The spontaneous hemin release form Lumbricus terrestris hemoglobin

Comparative Biochemistry and Physiology - A Physiology

Volumn 118, Issue 4, 1997, Pages 1241-1245

  Smith, M L ^a,d   Paul, J ^b   Ohlsson, P I ^c   Paul, K G ^c  

^a 2330 South Industrial Park   (United States)

^b BILKENT UNIVERSITY   (Turkey)

^c UMEÅ UNIVERSITY   (Sweden)

^d Chuparosa Research   (United States)

Author keywords

Carbon monoxide; Earthworm; Hemin; Hemin transfer; Hemoglobin; Infrared; Lumbricus terrestris; Protein dynamics; Protein stability

Indexed keywords

CARBON MONOXIDE; HEMIN;

ARTICLE; BETA CHAIN; EARTHWORM; EFFECTOR CELL; ENZYME ACTIVITY; ERYTHROCYTE MEMBRANE; NONHUMAN; OXYGEN TRANSPORT; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN TRANSPORT;

EID: 0031415597     PISSN: 03009629     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9629(97)00224-7     Document Type: Article

References (20)

1. Bunn, H.F.; Forget, B.G. Hemoglobin: Molecular, Genetic and Clinical Aspects. Philadelphia, PA: W.B. Saunders Company; 1986:573-587.
2. Darawshe, S.; Tsafadyah, Y.; Daniel, E. Quaternary structure of erythrocruorin from the nemotode Ascaris suum. Evidence for unsaturated haem-binding sites. Biochem. J. 242:689-694; 1987.
3. Feigelson, P.; Greengard, O. A microsomal iron-porphyrin activator of rat liver tryptophan pyrrolase. J. Biol. Chem. 236: 153-157;1961.
4. Hargrove, M.S.; Barrick, D.; Olson, J.S. The association rate constant for heme binding to globin is independent of protein structure. Biochemistry 35:11293-11299;1966.
5. Hendrickson, W.A.; Royer, W.E., Jr. Principles in the assembly of annelid erythrocruorins. Biophys. J. 49:177-189;1986.
6. Igarashi, Y.; Kimura, K.; Kajita, A. Calcium-dependent allosteric modulation of the giant hemoglobin from the terrestrial oligochate, Eisenia foetida. Biochem. Int. 10:611-618;1985.
7. Nagel, R.L.; Ranney, H.M. Drug induced oxidative denaturation of hemoglobin. Sem. Hematol. X:269-78;1973.
8. Ochiai, T. Dissociation and oxygen equilibrium properties of earthworm hemoglobin. Arch. Biochem. Biophys. 226:111-117;1983.
9. Ochiai, T.; Hoshina, S.; Usuki, I. Zinc as modulator of oxygenation function and stabilizer of quaternary structure in earthworm hemoglobin. Biochim. Biophys. Acta 1203:310-314;1993.
10. O'Keeffe, D.H.; Ebel, R.E.; Peterson, J.A.; Maxwell, J.C.; Caughey, W.S. An infrared spectroscopic study of carbon monoxide bonding to ferrous cytochrome P-450. Biochemistry 17:5845-5852;1978.
11. Ownby, D.W.; Zhu, H.; Schneider, K.; Beavis, R.C.; Chiat, B.T.; Riggs, A.F. The extracellular hemoglobin of the earthworm Lumbricus terrestris. Determination of subunit stoichiometry. J. Biol. Chem. 268:13539-13547;1993.
12. Potter, W.T.; Hazzard, J.H.; Choc, M.G.; Tucker, M.P.; Caughey, W.S. Infrared spectra of carbonyl hemoglobins: Characterization of dynamic heme pocket conformers. Biochemistry 29:6283-6295;1990.
13. Royer, W.E., Jr.; Hendrickson, W.A. Molecular symmetry of Lumbricus erythrocruorin. 263:13762-13765;1988.
14. Smith, M.L.; Hjortsberg, K.; Roméo, P.H.; Rosa, J.; Paul, K.G. Mutant hemoglobin stability depends upon location and nature of single point mutation. FEBS Lett. 169:147-150;1984.
15. Smith, M.L.; Paul, J.; Hjortsberg, K.; Ohlsson, P.I.; Paul, K.G. Hemeprotein fission under nondenaturing conditions. Proc. Nat. Acad. Sci. USA 88:882-886;1991.
16. Smith, M.L.; Paul, J.; Ohlsson, P.I.; Paul, K.G. Correlation between reduction potential, CO stretch frequency and CO half-bandwidth in hemoproteins. Biochemistry 23:6776-6785:1984.
17. Uuno, R.; Shimizu, T.; Kondo, K.; Hayaishi, O. Activation mechanism of prostaglandin synthetase by hemoproteins. J. Biol. Chem. 257:5584-5588:1982.
18. Vinogradov, S.N.; Sharma, P.K.; Qabar, A.N.; Wall, J.S.; Westrick, J.A.; Simmons, J.H.; Gill, S.J. A dodecamer of globin chains is the principal functional subunit of the extracellular hemoglobin of Lumbricus terrestris. J. Biol. Chem. 266: 13091-13096;1991.
19. Wallace, W.J.; Maxwell, J.C.; Caughey, W.S. A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes. Biochem. Biophys. Res. Comm. 57:1104-1110;1974.
20. Zhu, H.; Hargrove, M.; Xie, Q.; Nozaki, Y.; Linse, K.; Smith, S.S.; Olson, J.S.; Riggs, A.F. Stoichiometry of subunits and heme content of hemoglobin from the earthworm Lumbricus terrestris. J. Biol. Chem. 271:29999-30006;1996.