Wavelength-dependent Spectral Changes Accompany CN-hemin Binding to Human Apohemoglobin

Overview

Journal J Protein Chem

Specialties Biochemistry
Chemistry

Date 2001 Mar 10

PMID 11233172

Citations 3

Authors

G Vasudevan

M J McDonald

Affiliations

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Abstract

The interaction of apohemoglobin with two heme derivatives, CN-protohemin and CN-deutero-hemin, was monitored at multiple Soret wavelengths (417-423 and 406-412 nm, respectively) in 0.05 M potassium phosphate buffer, pH 7.0, at 10 degrees C and revealed, as previously reported, a multiphasic kinetic reaction. Wavelength-dependent reactions were observed for both CN-protohemin and CN-deuterohemin derivatives with the alpha chain (bathochromic entity) displaying faster (4- to 7-fold) rates throughout the courses of both heme-binding reactions. The basis of this spectrally heterogeneous kinetic phenomenon could be deduced from molecular modeling studies of alpha- and beta-chain structures. Key differences in the number of stabilizing contacts of the two chains with the peripheral alpha propionyl 45(CE3); 58(E7); 61(E10) as well as the beta vinyl 38(C4); 71(E15); 106(G8) groups were found. Furthermore, RMS plots comparing apo- and heme-containing subunits reveal substantial structural disparities in the C-CD-F-FG helical regions of the alphabeta dimer interface.

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References

Vasudevan G, McDonald M . Analysis of the global architecture of hemoglobin A2 by heme binding studies and molecular modeling. J Protein Chem. 1998; 17(4):319-27. DOI: 10.1023/a:1022551131455. View

Sobolev V, Sorokine A, Prilusky J, Abola E, Edelman M . Automated analysis of interatomic contacts in proteins. Bioinformatics. 1999; 15(4):327-32. DOI: 10.1093/bioinformatics/15.4.327. View

MOULTON D, McDonald M . Kinetics of human apohemoglobin dimer dissociation. Biochem Biophys Res Commun. 1994; 199(3):1278-83. DOI: 10.1006/bbrc.1994.1369. View

GIBSON Q, Antonini E . Kinetic studies on the reaction between native globin and haem derivatives. Biochem J. 1960; 77:328-41. PMC: 1204989. DOI: 10.1042/bj0770328. View

Winterhalter K, Glatthaar B . Intermediates of hemoglobin and their relation to biosynthesis. Ser Haematol. 1971; 4(3):84-96. View

ISHIMORI K, Morishima I . Study of the specific heme orientation in reconstituted hemoglobins. Biochemistry. 1988; 27(13):4747-53. DOI: 10.1021/bi00413a025. View

Rose M, Olson J . The kinetic mechanism of heme binding to human apohemoglobin. J Biol Chem. 1983; 258(7):4298-303. View

Schaad O, Vallone B, Edelstein S . Critical residues responsible for self-association differences of hemoglobin alpha and beta chains: analysis by molecular modeling. C R Acad Sci III. 1993; 316(6):564-71. View

Vasudevan G, McDonald M . Spectral demonstration of semihemoglobin formation during CN-hemin incorporation into human apohemoglobins. J Biol Chem. 1997; 272(1):517-24. DOI: 10.1074/jbc.272.1.517. View

10.

Suzuki H . Binding reaction of hemin to globin. J Biochem. 1985; 98(5):1181-90. DOI: 10.1093/oxfordjournals.jbchem.a135384. View

11.

Aojula H, Wilson M, Drake A . Characterization of haem disorder by circular dichroism. Biochem J. 1986; 237(2):613-6. PMC: 1147030. DOI: 10.1042/bj2370613. View

12.

La Mar G, Yamamoto Y, Jue T, Smith K, Pandey R . 1H NMR characterization of metastable and equilibrium heme orientational heterogeneity in reconstituted and native human hemoglobin. Biochemistry. 1985; 24(15):3826-31. DOI: 10.1021/bi00336a002. View

13.

Park R, McDonald M . Kinetics of heme binding to semi-alpha-hemoglobin. Biochem Biophys Res Commun. 1989; 162(1):522-7. DOI: 10.1016/0006-291x(89)92028-7. View

14.

Baldwin J . The structure of human carbonmonoxy haemoglobin at 2.7 A resolution. J Mol Biol. 1980; 136(2):103-28. DOI: 10.1016/0022-2836(80)90308-3. View

15.

Peitsch M . ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochem Soc Trans. 1996; 24(1):274-9. DOI: 10.1042/bst0240274. View

16.

Inaba K, ISHIMORI K, Imai K, Morishima I . Substitution of the heme binding module in hemoglobin alpha- and beta-subunits. Implication for different regulation mechanisms of the heme proximal structure between hemoglobin and myoglobin. J Biol Chem. 2000; 275(17):12438-45. DOI: 10.1074/jbc.275.17.12438. View

17.

Guex N, Diemand A, Peitsch M . Protein modelling for all. Trends Biochem Sci. 1999; 24(9):364-7. DOI: 10.1016/s0968-0004(99)01427-9. View

18.

Yip Y, Waks M, BEYCHOK S . Reconstitution of native human hemoglobin from separated globin chains and alloplex intermediates. Proc Natl Acad Sci U S A. 1977; 74(1):64-8. PMC: 393197. DOI: 10.1073/pnas.74.1.64. View

19.

Cassoly R, Bucci E, IWATSUBO M, Banerjee R . Functional studies on human semi-hemoglobin. Biochim Biophys Acta. 1967; 133(3):557-67. DOI: 10.1016/0005-2795(67)90560-0. View

20.

Chiba K, Kihara H, Suzuki H . Kinetics of the reconstitution of hemoglobin from semihemoglobins alpha and beta with heme. Eur Biophys J. 1992; 21(2):85-92. DOI: 10.1007/BF00185423. View