Spectroelectrochemistry of heme proteins: Effects of active-site heterogeneity on Nernst plots

Bioelectrochemistry and Bioenergetics

Volumn 48, Issue 1, 1999, Pages 79-86

  Taboy, Céline H ^a   Bonaventura, Celia ^b   Crumbliss, Alvin L ^a  

^a DUKE UNIVERSITY   (United States)

^b DUKE UNIVERSITY MARINE LABORATORY   (United States)

Author keywords

Aplysia; Heme proteins; Hemoglobin; Myoglobin; Non Nernstian systems; Spectroelectrochemistry

Indexed keywords

MOLECULAR STRUCTURE; REDOX REACTIONS;

MYOGLOBIN; NERNST PLOTS; SPECTROELECTROCHEMISTRY;

HEMOGLOBIN;

HEMOGLOBIN; HEMOPROTEIN; MYOGLOBIN;

APLYSIA; ARTICLE; ELECTROCHEMISTRY; HORSE; HUMAN; MALE; NONHUMAN; OXIDATION REDUCTION REACTION; OXYGEN AFFINITY; OXYGENATION; SPERM; WHALE;

ALGORITHMS; ANIMALS; APLYSIA; ELECTROCHEMISTRY; HEMEPROTEINS; HORSES; KINETICS; MODELS, CHEMICAL; MYOGLOBIN; OXIDATION-REDUCTION; OXYGEN; PROTEIN BINDING; WHALES;

APLYSIA; CETACEA; EQUUS CABALLUS; PHYSETER CATODON;

EID: 0033029098     PISSN: 03024598     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0302-4598(98)00236-0     Document Type: Article

References (26)

1. 0 and Deer Lodge β2(NA2)His→Arg. Biochemistry. 37:1998;496-506.
2. Faulkner K.M., Bonaventura C., Crumbliss A.L. A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins. J. Biol. Chem. 270:1995;13604-13612.
3. T. Hill, Cooperativity Theory in Biochemistry, Springer, Berlin, 1984.
4. J. Wyman, S.J. Gill, Binding and Linkage, University Science Books, Mill Valley, CA, 1990.
5. E. Di Cera, Thermodynamic Theory of Site-Specific Binding Processes in Biological Macromolecules, Cambridge Univ. Press, Cambridge, UK, 1995.
6. E. Antonini, M. Brunori, Hemoglobin and Myoglobin in their Reactions with Ligands, North-Holland, Amsterdam 1971, pp. 19, 331, and references therein.
7. Faulkner K.M., Bonaventura C., Crumbliss A.L. A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins. Inorg. Chim. Acta. 226:1994;187-194.
8. Antonini E., Wyman J., Brunori M., Taylor J.F., Rossi-Fanelli A., Caputo A. Studies on the oxidation-reduction potentials of heme proteins. 1: Human hemoglobin. J. Biol. Chem. 239:1964;907-912.
9. Di Cera E. Site-specific thermodynamics: understanding cooperativity in molecular recognition. Chem. Rev. 98:1998;1563-1591.
10. Malmström B.G. Cytochrome c oxidase: some current biochemical and physical problems. Q. Rev. Biophys. 6:1974;389-431.
11. Kristensen E.W., Igo D.H., Elder R.C., Heineman W.R. Non-Nernstian behavior of Nernstian plots from spectroelectrochemistry experiments. J. Electroanal. Chem. 309:1991;61-72.
12. Banerjee R., Cassoly R. Preparation and properties of the isolated α and β chains of human hemoglobin in the ferri state: investigation of oxidation-reduction equilibria. J. Mol. Biol. 42:1969;337-340.
13. R.A. Greenwald, in: CRC Handbook of Methods for Oxygen Radical Research, CRC Press, Boca Raton, FL, 1985, pp. 137-141.
14. Brunori M., Glacometti G.M., Antonini E., Wyman J. Denaturation of Aplysia myoglobin. Equilibrium study. J. Biol. Chem. 63:1972;139-152.
15. Brunori M., Saggese U., Rotitio G.C., Antonini E., Wyman J. Redox equilibrium of sperm whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin. Biochemistry. 10:1971;1604-1609.
16. Riggs F., Walbach R.A. Sulfhydryl groups and the structure of hemoglobin. J. Gen. Physiol. 39:1956;585-605.
17. Bolognesi M., Onesti S., Gatti G., Coda A., Ascenzi P., Brunori M. Aplysia limacina myoglobin crystallographic analysis at 1.6 Å resolution. J. Mol. Biol. 205:1989;529-544.
18. Taylor J.F., Morgan V.E. Oxidation-reduction potentials of the metmyoglobin-myoglobin system. J. Biol. Chem. 144:1942;15.
19. Shikama K., Matsuoka A. Aplysia myoglobin with unusual properties: another prototype in myoglobin and hemoglobin biochemistry. Biol. Rev. (Cambridge). 69:1994;233-251.
20. Brunori M., Alfsen A., Saggese U., Antonini E., Wyman J. Studies on the oxidation-reduction potentials of heme proteins. VII: Oxidation-reduction equilibrium of hemoglobin bound to haptoglobin. J. Biol. Chem. 243:1968;2950-2954.
21. Moore G.R., Pettigrew G.W., Rogers N.K. Factors influencing redox potential of electron transfer proteins. Proc. Natl. Acad. Sci. 83:1986;4998-4999.
22. Zhou H.-X. Control of reduction potential by protein matrix: lesson from a spherical protein model. JBIC. 2:1997;109-113.
23. Mauk A.G., Moore G.R. Control of metalloprotein redox potentials: what does site-directed mutagensis of hemoproteins tell us? JBIC. 2:1997;119-125.
24. Gunner M.R., Alexov E., Torres E., Lipovaca S. The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis. JBIC. 2:1997;126-134.
25. Warshel A., Papazyan A., Muegge I. Microscopic and semimacroscopic redox calculations: what can and cannot be learned from continuum models. JBIC. 2:1997;143-152.
26. Lloyd E., King B.C., Hawkridge F.M., Mauk A.G. Electrostatic modulation of ligand binding and electrochemical properties of myglobin: the role of charge compensation. Inorg. Chem. 37:1998;2888-2892.