Plants, humans and hemoglobins

Trends in Plant Science

Volumn 8, Issue 8, 2003, Pages 387-393

  Kundu, Suman ^a   Trent III, James T ^a   Hargrove, Mark S ^a  

^a IOWA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0042194778     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(03)00163-8     Document Type: Review

References (63)

1. Kendrew, J.C. et al. (1958) A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181, 662-666
2. Appleby, C.A. (1984) Leghemoglobins and Rhizobium respiration. Annu. Rev. Plant Physiol. 35, 443-478
3. Bogusz, D. et al. (1988) Functioning haemoglobin genes in non-nodulating plants. Nature 331, 178-180
4. Taylor, E.R. et al. (1994) A cereal haemoglobin gene is expressed in seed and root tissue under anaerobic conditions. Plant Mol. Biol. 24, 853-862
5. Dordas, C. et al. (2003) Plant hemoglobins, nitric oxide, and hypoxic stress. Ann. Bot. 91, 173-178
6. Brunori, M. (2001) Nitric oxide, cytochrome-c oxidase, and myoglobin. Trends Biochem. Sci. 26, 21-23
7. Brunori, M. (2001) Nitric oxide moves myoglobin centre stage. Trends Biochem. Sci. 26, 209-210
8. Wittenberg, J.B. et al. (2002) Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J. Biol. Chem. 277, 871-874
9. Weber, R. and Vinogradov, S. (2001) Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol. Rev. 81, 569-628
10. 2, NO, and CO by electrostatic interactions with the bound ligand. J. Biol. Inorg. Chem. 2, 544-552
11. Perutz, M. et al. (1998) The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annu. Rev. Biophys. Biomol. Struct. 27, 1-34
12. Appleby, C.A. (1962) The oxygen equilibrium of leghemoglobin. Biochim. Biophys. Acta 60, 226-235
13. Imamura, T. and Riggs, A. (1972) Equilibria and kinetics of ligand binding by leghemoglobin from soybean root nodules. J. Biol. Chem. 247, 521-526
14. Wittenberg, J.B. et al. (1972) The kinetics of the reactions of leghemoglobin with oxygen and carbon monoxide. J. Biol. Chem. 247, 527-531
15. Gibson, Q.H. et al. (1989) The kinetics of ligand binding to plant hemoglobins: structural implications. J. Biol. Chem. 264, 100-107
16. Rohlfs, R.J. et al. (1988) A comparison of the geminate recombination kinetics of several monomeric heme proteins. J. Biol. Chem. 263, 1803-1813
17. Wittenberg, J.B. (1965) Myoglobin-facilitated diffusion of oxygen. J. Gen. Physiol. 49, 57-74
18. Wittenberg, J. et al. (1974) Facilitated oxygen diffusion. The role of leghemoglobin in nitrogen fixation by bacteroids isolated from soybean root nodules. J. Biol. Chem. 249, 4057-4066
19. Murray, J. and Wyman, J. (1971) Facilitated diffusion. J. Biol. Chem. 246, 5903-5906
20. Hargrove, M.S. et al. (1997) Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants. J. Mol. Biol. 266, 1032-1042
21. Kundu, S. and Hargrove, M.S. (2003) Distal heme pocket regulation of ligand binding and stability in soybean leghemoglobin. Proteins 50, 239-248
22. Kundu, S. et al. (2002) The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme. Proteins 46, 268-277
23. Antonini, E. and Brunori, M. (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands, North-Holland Publishing Company
24. Olson, J.S. and Phillips, G.N. Jr (1996) Kinetic pathways and barriers for ligand binding to myoglobin. J. Biol. Chem. 271, 17593-17596
25. Barrick, D. et al. (1997) A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin. Nat. Struct. Biol. 4, 78-83
26. Smerdon, S.J. et al. (1993) Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin. Biochemistry 32, 5132-5138
27. Duff, S.M.G. et al. (1997) Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. J. Biol. Chem. 272, 16746-16752
28. 2-binding kinetics of a recombinant protein synthesized in Escherichia coli. Plant Physiol. 115, 1259-1266
29. Trevaskis, B. et al. (1997) Two hemoglobin genes in Arabidopsis thaliana: the evolutionary origins of leghemoglobins. Proc. Natl. Acad. Sci. U. S. A. 94, 12230-12234
30. Hunt, P.W. et al. (2001) Expression and evolution of functionally distinct haemoglobin genes in plants. Plant Mol. Biol. 47, 677-692
31. Arredondo-Peter, R. et al. (1998) Plant hemoglobins. Plant Physiol. 118, 1121-1125
32. Hargrove, M. et al. (2000) Crystal structure of a nonsymbiotic plant hemoglobin. Struct. Fold. Des. 8, 1005-1014
33. Kundu, S. et al. (2003) Direct measurement of equilibrium constants for high-affinity hemoglobins. Biophys. J. 84, 3931-3940
34. Hargrove, M.S. (2000) A flash photolysis method to characterize hexacoordinate hemoglobin kinetics. Biophys. J. 79, 2733-2738
35. Trent, J.T. III et al. (2001) A model for ligand binding to hexacoordinate hemoglobins. Biochemistry 40, 6155-6163
36. Falzone, C.J. et al. (2002) The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state. J. Mol. Biol. 324, 1015-1029
37. Hvitved, A.N. et al. (2001) Ligand binding and hexacoordination in Synechocystis hemoglobin. J. Biol. Chem. 276, 34714-34721
38. Couture, M. et al. (2000) Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket. Eur. J. Biochem. 267, 4770-4780
39. Couture, M. et al. (1999) Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands. J. Biol. Chem. 274, 6898-6910
40. Pesce, A. et al. (2000) A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family. EMBO J. 19, 2424-2434
41. Watts, R. et al. (2001) A hemoglobin from plants homologous to truncated hemoglobins of microorganisms. Proc. Natl. Acad. Sci. U. S. A. 98, 10119-10124
42. Burmester, T. et al. (2002) Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol. Biol. Evol. 19, 416-421
43. Burmester, T. et al. (2000) A vertebrate globin expressed in the brain. Nature 407, 520-523
44. Trent, J.T. III and Hargrove, M.S. (2002) A ubiquitously expressed human hexacoordinate hemoglobin. J. Biol. Chem. 277, 19538-19545
45. Trent, J.T. III et al. (2001) Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen. J. Biol. Chem. 276, 30106-30110
46. Awenius, C. et al. (2001) Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis. Biochem. Biophys. Res. Commun. 287, 418-421
47. Hankeln, T. et al. (2002) Characterization of Drosophila hemoglobin. Evidence for hemoglobin-mediated respiration in insects. J. Biol. Chem. 277, 29012-29017
48. Feldman, P.L. et al. (1993) The surprising life of nitric oxide. Chem. Eng. News 20, 26-38
49. Doherty, D. et al. (1998) The rate of reaction with NO determines the hypertensive effect of cell-free hemoglobin. Nat. Biotechnol. 16, 672-676
50. Flogel, U. et al. (2001) Myoglobin: a scavenger of bioactive NO. Proc. Natl. Acad. Sci. U. S. A. 98, 735-740
51. Bowles, D.J. (1990) Defense-related proteins in higher plants. Annu. Rev. Biochem. 59, 873-907
52. Delledonne, M. et al. (1998) Nitric oxide functions as a signal in plant disease resistance. Nature 394, 585-588
53. Fukuto, J. and Wink, D. (1999) Nitric oxide (NO): formation and biological roles in mammalian systems. Met. Ions Biol. Syst. 36, 547-595
54. Sun, Y. et al. (2001) Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemia injury. Proc. Natl. Acad. Sci. U. S. A. 98, 15306-15311
55. Hendriks, T. et al. (1998) A nonsymbiotic hemoglobin gene is expressed during somatic embryogenesis in Cichorium. Biochim. Biophys. Acta 1443, 193-197
56. Helleboid, S. et al. (2000) Three major somatic embryogenesis related proteins in Cichorium identified as PR proteins. J. Exp. Bot. 51, 1189-1200
57. Herbers, K. et al. (1996) Salicylic acid-independent induction of pathogenesis-related protein transcripts by sugars is dependent on leaf developmental stage. FEBS Lett. 397, 239-244
58. Lorberth, R. et al. (1992) Promoter elements involved in environmental and developmental control of potato proteinase inhibitor II expression. Plant J. 2, 477-486
59. Delledonne, M. et al. (2001) Signal interactions between nitric oxide and reactive oxygen species intermediates in the plant hypersensitive disease resistance response. Proc. Natl. Acad. Sci. U. S. A. 98, 13454-13459
60. Gardner, P.R. et al. (2001) Dioxygen dependent metabolism of nitric oxide in mammalian cells. Free Radical Biol. Med. 31, 191-204
61. Gardner, P.R. et al. (1998) Nitric oxide dioxygenase: an enzymatic function for flavohemoglobin. Proc. Natl. Acad. Sci. U. S. A. 95, 10378-10383
62. Geuens, E. et al. A globin in the nucleus! J. Biol. Chem. (in press)
63. Seregelyes, C. et al. (2000) Nuclear localization of a hypoxia-inducible novel non-symbiotic hemoglobin in cultured alfalfa cells. FEBS Lett 482, 125-130