Hemoglobin biochemistry

Szebeni J, Hauser H, Eskelson CD, et al. Interaction of hemoglobin derivatives with liposomes. Membrane cholesterol protects against the changes of hemoglobin. Biochemistry 1988 27 6425. 

Sharma, V. S., Traylor, T. G., Gardiner, R., and Mizukami, H. (1987). Reaction of nitric oxide with heme proteins and model compounds of hemoglobin. Biochemistry 26, 3837-3843. 

Kiehs, K., C. Hansch, and L. Moore, The role of hydrophobic bonding in the binding of organic compounds by bovine hemoglobin , Biochemistry, 5,2602-2605 (1966). 

Dickerson, R. E., and I. Geis, Hemoglobin. Menlo Park, Calif. Benjamin/Cummings, 1983. A magnificent presentation of every facet of hemoglobin biochemistry and genetics. 

Mueser T, Rogers P, Arnone A. Interface sliding as illustrated by the multiple quaternary structures of Uganded hemoglobin. Biochemistry 2000 39 15353-15364. 

Eich RF, Li TS, Lemon DD, Doherty DH, Curry SR, Aitken IF, Mathews AJ, Johnson KA, Smith RD, Phillips GN, Olson JS. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry 1996 35 6976-6983. 

Chan ML, Rogers PH, Amone A. 1998. Crystal structure of the S-nitroso form of Uganded human hemoglobin. Biochemistry 37(47) 16459-16464. 

Chan ML, Kavanaugh JS, Rogers PH, Amone A. 2004. Crystallographic analysis of the interaction of nitric oxide with quatemary-T human hemoglobin. Biochemistry 43(1) 118-132. 

Benesch, R., Benesch, R., Raenthal, R., and Maeda, N. Affinity labeling of the polyphosphate binding site of hemoglobin. Biochemistry 11(19) 3576-3582,1972. 

ScHROEDEB, W. A., Shelton, J. R., Shelton, J. B., Gormick, J., and Jones, R. T. (1963a). The amino acid sequence of the gamma chain of human fetal hemoglobin. Biochemistry 2, 992-1008. 

Manz, B Stilbs, P Jonsson, B Soderman, O Callaghan, PT, NMR Imaging of the Time Evolution of Electroosmotic Flow in a Capillary, Journal of Physical Chemistry 99, 11297, 1995. Matthew, JB Hanania, GIH Gurd, FRN, Electrostatic Effects in Hemoglobin Bohr Effect and Ionic Strength Dependence of Individual Groups, Biochemistry 18, 1928, 1979. 

Matthew, JB Hanania, GIH Gurd, ERN, Electrostatic Effects in Hemoglobin Hydrogen Ion Equilibria in Human Deoxy- and Oxyhemoglobin A, Biochemistry 18, 1919, 1979. 

Orttung, WH, Proton Binding and Dipole Moment of Hemoglobin. Refined Calculations, Biochemistry 9, 2394, 1970. 

Figure 6-11. Representation of the sticky patch (A) on hemoglobin S and its "receptor" (A) on deoxyhemoglobin A and deoxyhemoglobin S. The complementary surfaces allow deoxyhemoglobin S to polymerize into a fibrous structure, but the presence of deoxyhemoglobin A will terminate the polymerization by failing to provide sticky patches. (Modified and reproduced, with permission, from Stryer L Biochemistry, 4th ed. Freeman, 1995.)...

The Hemoglobin Protein A Useful Teaching Model. Department of Biochemistry, Medical College of Wisconsin,... 

Mintorovitch, J., D.V. Pelt, and J.D. Satterlee. 1989. Kinetic study of the slow cyanide binding to Glycera dibranchiata monomer hemoglobin components HI and IV. Biochemistry 28 6099-6104. 

Figure 4.3 Myoglobin and hemoglobin quaternary structures. (Reprinted from Figure 4.2 of Cowan, J. A. Inorganic Biochemistry, An Introduction, 2nd ed., Wiley-VCH, New York, 1997. Copyright 1997, Wiley-VCH.)...

Y. Nomura and M. Tamura. Quantitative analysis of hemoglobin oxygenation state of rat brain in vivo by picosecond time-resolved spectrophotometry. Journal of Biochemistry, 109 455-461, 1991. 

Andreyuk GM, Kisel MA. Conversion of hemoglobin to hemichrome by lysophospholipids. Biochemistry (Mosc) 64, 867, 1999. 

Szebeni J, Di lorio EE, Hauser H, et al. Encapsulation of hemoglobin in phospholipid liposomes characterization and stability. Biochemistry 1985 24 2827. 

The term interaction is sometimes used almost synonymously with cooperativity. In this book we reserve the term interaction to mean direct interaction energy between two (or more) particles. Indeed, sometimes interaction, in the above sense, is the sole source of cooperativity, in which case the two terms may be used interchangeably. However, in most cases of interest in biochemistry, interaction in the above sense is almost negligible, such as in two oxygen molecules in hemoglobin. Cooperativity in such systems is achieved by indirect routes of communication between the ligands. 

Mehanna, A.S. Abraham, D.J. Comparison of crystal and solution hemoglobin binding of selected antigelling agents and allosteric modifiers. Biochemistry 1990, 29, 3944-3952. 

Nagai, M., et al. (1991) Unusual CO bonding geometry in abnormal subunits of hemoglobin M Boston hemoglobin M Saskatoon. Biochemistry 30, 6495-6503. 

Franzen, S., Bohn, B., Poyart, C., and Martin, J. L. 1995. Evidence for sub-picosecond heme doming in hemoglobin and myoglobin A time-resolved resonance Raman comparison of carbonmonoxy and deoxy species. Biochemistry 34 1224-37. 

---