Bridging the gap between chemistry, physiology, and evolution: Quantifying the functionality of sperm whale myoglobin mutants

Comparative Biochemistry and Physiology -Part A : Molecular and Integrative Physiology

Volumn 161, Issue 1, 2012, Pages 9-17

  Dasmeh, Pouria ^a   Kepp, Kasper P ^a  

^a TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; MYOGLOBIN; OXYGEN;

ARTICLE; HYPOXIA; MUSCLE TISSUE; NONHUMAN; OXYGEN CONSUMPTION; OXYGEN TRANSPORT; OXYGENATION; PARTIAL PRESSURE; PHYSIOLOGY; SPERM WHALE; ANIMAL; CHEMISTRY; DIVING; GENETIC SELECTION; GENETICS; HUMAN; METABOLISM; MOLECULAR EVOLUTION; MUSCLE CELL; PRESSURE; WHALE;

ANIMALS; DIVING; EVOLUTION, MOLECULAR; HUMANS; MUSCLE CELLS; MYOGLOBIN; OXYGEN; PARTIAL PRESSURE; SELECTION, GENETIC; SPERM WHALE; WHALES;

EID: 80052659359     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2011.07.027     Document Type: Article

References (46)

1. Bangsbo, J., Muscle oxygen uptake in humans at onset of and during intense exercise. Acta Physiol. Scand. 168 (2000), 457–464.
2. Berenbrink, M., Mirceta, S., How to make a whale: molecular signature of myoglobin in diving birds and mammals. Comp. Biochem. Physiol. A, 153, 2009, S44.
3. Bucci, E., Thermodynamic approach to oxygen delivery in vivo by natural and artificial oxygen carriers. Biophys. Chem. 142 (2009), 1–6.
4. Davis, R.W., Kanatous, S.B., Convective oxygen transport and tissue oxygen consumption in Weddell seals during aerobic dive. J. Exp. Biol. 202 (1999), 1091–1113.
5. Duteil, S., Bourrilhon, C., Raynaud, J.S., Wary, C., Richardson, R.S., Leroy-Willig, A., Jouanin, J.C., Guezennec, C.Y., Carlier, P.G., Metabolic and vascular support for the role of myoglobin in humans: a multiparametric NMR study. Am. J. Physiol. Regul. Integr. Comp. Physiol. 287:6 (2004), R1441–1449.
6. Elber, R., Ligand diffusion in globins: simulations versus experiment. Curr. Opin. Struct. Biol. 20 (2010), 162–167.
7. Frauenfelder, H., McMahon, B.H., Fenimore, P.W., Myoglobin: the hydrogen atom of biology and a paradigm of complexity. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 8615–8617.
8. Gimenez, M., Sanderson, R.J., Reiss, O.K., Banchero, N., Effects of altitude on myoglobin and mitochondrial protein in canine skeletal muscle. Respiration 34 (1977), 171–176.
9. Groebe, K., An easy-to-use model for O2 supply to red muscle. Validity of assumptions, sensitivity to errors in data. Biophys. J. 68 (1995), 1246–1269.
10. Gros, G., Wittenberg, B.A., Jue, T., Myoglobin's old and new clothes: from molecular structure to function in living cell. J. Exp. Biol. 213 (2010), 2713–2715.
11. Guyton, G.P., Stanek, K.S., Schneider, R.C., Hochachka, P.W., Hurford, W.E., Zapol, D.G., Liggins, G.C., Zapol, W.M., Myoglobin saturation in free-diving Weddell seals. J. Appl. Physiol. 79 (1995), 1148–1155.
12. Hill, R., Oxygen dissociation curves of muscle haemoglobin. Proc. R. Soc. Lond. B 120 (1936), 472–483.
13. Jensen, K.P., Ryde, U., Comparison of the chemical properties of iron and cobalt porphyrins and corrins. ChemBioChem 4 (2003), 413–424.
14. 2: reasons for reversible binding and spin inversion. J. Biol. Chem. 279 (2004), 14561–14569.
15. Kendrew, J.C., Bodo, G., Dintzis, H.M., Parrish, R.G., Wyckoff, H., Phillips, D.C., A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181 (1958), 662–666.
16. Kooyman, G.L., Ponganis, P.J., The physiological basis of diving to depth: birds and mammals. Annu. Rev. Physiol. 60 (1998), 19–32.
17. Krogh, A., The number and the distribution of capillaries in muscle with the calculation of the oxygen pressure necessary for supplying the tissue. J. Physiol. (London) 52 (1919), 409–515.
18. Lin, P.C., Kreutzer, U., Jue, T., Anisotropy and temperature dependence of myoglobin translational diffusion in myocardium: implication for oxygen transport and cellular architecture. Biophys. J. 92 (2007), 2608–2620.
19. Lin, P.C., Kreutzer, U., Jue, T., Myoglobin translational diffusion in rat myocardium and its implication on intracellular oxygen transport. J. Physiol. 578 (2007), 595–603.
20. Masuda, K., Truscott, K., Lin, P.C., Kreutzer, U., Chung, Y., Sriram, R., Jue, T., Determination of myoglobin concentration in blood-perfused tissue. Eur. J. Appl. Physiol. 104 (2008), 41–48.
21. McGuire, B.J., Secomb, T.W., A theoretical model for oxygen transport in skeletal muscle under conditions of high oxygen demand. J. Appl. Physiol. 91 (2001), 2255–2265.
22. Mendez, J., Keys, A., Density and composition of mammalian muscle. Metabolism 9 (1960), 184–188.
23. Mirceta, S., Campbell, K.L., Berenbrink, M., Molecular evolution of myoglobin in small diving mammals. Comp. Biochem. Physiol. A 153 (2009), S98–S99.
24. Nemeth, P.M., Lowry, O.H., Myoglobin levels in individual human skeleton-muscle fibers of different types. J. Histochem. Cytochem. 132 (1984), 1211–1216.
25. Noren, S.R., Williams, T.M., Body size and skeletal muscle myoglobin of cetaceans: adaptations for maximizing dive duration. Comp. Biochem. Physiol. A 126 (2000), 181–191.
26. 2 binding diffusion into red blood cells to ligand pathways in globins” 2008, Springer, Milan, Italy.
27. Ostermann, A., Waschipky, R., Parak, F.G., Nienhaus, G.U., Ligand binding and conformational motions in myoglobin. Nature 404 (2000), 205–208.
28. Papadopoulos, S., Endeward, V., Revesz-Walker, B., Jürgens, K.D., Gros, G., Radial and longitudinal diffusion of myoglobin in single living heart and skeletal muscle cells. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 5904–5909.
29. Perutz, M.F., Mathews, F.S., An X-ray study of azide methaemoglobin. J. Mol. Biol. 21 (1966), 199–207.
30. Ponganis, P.J., Kreutzer, U., Sailasuta, N., Knower, T., Hurd, R., Jue, T., Detection of myoglobin desaturation in Mirounga angustirostris during apnea. Am. J. Physiol. Regul. Integr. Comp. Physiol. 282 (2002), R267–R272.
31. Romero-Herrera, A.E., Lehmann, H., Joysey, K.A., Fridays, A.E., Molecular evolution of myoglobin and the fossil record: a phylogenetic synthesis. Nature 246 (1973), 389–395.
32. Rossi-Fanelli, A., Antonini, E., Studies on the oxygen and carbon monoxide equilibria of human myoglobin. Arch. Biochem. Biophys. 77 (1958), 478–492.
33. Scholander, P.F., Experimental investigation on the respiratory function in diving mammals and birds. Hvalrad. Skr. 22 (1940), 1–131.
34. Scott, E.E., Gibson, Q.H., Olson, J.S., Mapping the pathways for O2 entry into and exit from myoglobin. J. Biol. Chem. 276 (2001), 5177–5188.
35. Springer, B.A., Sligar, S.G., High-level expression of sperm whale myoglobin in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 84 (1987), 8961–8965.
36. Suzuki, T., Imai, K., Evolution of myoglobin CMLS. Cell. Mol. Life Sci. 54 (1998), 979–1004.
37. Tawara, T., On the respiratory pigments of whale(Studies on whale blood II.). Sci. Rep. Whales Res. Inst. 3 (1950), 96–101.
38. Terrados, N., Jansson, E., Sylven, C., Kaijser, L., Is hypoxia a stimulus for synthesis of oxidative enzymes and myoglobin?. J. Appl. Physiol. 68 (1990), 2369–2372.
39. Tilton, R.F., Kuntz, I.D., Petsko, G.A., Cavities in proteins-structure of a metmyoglobin-xenon complex solved to 1.9 A-. Biochemistry 23 (1984), 2849–2857.
40. Varadarajan, R., Szabo, A., Boxer, S.G., Cloning, expression in Escherichia coli, and reconstitution of human myoglobi. Proc. Natl. Acad. Sci. U. S. A. 82 (1985), 5681–5684.
41. Wajcman, H., Kiger, L., Marden, M.C., Structure and function evolution in the superfamily of globins. C. R. Biol. 332 (2009), 273–282.
42. Whitehead, H., Perrin, W., Würsig, B., Thewissen, J., (eds.) Encycl. Mar. Mam., 2002, Academic Press, 1165–1172.
43. Wittenberg, J.B., Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol. Rev. 50 (1970), 559–636.
44. Wittenberg, B.A., Wittenberg, J.B., Transport of oxygen in muscle. Rev. Physiol. 51 (1989), 857–878.
45. Wittenberg, J.B., Wittenberg, B.A., Myoglobin function reassessed. J. Exp. Biol. 206 (2003), 2011–2020.
46. Zaia, J., Annan, R.S., Biemann, K., The correct molecular weight of myoglobin, a common calibrant for mass spectrometry. Rapid Commun. Mass Spectrom. 6 (1992), 32–36.