
O2 Affinity of Mb & Hb: Hill Plot
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O2 Binding Curve: Effect of Cooperativity
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Effect of pH on Oxygenation of Hb/Mb
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Oxygenation of Hb becomes pH dependent: Bohr Effect
Christian Bohr, father of Niels Bohr discoveredthis effect. An increase in concentration ofprotons and/or carbon dioxide will reduce theoxygen affinity of hemoglobin
The chemical basis for the Bohr effect is due tothe formation of two salt bridges of thequaternary structure. One of the salt bridges isformed by the interaction between Histidine 146and Lysine 40. This connection will help to orientthe histidine residue to also interact in anothersalt bridge formation with the negatively chargedaspartate 94. The second bridge is formed withthe aid of an additional proton on the histidineresidue.
Below a pH of 6, theimidazole ring ofhistidine is mostlyprotonated thusfavoring salt bridgeformation
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Role of Hb & Mb in O2 & CO2 transport
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Role of Hb & Mb in O2 & CO2 transport
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2, 3 biphospho glycerate (BPG)
2,3- Biphosphoglycerate
The organic compound 2, 3 biphospho glycerate (BPG) binds to hemoglobin Aand reduces its O2 affinity by a factor of 26. This at the first instance will makeone wonder why? Interestingly, this increases the oxygen-binding affinity of fetalhemoglobin (Hb-F) relative to that of maternal (Hb-A) hemoglobin. Thisdifference in oxygen affinity allows oxygen to be effectively transferred frommaternal to fetal red cells, the transport of oxygen from mother to fetus.
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Hemoglobin A and Hemoglobin F Differences Babies are born with hemoglobin F (Fetal),but after a few months, the body shuts off itssynthesis and starts making hemoglobin A(Adult). That's called the hemoglobin switch.
From the structural point of view, the adult hemoglobin is composed of 4heme groups, 2 alpha chains and 2 beta chains. The fetal hemoglobin isalso composed of 4 heme groups, 2 alpha chains and 2 delta chains. The chain is 72% identical in amino acid sequence with the β chain. Onenoteworthy change is the substitution of a serine residue for Histidine143 in the β chain. In addition, the fetal hemoglobin and adulthemoglobin are found to be different near the 2,3 BPG binding site. The2,3 BPG binds less tightly with the deoxy form of fetal hemoglobin ascompared to the deoxy form of adult hemoglobin.
Hb A chain
Histidine
Hb F d chain Serine
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Hemoglobin S (Sickle Cell Anemia)
Sickle-cell anemia is caused by a mutation in the β-globin chain ofhaemoglobin, causing a hydrophilic amino acid glutamic acid to bereplaced with the hydrophobic amino acid valine.
In areas where malaria is a problem, people's chances of survival actually increaseif they carry sickle-cell trait (Carrier). The malaria parasite has a complex life cycleand spends part of it in red blood cells. In a carrier, the presence of the malariaparasite causes the red blood cells with defective haemoglobin to ruptureprematurely, making the plasmodium unable to reproduce. The polymerization ofHb S affects the ability of the parasite to digest Hb.
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Role of Distal Histidine: Binding of CO vs O2
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Role of Distal Histidine: Binding of CO vs O2
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Role of Distal Histidine: Binding of CO vs O2
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Role of Distal Histidine: Crystallographic Evidence
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Binding Effect of CO vs O2 to Hb and Mb
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Role of Protein Chain
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Synthetic Hemes (without protein chains)
Balch et al. J. Am. Chem. Soc. 1984, 106, 7779
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Model Systems for Hemoglobin and MyoglobinMethods used to inhibit the formation of μ-oxo-diiron(III)hemes: The use of low temperature so that the reactions leading to dimerization are very slow
Using steric constrains in such a way that the dimerization is inhibited: With the use ofsteric constrains a good no of Fe(II) porphyrin have been synthesized which have specialstructural features designed to facilitate reversible binding of oxygen without oxidation.Some of them are represented in the figures below namely- “picket-fence”, “strapped”,“capped”.
At room temperature this “tail-base” complex is capable offorming a μ–oxo–dimer and however it undergoes reversibleoxygenation at -45 °C leading to dimerization is prevented.
A= NH, R = H, CH2CH2COOH, CH2CH2COOMe
“picket-fence” porphyrin withsubstituted imidazole axial ligands
single-strapped, and double-strapped Capped porphyrinates
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Rigid surface attachment of the iron complex to a surface (e.g., silica gel) so thatthe dimerization is prevented
Treatment of polystyrene–Fe(II)(TPP)Im complex with O2 in benzene led to oxidation and formation of the μ-oxo dimer:
Therefore, the cross-linked polystyrene ligand was not sufficiently rigid to prevent dimerizationon treatment with oxygen. However, Fe (II)(TPP)Im–silica gel complex reversibly binds O2:
Polystyrene-Fe(II)(TPP)Im complex
Attached to modified silica gel
NB: CoboglobinA coboglobin is a synthetic compound, a metalloprotein chemically similar to hemoglobin ormyoglobin but using the metal cobalt instead of iron (hence the name). Just like hemoglobin andmyoglobin, the coboglobins are able to reversibly bind molecular oxygen (O2) at the metal atom.However they lose this ability much faster than the natural molecules.
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Hemocyanin, Hc (Greek: Blue Blood)
O2 carrying protein with Cu centre as active metal site.
Hc functions as O2 transporter and ensures sufficient O2 in the bodytissues of these “SLOW MOVERS”.
The Asymmetric unit of the hemocyanin crystal consists of six protein subunits each of mass ca.75kDa with an overall mass ca. 460kDa.
Found in some arthropods (Shrimps, Crabs) & Mollusks (Octopus,Snails).
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Hemocyanin, Hc (Greek: Blue Blood)
Deoxy-form: Colorless
Oxy-form: Blue (LMCT)
Each Cu (I) centre (d10 ) is diamagnetic.
Each Cu centre in a sq. planer environment with empty coordination site for O2 binding.
Cu-Cu distance (internuclear): 3.7 ± 0.3 Å& Cu-N bond distance: 2Å
Intranuclear Cu-Cu distance 3.6 Å
Oxygen coordination with Cu centers distort the histidines bind protein chains.
Strong antiferromagnetic coupling between two Cu (II) centre (d9) at RT essentially make them diamagnetic.
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Spectral signature of deoxy-Hc & oxy-Hc
deoxyhemocyanin
oxyhemocyanin
Significance charge transfer occurs between the coordinated peroxo group and the metal
centers.
Resonance Raman for O-O stretching frequency at 803 cm-1
confirms the peroxo linkage Bertini, I.; Gray, H. B.; Lippard, S. J.; Valentine, J. S.; Bioinorganic Chemistry; UniversityScience Books;
Mill valley, California, 1994
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X-ray structure of deoxy-Hc and oxy-Hc
PDB ID: 1LLADeoxy-hemocyanin
PDB ID: 1NOLOxy-hemocyanin
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Hemocyanin: Model Complex
N N
NN
NNHB
N N
NN
NNCu BHCuO
O
Kitazima et al. J. Am. Chem. Soc. 1992, 114, 1277-1291
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Illustration of the relevant steps for O2 binding to deoxy-hemocyanin
CuI
NN
N
CuI
N
N
N
+
O O 2
deoxyHc
oxyHc
Antiferromagnetic(superexchange stabilization)
S/T - ISC
Ferromagnetic (exchange stabilization)
Charge transfer
delocalization - reduced exchange stabilization
Metz, M.; Solomon, E. I.; J. Am. Chem. Soc. 2001, 123, 4938-4950.
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O2 carrying protein with binuclear Fe complex as active site.
Hemerythrin, Hr : Di-oxygen Carrier
Have been found in marine invertebrate phyla including thesipunculids, the brachiopods, the priapulids, and some annelids.
Consists of eight identical subunits (Mol. Wt. 107-108 kDa), eachcontaining two Fe(II) atoms in deoxy form.
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Hemerythrin, Hr : Di-oxygen Carrier
PDB ID: 1HMO
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Spectral features of deoxy-Hr, met Hr & oxy-Hr
Bertini, I.; Gray, H. B.; Lippard, S. J.; Valentine, J. S.; Bioinorganic Chemistry; UniversityScience Books; Mill valley, California, 1994
Considerable charge transfer occurs between the coordinated peroxogroup and the metal center.
Resonance Raman for O-O stretching frequency at 844 cm-1 confirms the peroxo linkage
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Azidomet Hemerythrin & Structural Model of Met-Hr
FeIII
NN
N
HN
NH
HN
His73
His101
His77
FeIII
N
N
HN
NH
His54
His25
O
OO
Asp106O
Glu58
O
N3
An inactive form of protein
Contains (μ-oxo) diiron (III) centers
Azide anion( N3-) is coordinate to
Fe, at the site normally occupied by O2 in oxy-Hr.
Antiferromagnetic spin exchange between the two high spin Fe(III) centers.
FeIII
NN
N
FeIII
N
N
O
OO
RO
R
O
NNH
NH
NH
N3 =
(A). Holmes, M.A.; Stenkamp, R. E.; J. Mol. Biol. 1991, 220, 723-737; (B). Armstrong, W. H.; Lippard, S. J. J. Am. Chem. Soc. 1983, 105, 4837-4838; (C). Wieghardt, K.; Pohl, K.; Gebert, W. Angew. Chem., Int. Ed. Engl. 1983, 22, 727.
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Structural Models for Hemerythrin
Mizoguchi et al. Inorg. Chem. 2001, 40, 4662-4673
Optical spectra of [Fe2(µ-OH)(µ-Ph4DBA)(DPE)2(OTf)] in EtCN at -78 °C before (- - -) and after (-) addition of dioxygen.
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Schematic Summary of the Redox State s of the binucler ironcenter & their Interconversion
Handbook of Metalloproteins, Online © 2006 John Wiley & Sons, Ltd
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Metalloproteins Active Site (deoxy)
Color Change(deoxy to oxy)
Molecular Weight
Source
Hemoglobin Fe(II) [in Heme]
Purple to Red 64, 000 Higher form of life
Myoglobin Fe(II) [in Heme]
Purple to Red 17,100 Higher form of life
Hemocyanin Cu(I)….Cu(I) Colorless to Blue
~ 9 x 106 Arthopods, Molluscs
Hemerythrin Fe(II) ….Fe(II) Colorless to Burgundy
108,000 MarineInvertebrates
O2 Carrying Protein in Biology
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1. Give brief descriptions of the following: (a) peptide; (b) naturally occurring amino acids; (c)metalloprotein; (d) haem unit
2. Compare the modes of binding of O2 to the metal centres in (a) myoglobin, (b) haemerythrinand (c) haemocyanin. Indicate what supporting experimental evidence is available for thestructures you describe.
3. Give an account of the storage and transport of metalloproteins in mammals. How does theuptake of iron by aerobic microorganisms differ from that in mammals?
4. (a) Briefly describe the mode of binding of O2 to the iron centre in one haem unit ofhaemoglobin. (b) What are ‘picket fence’ porphyrins and why are they used inmodel studies of O2 binding to myoglobin or haemoglobin? (c) The binding of O2 tohaemoglobin exhibits a ‘cooperativity’ effect. What is meant by this statement? (d) Why isthe change from deoxyhaemoglobin to the oxy-form accompanied by a decrease in theobserved magnetic moment?
5. Draw the active site structures of deoxy & oxy form of (a) haemoglobin (b) hemocyanin and (c) hemerythrin?
6. Explain the term “Bohr Effect”?7. Explain the term haematin formation with the possible fate of Fe (II) centre?
Problems