Hemoglobin San Diego (β109 (G11) Val→Met) CRYSTAL STRUCTURE OF THE DEOXY FORM

Anderson, N. Leigh

doi:10.1172/jci107554

Cited by 17 publications

(8 citation statements)

References 9 publications

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“…The fuiictional and structural properties of Hb San Diego have been discussed previously (Nute et al, 1974;Anderson, 1974). The present data confirm that haemolysates containing Hb San Diego have a two-fold increase in oxygen affinity compared with normal.…”

Section: Discussionsupporting

confidence: 89%

Erythraemia due to Haemoglobin San Diego

et al. 1975

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A 63-year-old man with erythraemia was found to have a high affinity haemoglobin which was subsequently identified as Hb San Diego beta 109 (G11) Val leads to Met, recently described in a Filipino family (Nute et al, 1974). The oxygen affinity of the haemolysates was increased approximately two-fold at pH values between 6.04 and 7.90. The n value was nearly normal (2.5-2.9) in the upper range of saturation (70-95% oxygenation) but was somewhat diminished (1.9-2.1) below this range. In vitro biosynthesis of globin by reticulocytes showed that there was balanced synthesis of alpha and beta chains (alpha:beta ratio = 1).

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Section: Discussionsupporting

confidence: 89%

Erythraemia due to Haemoglobin San Diego

et al. 1975

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“…The presence of a cooperative interaction across the al/31 interface was suggested by observations for Hb San Diego [Val-/3109(G1 l)-*-Met] with mutation at the al/31 interface. Loukopoulos et al (1986) showed that Hb San Diego has significantly decreased cooperativity as compared to normal Hb A, while X-ray crystallographic analysis on mixed crystals of deoxyHb San Diego and deoxyHb A did not clearly show significant differences at the a 1/32 interface (Anderson, 1974). Moreover, ElAntri et al (1989) suggested a significant role of the al/31 interface by comparison of the sulfhydryl vibrational absorption of Cys-/3112 in Hb San Diego with that in normal Hb A. Kawamura-Konishi and Suzuki (1988) measured the reconstitution kinetics of chemically modified Hbs from the modified a and ß chains.…”

Section: Discussionmentioning

confidence: 95%

Oxygen equilibrium properties of asymmetric nickel(II)-iron(II) hybrid hemoglobin

Shibayama¹,

Imai²,

Morimoto³

et al. 1993

Biochemistry

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Asymmetric Ni(II)-Fe(II) hybrid hemoglobin, XL[alpha(Fe)beta(Fe)][alpha(Ni)beta(Ni)], in which the alpha 1 beta 1 dimer containing ferrous protoporphyrin IX and the complementary alpha 2 beta 2 dimer containing Ni(II) protoporphyrin IX were cross-linked between Lys-82 beta 1 and Lys-82 beta 2 by reaction with bis(3,5-dibromosalicyl) fumarate, was synthesized and characterized. We have previously shown that (i) Ni(II) protoporphyrin IX, which binds neither oxygen nor carbon monoxide, mimics a fixed deoxyheme with respect to its effect on the oxygen equilibrium properties of the counterpart iron subunits in both symmetric Ni(II)-Fe(II) hybrid Hbs [Shibayama, N., Morimoto, H., & Miyazaki, G. (1986) J. Mol. Biol. 192, 323-329] and (ii) the cross-linking used in this study little affects the oxygen equilibrium properties of hemoglobin [Shibayama, N., Imai, K., Hirata, H., Hiraiwa, H., Morimoto, H., & Saigo, S. (1991) Biochemistry 30, 8158-8165]. These remarkable features of our model allowed us to measure the oxygen equilibrium curves for the first two steps of oxygen binding to the alpha 1 beta 1 dimer within the hemoglobin tetramer. At all pH values examined, the affinities of this asymmetric hybrid for the first oxygen molecule are as low as those of native hemoglobin. The hybrid did not show cooperative oxygen binding at pH 6.4, while significant cooperativity was observed with rising pH; i.e., the Hill coefficient was increased from 1.41 to 1.53 upon a pH change from 7.4 to 8.4. The electronic absorption spectrum of Ni(II) protoporphyrin IX in the alpha 2 subunit was changed upon carbon monoxide (or oxygen) binding to the alpha 1 beta 1 dimer.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…This could arise from the fact that the fully liganded form is less sensitive to changes in the heme geometry than the deoxy form; no change in the heme region in the liganded form does not mean no change in the deoxy form between the two hemoglobins. However this hypothesis can be discarded since crystallographic studies on the deoxy form [6] failed to reveal any tilt of the heme nor change at the alp2 interface.…”

Section: Discussionmentioning

confidence: 99%

“…This mutation could involve indirect alterations at the alp2 interface accompanied by a tilt of the hemes. Crystallographic analysis on deoxy Hb San Diego did not clearly reveal a tilt of the hemes nor any significant differences at the alp2 interface [6]. Moreover, the dependence of the oxygen affinity of Hb San Diego upon addition of chloride or organophosphate strongly suggests that the p-109 Val + Met mutation is not transmitted to the alp2 contacts [7].…”

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confidence: 99%

Implication of the α1β1 interface in the hemoglobin affinity changes

Antri¹,

Zentz²,

Alpert³

1989

European Journal of Biochemistry

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The α1β1 interface of normal and mutated San Diego hemoglobins in their fully liganded form was investigated, through the SH vibrational absorption of β‐112 cysteine, byFourier‐transform infrared spectroscopy. The center frequency of this thiol group was significantly shifted in San Diego hemoglobin compared with normal human hemoglobin. Different dimer organization between the two proteins was also revealed by circular dichroism of the heme. These findings agree well with assessment that the α1β1 interface, far from being inert, is involved in the affinity changes of the hemoglobin molecule.

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Hemoglobin San Diego (β109 (G11) Val→Met) CRYSTAL STRUCTURE OF THE DEOXY FORM

Cited by 17 publications

References 9 publications

Erythraemia due to Haemoglobin San Diego

Erythraemia due to Haemoglobin San Diego

Oxygen equilibrium properties of asymmetric nickel(II)-iron(II) hybrid hemoglobin

Implication of the α1β1 interface in the hemoglobin affinity changes

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