Three Dimensional Fourier Synthesis of Horse Deoxyhaemoglobin at 2.8 Å Resolution

Bolton, W.; Perutz, M. F.

doi:10.1038/228551a0

Cited by 268 publications

(122 citation statements)

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“…These results are in a good agreement with the classification established on the heme iron spin state. X-ray analyses by Perutz et al [1,2] have shown that the structure of deoxyhemoglobin differs profoundly from the structure of methemoglobin, which was considered structurally identical with oxyhemoglobin. The recent X-ray comparison analyses by Heidner et al [3] and Deatherage et al 141 have demonstrated that the conformation of crystalline methemoglobin is not identical with that of crystalline carbonmonoxyhemoglobin and cyanomethemoglobin, and the conformational differences can be expected to influence the properties of hemoglobin derivatives in solutions.…”

mentioning

confidence: 99%

The Interaction of Human Hemoglobin with Erythrosin

Kalousek¹,

Jandová²,

Vodrážka³

1978

European Journal of Biochemistry

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The interactions of erythrosin with deoxyhemoglobin, oxyhemoglobin, carbonmonoxyhemoglobin, methemoglobin, cyanomethemoglobin and hemoglobin α and β chains have been studied by using the equilibrium dialysis, the difference and circular dichroic (CD) spectra and stopped‐flow method. The values of equilibrium and kinetic parameters, as well as CD characteristics, show that in addition to a number of weak binding sites hemoglobin contain four, relatively strong binding sites, one per chain. The properties of the strong binding sites depend on the ligand of the heme group and the charge of the heme group is not directly responsible for this fact. Consequently the properties of deoxyhemoglobin and methemoglobin, differing from the mutually close properties of the other derivatives, confirm that the state of the heme group affects the conformation of hemoglobin molecules in solution. These results are in a good agreement with the classification established on the heme iron spin state.

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mentioning

confidence: 99%

The Interaction of Human Hemoglobin with Erythrosin

Kalousek¹,

Jandová²,

Vodrážka³

1978

European Journal of Biochemistry

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“…One possible explanation is that in this pH range small conformational changes may occur which permit the arginine in position 95 (G2) of the ot chain to form a van der Waals contact, either with tryptophan residue in position 837 (C3) (which in normal hemoglobin forms an a1-p2 contact with position a95), or else with some other residue in the 8 chain. Such an explanation appears reasonable in view of the fact that in normal oxyhemoglobin, arginine in position a92 (FG4) forms three van der Waals type bonds in the critical a,-/?2 contacts and arginine in position 840 (C6) participates in four such contacts by means of van der Waals interactions [4]; upon deoxygenation, conformational changes occur which disrupt one of these contacts in the ot92 arginine, and two of the contacts in the 840 arginine [34]. A complete understanding ofthe interesting and unusual properties of hemoglobin St Luke's will require the X-ray analysis of both its oxy and deoxy structures.…”

Section: Discussionmentioning

confidence: 99%

Hemoglobin St Luke's or α^95Arg₂ (G2) β₂

Bannister

Grech

Plese

et al. 1972

European Journal of Biochemistry

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A new hernoglobin variant, designated hemoglobin-St Luke's, was detected by routine starch-gel electrophoresis in four members of a Maltese family. The carriers of this abnormality are clinically and hematologically normal. Structural analyses showed the replacement of prolyl residue in position 95 (G2) of the alpha chain by an arginyl residue. The relative amount of hemoglobin-St Luke's present in the red cell hemolysates of its carrier is approximately loo/,, compared to about 2301, for hemoglobin-G Georgia and 15Oj, for hemoglobin-Rampa (the other two variant,s in which prolyl residue a95 (G2) is replaced). Sedimentation velocity studies of hemoglobin-St Luke's in NaCl solutions of increasing concentration up to 2 M indicak &hat the oxy derivative is extensively dissociated into dimers in 0.1 M NaCl a t neutral pH; whereas under the same conditions, the deoxygenated molecule retains a tetrameric structure. In the deoxy state, appreciable tetramer formation occurs even in 2 M NaCI. In addition, association-dissociation in oxyor cyanferrihemoglobin St Luke's is both pH and temperature dependent.Hemoglobins G Georgia and Rainpa are variants in which the proIyl residue in position 95 of the cx chain is replaced by a leucyl and a seryl residue, respectively [I, 2 ) . The liganded derivatives of these abnormal hemoglobins are extensively dissociated into dimers in NaCl solutions of low molarity and a t neutral pH [3]. I n contrast, the deoxygenated derivatives of the two variants are tetramers under the same conditions. The substitution of the prolyl residue occurs a t a site which involves one of the critical contacts ; these contacts are broken when hemoglobin tetramers dissociate into dimers [41. The introduction of either a leucyl residue or a seryl residue in position a95 (G2) ruptures the contacts normally present between Pro-ag5 (G2) and Trp-/337 (C3) in oxygenated hemoglobin [4], and causes an extensive disruption of the al-& contact, probably because the contact becomes accessible to water 131. The greatly increased degree of dimer formation of the two variants is associated with an increased affinity for oxygen and a decrease in heme-heme interaction [3] ; carriers of these abnormalities appear normal.Abbreviation. Hb, hemoglobin.We recently observed an additional variant in which the prolyl residue in position a95 is substituted by an arginyl residue. The variant, t-ermed HbSt Luke's, was present in four members of a Maltese family. This paper describes results of structural analyses and data from sedimentation velocity analyses of the oxy (or cyanferri) and deoxy forms of Hb-St Luke's as a function of salt concentration, pH, and temperature. Results of a few oxygen equilibrium experiments are also included. MATERIALS AND METHODSBlood samples from members of family M were collected with EDTA as anticoagulant. Hematological studies were made by standard methods [5]. Parts of the samples were mailed by air from Malta to Augusta (Georgia, U.S.A.). Hemolysates were prepared by mixing 1 vol. washed packed cel...

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“…These would not be expected to greatly affect the stereochemistry of the contact although the hydrogen bonding of the G4 Asn in human oxyhaemoglobin stabilizes the oxy form and the dimensions are important (Morimoto et al 1971). In the deoxyhaemoglobin contacts (Bolton and Perutz 1970) additional side chains are brought into contact by the sliding and rotation, and Val for Pro G2 is involved in the contact. Although not previously recorded for f3-chains this residue or isoleucine is common in myoglobins, which do not form tetramers.…”

Section: Discussionmentioning

confidence: 99%

“…Most of these sites are variable in different species; the substitutions of Lys for Gly GH2, and Lys for Asn G 10 have not been recorded previously. Bolton and Perutz (1970) without the numbers representing atoms in contact for each residue. Below each residue of horse globin chains any different residue in shark chains is shown in parentheses.…”

Section: Discussionmentioning

confidence: 99%

Haemoglobins of the Shark, Heterodontus portusjacksoni III. Amino Acid Sequence of the ß -Chain

Fisher¹,

Nash²,

Thompson³

1977

Aust. Jnl. Of Bio. Sci.

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The amino acid sequence of the p-chain of the principal haemoglobin from the shark H. portusjacksoni has been determined. The chain has 141 residues, the same as that of mammalian IX-chains and less than the 146 residues of mammalian p-chains or the 148 residues of the IX-chain from the tetrameric shark haemoglobin. The sequence was deduced from the sequences of peptides obtained by digestion of the globin or its cyanogen bromide fragments with trypsin, chymotrypsin, pepsin and papain.The difference in length of the p-chain is most readily accounted for by the absence of the D helix. This small helical section is normally present in myoglobins and p-globins but absent in IX-chains. The deduction that it is absent from shark p-chain is based on considerations of homology. The p-chain shows the insertion of histidine P2 and the deletions corresponding to residues A17 and AB1 relative to IX-and myoglobin chains.The reactive thiol group in shark haemoglobin was shown by radioactive labelling to be residue 51 in the P-chain, immediately preceding the E helix.The amino acid sequence of shark p-chain shows 92 differences from human p-chain, significantly more differences than shown by chicken or frog p-chains, in line with its earlier time of divergence.If the tertiary structure of the shark p-chain is the same as that of the horse then there are two changes in the IXl pz contact site in oxyhaemoglobin and an additional one in deoxyhaemoglobin.When both IX-and p-chain contacts are considered there is a total of nine changes in residues involved in the IXl pz contacts. There is no Bohr effect in shark haemoglobin, and of the residues normally involved in this effect the C-terminal histidine residue of the p-chain is present, but the aspartyl (FG1) residue to which it is salt-linked is not, being replaced by a glutamyl residue.

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Three Dimensional Fourier Synthesis of Horse Deoxyhaemoglobin at 2.8 Å Resolution

Cited by 268 publications

References 7 publications

The Interaction of Human Hemoglobin with Erythrosin

The Interaction of Human Hemoglobin with Erythrosin

Hemoglobin St Luke's or α^95Arg₂ (G2) β₂

Haemoglobins of the Shark, Heterodontus portusjacksoni III. Amino Acid Sequence of the ß -Chain

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Three Dimensional Fourier Synthesis of Horse Deoxyhaemoglobin at 2.8 Å Resolution

Cited by 268 publications

References 7 publications

The Interaction of Human Hemoglobin with Erythrosin

The Interaction of Human Hemoglobin with Erythrosin

Hemoglobin St Luke's or α95Arg2 (G2) β2

Haemoglobins of the Shark, Heterodontus portusjacksoni III. Amino Acid Sequence of the ß -Chain

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Hemoglobin St Luke's or α^95Arg₂ (G2) β₂