Microbial globins

Advances in Microbial Physiology

Volumn 47, Issue , 2003, Pages 255-310

  Wu, Guanghui ^a   Wainwright, Laura M ^a   Poole, Robert K ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; FLAVOHEMOGLOBIN; FLAVOPROTEIN; GLOBIN; HEME DERIVATIVE; HEMOGLOBIN; HEMOPROTEIN; MYOGLOBIN; NITRIC OXIDE; OXYGEN; PEROXIDASE; PROTEIN VGB; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ALPHA HELIX; BACTERIAL GROWTH; BACTERIAL METABOLISM; BACTERIUM MUTANT; BINDING SITE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; EUKARYOTE; HOST PATHOGEN INTERACTION; LIGAND BINDING; MICROORGANISM; NITROSATION; NONHUMAN; OXIDATIVE STRESS; OXYGEN TRANSPORT; PHENOTYPE; PLANT; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; REVIEW; STRESS; TRANSCRIPTION REGULATION; VITREOSCILLA; YEAST;

ANIMALIA; BACTERIA (MICROORGANISMS); EUKARYOTA; NEGIBACTERIA; VITREOSCILLA;

EID: 0141449046     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2911(03)47005-7     Document Type: Review

References (163)

1. Andersson, C.I., Holmberg, N., Farres, J., Bailey, J.E., Bulow, L. and Kallio, P.T. (2000) Error-prone PCR of Vitreoscilla hemoglobin (VHb) to support the growth of microaerobic Escherichia coli. Biotechnol. Bioeng. 70, 446-455.
2. Andersson, C.R., Jensen, E.O., Llewellyn, D.J, Dennis, E.S. and Peacock, W.J. (1996) A new hemoglobin gene from soybean: a role for hemoglobin in all plants. Proc. Natl. Acad. Sci. USA 93, 5682-5687.
3. + reductases. FEBS Lett. 302, 247-252.
4. Anjum, M.F., Ioannidis, N. and Poole, R.K. (1998) Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli. FEMS Microbiol. Lett. 166, 219-223.
5. Appleby, C.A. (1984) Leghemoglobin and Rhizobium respiration. Ann. Rev. Plant. Physiol. 35, 443-478.
6. Ascenzi, P., Salvati, L. and Brunori, M. (2001) Does myoglobin protect Trypanosoma cruzi from the antiparasitic effects of nitric oxide? FEBS Lett. 501, 103-105.
7. Bailey, J.E., Shurlati, A., Hatzimanikatis, V., Lee, K., Renner, W.A. and Tsai, P.S. (1996) Inverse metabolic engineering: a strategy for directed genetic engineering of useful phenotypes. Biotech. Bioeng. 52, 109-121.
8. Bollinger, C.J., Bailey, J.E. and Kallio, P.T. (2001) Novel hemoglobins to enhance microaerobic growth and substrate utilization in Escherichia coli. Biotechnol. Prog. 17, 798-808.
9. Bolognesi, M., Boffi, A., Coletta, M., Mozzarelli, A., Pesce, A., Tarricone, C. and Ascenzi, P. (1999) Anticooperative ligand binding properties of recombinant ferric Vitreoscilla homodimeric hemoglobin: a thermodynamic, kinetic and X-ray crystallographic study. J. Mol. Biol. 291, 637-650.
10. Bonamore, A., Chiancone, E. and Boffi, A. (2001) The distal heme pocket of Escherichia coli flavohemoglobin probed by infrared spectroscopy. Biochim. Biophys. Acta. 1549, 174-178.
11. Brunori, M. (2001) Nitric oxide, cytochrome-c oxidase and myoglobin. TIBS 26, 21-23.
12. Buisson, N. and Labbe-Bois, R. (1998) Flavohemoglobin expression and function in Saccahromyces cerevisiae. No relationship with respiration and complex response to oxidative stress. J. Biol. Chem. 273, 9527-9533.
13. Burmester, T., Weich, B., Reinhardt, S. and Hankeln, T. (2000) A vertebrate globin expressed in the brain. Nature 407, 520-523.
14. Cole, S.T., Elglmeler, K., Parkhill, J., James, K.D., Thomson, N.R., Wheeler, P.R., Honoré, N., Garnler, T., Churcher, C., Harris, D., Mungall, K., Basham, D., Brown, D., Chillingworth, T., Connor, R., Davies, R.M., Devlin, K., Duthoy, S., Feltwell, T., Fraser, A., Hamlin, N., Holroyd, S., Hornsby, T., Jagels, K., Lacroix, C., Maclean, J., Moule, S., Murphy, L., Oliver, K., Quail, M.A., Rajandream, M.-A., Rutherford, K.A., Rutter, S., Seeger, K., Simon, S., Simmonds, M., Skelton, J., Squares, R., Squares, S., Stevens, K., Taylor, K., Whitehead, S., Woodward, J.R. and Barrell, B.G. (2001) Massive gene decay in the leprosy bacillus. Nature 409, 1007-1011.
15. Couture, M., Chamberland, H., St-Pierre, B., Lafontaine, J. and Guertin, M. (1994) Nuclear genes encoding chloroplast hemoglobins in the unicellular green alga Chlamydomonas eugametos. Mol. Gen. Genet. 243, 185-197.
16. Couture, M., Das, T.K., Lee, H.C., Peisach, J., Rousseau, D.L., Wittenberg, B.A., Wittenberg, J.B. and Guertin, M. (1999a) Chlamydomonas chloroplast ferrous hemoglobin: heme pocket structure and reactions with ligands. J. Biol. Chem. 274, 6898-6910.
17. Couture, M., Das, T.K., Savard, P.Y., Ouellet, Y., Wittenberg, J.B., Wittenberg, B.A., Rousseau, D.L. and Guertin, M. (2000) Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket. Eur. J. Biochem. 267, 4770-4780.
18. Couture, M., Yeh, S.R., Wittenberg, B.A., Wittenberg, J.B, Ouellet, Y., Rousseau, D.L. and Guertin, M. (1999b) A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 96, 11223-11228.
19. Cramm, R., Siddiqui, R.A. and Friedrich, B. (1994) Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus. J. Biol. Chem. 269, 7349-7354.
20. Crawford, M.J. and Goldberg, D.E. (1998a) Role for the Salmonella flavohemoglobin in protection from nitric oxide. J. Biol. Chem. 273, 12543-12547.
21. Crawford, M.J. and Goldberg, D.E. (1998b) Regulation of the Salmonella typhimurium flavohemoglobin gene - a new pathway for bacterial gene expression in response to nitric oxide. J. Biol. Chem. 273, 34028-34032.
22. Crawford, M.J. and Goldberg, D. (1999) Correction. Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide. J Biol Chem 274, 3918.
23. Crawford, M.J., Sherman, D.R. and Goldberg, D.E (1995) Regulation of Saccharomyces cerevisiae flavohemoglobin gene expression. J. Biol. Chem. 270, 6991-6996.
24. Cross, R., Aish, J., Paston, S.J., Poole, R.K. and Moir, J.W.B. (2000) Cytochrome c′ from Rhodobacter capsulatus confers increased resistance to nitric oxide. J. Bacteriol. 182, 1442-1447.
25. Cross, R., Lloyd, D., Poole, R.K. and Moir, J.W.B. (2001) Enzymatic removal of nitric oxide catalyzed by cytochrome c′ in Rhodobacter capsulatus. J. Bacteriol. 183, 3050-3054.
26. Cruz-Ramos, H., Crack, J., Wu, G., Hughes, M.N., Scott, C., Thomson, A.J., Green, J. and Poole, R.K. (2002) NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp. EMBO J. 21, 3235-3244.
27. Das, T.K., Couture, M., Lee, H.C., Peisach, J., Rousseau, D.L., Wittenberg, B.A., Wittenberg, J.B. and Guertin, M. (1999) Identification of ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the heme. Biochemistry 38, 15360-15368.
28. 2 stretching modes in oxyhemoglobins. Proc. Natl. Acad. Sci. USA 98, 479-484.
29. Das, T.K., Weber, R.E., Dewilde, S., Wittenberg, J.B., Wittenberg, B.A., Yamauchi, K., Van Hauwart, M.L., Moens, L. and Rousseau, D.L. (2000) Ligand binding in the ferric and ferrous states of Paramecium hemoglobin. Biochemistry 39, 14330-14340.
30. Denariaz, G., Ketchum, P.A., Payne, W.J., Liu, M.Y., Legall, J., Moura, I. and Moura, J.J. (1994) An unusual hemoprotein capable of reversible binding of nitric oxide from the gram-positive Bacillus halodenitrificans. Arch. Microbiol. 162, 316-322.
31. Dikshit, K.L., Dikshit, R.P. and Webster, D.A. (1990) Study of Vitreoscilla globin (vgb) gene expression and promoter activity in E. coli through transcriptional fusion. Nucl. Acid. Res. 18, 4149-4155.
32. Dikshit, K.L., Orii, Y., Navani, N., Patel, S., Huang, H.Y., Stark, B.C. and Webster, D.A. (1998) Site-directed mutagenesis of bacterial hemoglobin: the role of glutamine (E7) in oxygen-binding in the distal heme pocket. Arch Biochem Biophys 349, 161-166.
33. Dikshit, K.L., Spaulding, D., Braun, A. and Webster, D.A. (1989) Oxygen inhibition of globin gene transcription and bacterial haemoglobin synthesis in Vitreoscilla. J. Gen. Microbiol. 135, 2601-2609.
34. Dikshit, R.P., Dikshit, K.L., Liu, Y.X. and Webster, D.A. (1992) The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases. Arch. Biochem. Biophys. 293, 241-245.
35. Dikshit, K.L. and Webster, D.A. (88) Cloning, characterization and expression of the bacterial gene from Vitreoscilla in Escherichia coli. Gene 70, 377-386.
36. Eriksson, S., Lucchini, S., Thompson, A., Rhen, M. and Hinton, J.C.D. (2003) Unraveling the biology of macrophage infection by gene expression profiling of intracellular Salmonella enterica. Mol. Microbiol. 47, 103-118.
37. Ermler, U., Siddiqui, R.A., Cramm, R. and Friedrich, B. (1995b) Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 angstrom resolution. EMBO J 14, 6067-6077.
38. Ermler, U., Siddiqui, R.A., Cramm, R., Schroder, D. and Friedrich, B. (1995a) Crystallization and preliminary X-ray diffraction studies of a bacterial flavohemoglobin protein. Prot. Struct. Funct. Genet. 21, 351-353.
39. Eschenbrenner, M., Coves, J. and Fontecave, M. (1994) Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein. Biochem Biophys Res Comm 198, 127-131.
40. Falzone, C.J., Christie, Vu B., Scott, N.L. and Lecomte, J.T.J. (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.
41. Favey, S., Labesse, G., Vouille, V. and Boccara, M. (1995) Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937. Microbiology 141, 863-871.
42. Frey, A.D., Bailey, J.E. and Kallio, P.T. (2000) Expression of Alcaligenes eutrophus flavohemoprotein and engineered Vitreoscilla hemoglobin-reductase fusion protein for improved hypoxic growth of Escherichia coli. Appl Environ Microbiol 66, 98-104.
43. Frey, A.D., Farres, J., Bollinger, C.J.T. and Kallio, P.T. (2002) Bacterial hemoglobins and flavohemoglobins for alleviation of nitrosative stress in Escherichia coli. Appl. Environ. Microbiol. 68, 4835-4840.
44. Gagné, G. and Guertin, M. (1992) The early genetic response to light in the green unicellular alga Chlamydomonas eugametos grown under light dark cycles involves genes that represent direct responses to light and photosynthesis. Plant Molec. Biol. 18, 429-445.
45. Gardner, A.M. and Gardner, P.R. (2002) Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity. J. Biol. Chem. 277, 8166-8171.
46. Gardner, A.M., Martin, L.A., Gardner, P.R., Dou, Y. and Olson, J.S. (2000a) Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin) - the B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis. J. Biol. Chem. 275, 12581-12589.
47. Gardner, P.R., Costantino, G. and Salzman, A.L. (1998b) Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase. J. Biol. Chem. 273, 26528-26533.
48. Gardner, P.R., Gardner, A.M., Martin, L.A. and Salzman, A.L. (1998a) Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Proc. Nat. Acad. Sci. USA 95, 10378-10383.
49. Gardner, P.R., Gardner, A.M., Martin, L.A., Dou, Y., Li, T.S., Olson, J.S., Zhu, H. and Riggs, A.F. (2000b) Nitric-oxide dioxygenase activity and function of flavohemoglobins - sensitivity to nitric oxide and carbon monoxide inhibition. J. Biol. Chem. 275, 31581-31587.
50. Giangiacomo, L., Mattu, M., Arcovito, A., Bellenchi, G., Bolognesi, M., Ascenzi, P. and Boffi, A. (2001) Monomer-dimer equilibrium and oxygen binding properties of ferrous Vitreoscilla hemoglobin. Biochemistry 40, 9311-9316.
51. Gonzales-Prevatt, V. and Webster D.A. (1980) Purification and properties of NADH-cytochrome o Reductase from Vitreoscilla. J. Biol. Chem. 255, 1478-1482.
52. Green, J., Scott, C. and Guest, J.R. (2001) Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. In: Poole R. K. (ed.) Advances in Microbial Physiology, Vol 44. 1-34. Academic Press, London.
53. Hardison, R.C. (1996) A brief history of hemoglobins: plant, animal, protist, and bacteria. Proc. Natl. Acad. Sci. USA 93, 5675-5679.
54. Hausladen, A., Gow, A.J. and Stamler, J.S. (2001) Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen. Proc. Natl. Acad. Sci. USA 98, 10108-10112.
55. Hausladen, A., Gow, A.J. and Stamler, J.S. (1998) Nitrosative stress: metabolic pathway involving the flavohemoglobin. Proc. Natl. Acad. Sci. USA 95, 14100-14105.
56. Hill, D.R., Belbin, T.J., Thorsteinsson, M.V., Bassam, D., Brass, S., Ernst, A., Böger, P., Paerl, H., Mulligan, M.E. and Potts, M. (1996) GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp. J. Bacteriol. 178, 6587-6598.
57. Hu, Y., Butcher, P.D., Mangan, J.A., Rajandream, M.-A and Coates, A.R.M. (1999) Regulation of hmp gene transcription in Mycobacterium: effects of oxygen limitation and nitrosative and oxidative stress. J. Bacteriol. 181, 3486-3493.
58. Hvitved, A.N., Trent, J.T., Premer, S.A. and Hargrove, M.S. (2001) Ligand binding and hexacoordination in Synechocystis hemoglobin. J. Biol. Chem. 276, 34714-34712.
59. Iijima, M., Shimizu, H., Tanaka, Y. and Urushihara, H. (2000) Identification and characterization of two flavohemoglobin genes in Dictyostelium discoideum. Cell Struct. Funct. 25, 47-55.
60. Ilari, A., Bonamore, A., Farina, A., Johnson, K.A. and Boffi, A. (2002) The X-ray structure of ferric Escherichia coli flavohaemoglobin reveals an unexpected geometry of the distal heme pocket. J. Biol. Chem. 277, 23725-23732.
61. Ioannidis, N., Cooper, C.E. and Poole, R.K. (1992) Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem. J. 288, 649-655.
62. Jakob, W., Webster, D.A. and Kroneck, P.M. (1992) NADH-dependent methemoglobin reductase from the obligate aerobe Vitreoscilla: improved method of purification and reexamination of prosthetic groups. Arch Biochem Biophys 292, 29-33.
63. Joshi, M. and Dikshit, K.L. (1994) Oxygen dependent regulation of Vitreoscilla globin gene: evidence for positive regulation by FNR. Biochem. Biophys. Res. Commun. 202, 535-542.
64. Joshi, M.S., Ferguson, T.B., Han, T.H., Hyduke, D.R., Liao, J.C., Rassaf, T., Bryan, N., Feelisch, M. and Lancaster, J.R. (2002) Nitric oxide is consumed, rather than conserved, by reaction with oxyhemoglobin under physiological conditions. Proc. Natl. Acad. Sci. USA 99, 10341-10346.
65. Kallio, P.T., Tsai, P.S. and Bailey, J.E. (1996) Expression of Vitreoscilla hemoglobin is superior to horse heart myoglobin or yeast flavohemoglobin expression for enhancing Escherichia coli growth in a microaerobic bioreactor. Biotechnol Prog 12, 751-757.
66. Kaur, R., Pathania, R., Sharma, V., Mande, S.C. and Dikshit, K.L. (2002) Chimeric Vitreoscilla hemoglobin (VHb) carrying a flavoreductase domain relieves nitrosative stress in Escherichia coli: new insight into the functional role of VHb. Appl. Environ. Microbiol. 68, 152-160.
67. Keilin, D. (1953) Haemoglobin in fungi. Occurrence of haemoglobin in yeast and the supposed stabilization of the oxygenated cytochrome oxidase. Nature 172, 390-393.
68. Keilin, D. and Ryley, J.F. (1953) Haemoglobin in protozoa. Nature 172, 451.
69. Keilin, D. and Tissieres, A. (1953) Haemoglobin in moulds: Neurospora crassa and Penicillium notatum. Nature 172, 393-394.
70. Khosla, C. and Bailey, J.E. (1989b) Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli. J. Bacteriol. 171, 5990-6004.
71. Khosla, C., Curtis, J.E., DeModena, J., Rinas, U. and Bailey, J.E. (1990) Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli. Biotechnology 8, 849-853.
72. Khosla, C. and Bailey, J.E. (1988a) The Vitreoscilla hemoglobin gene: molecular cloning, nucleotide sequence and genetic expression in Escherichia coli. Mol. Gen. Genet. 214: 158-161.
73. Khosla, C. and Bailey, J.E. (1988b) Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli. Nature 331, 633-635.
74. Khosla, C. and Bailey, J.E. (1989a) Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli - implications for protein function. J. Mol. Biol. 210, 79-89.
75. Kiley, P.J. and Beinert, H. (1999) Oxygen sensing by the global regulator, FNR, the role of the iron-sulfur cluster. FEMS Microbiol. Rev. 22, 341-352.
76. Kim, S.O., Orii, Y., Lloyd, D., Hughes, M.N. and Poole, R.K. (1999) Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide. FEBS Lett. 445, 389-394.
77. Kobayashi, G., Nakamura, T., Ohmachi, H., Matsuoka, A., Ochiai, T. and Shikama, K. (2002) Yeast flavohemoglobin from Candida norvegensis. Its structural, spectral, and stability properties. J. Biol. Chem. 277, 42540-42548.
78. Kroneck, P.M., Jakob, W., Webster, D.A. and DeMaio, R. (1991) Studies on the bacterial hemoglobin from Vitreoscilla. Redox properties and spectroscopic characterization of the different forms of the hemoprotein. Biol Met 4, 119-125.
79. Lacelle, M., Kumano, M., Kurita, K., Yamane, K., Zuber, P. and Nakano, M.M. (1996) Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis. J. Bacteriol. 178, 3803-3808.
80. Lebioda, L. (2000) The honorary enzyme haemoglobin turns out to be a real enzyme. Cell Mol. Life Sci. 57, 1817-1819.
81. Lebioda, L., LaCount, M.W., Zhang, E.L., Chen, Y.P., Han, K.P., Whitton, M.M., Lincoln, D.E. and Woodin, S.A. (1999) An enzymatic globin from a marine worm. Nature 401, 445.
82. Lecomte, J.T.J., Scott, N.L., Vu, C. and Falzone, C.J. (2001) Binding of ferric heme by the recombinant globin from the cyanobacterium Synechocystis sp. PCC 6803. Biochem. 40, 6541-6552.
83. Liu, L.M., Zeng, M., Hausladen, A., Heitman, J. and Stamler, J.S. (2000) Protection from nitrosative stress by yeast flavohemoglobin. Proc. Natl. Acad. Sci. USA 97, 4672-4676.
84. Liu, L.M., Zeng, M., Hausladen, A., Heitman, J. and Stamler, J.S. (2000) Protection from nitrosative stress by yeast flavohemoglobin. Proc. Natl. Acad. Sci. USA 97, 4672-4676.
85. Macheroux, P., Hill, S., Austin, S., Eydmann, T., Jones, T., Kim, S.-O., Poole, R.K. and Dixon, R. (1998) Electron donation to the flavoprotein NifL, a redox-sensing transcriptional regulator. Biochem. J. 332, 413-419.
86. MacMicking, J.D., North, R.J., LaCourse, R., Mudgett, J.S., Shah, S.K. and Natan, C.F. (1997) Identification of nitric oxide as a protective locus against tuberculosis. Proc. Natl. Acad. Sci. USA 94, 5243-5248.
87. Membrillo-Hernández, J., Cook, G.M. and Poole, R.K. (1997) Roles of RpoS (sigma(s)), IHF and ppGpp in the expression of the hmp gene encoding the flavohemoglobin (Hmp) of Escherichia coli K-12. Mol. Gen. Genet. 254, 599-603.
88. Membrillo-Hernández, J., Coopamah, M.D., Anjum, M.F., Stevanin, T.M., Kelly, A., Hughes, M.N. and Poole, R.K. (1999) The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a "nitric oxide releaser," and paraquat and is essential for transcriptional responses to oxidative stress. J. Biol. Chem. 274, 748-754.
89. Membrillo-Hernández, J., Coopamah, M.D., Channa, A., Hughes, M.N. and Poole, R.K. (1998) A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. Mol. Microbiol. 29, 1101-1112.
90. Membrillohernandez, J., Ioannidis, N. and Poole, R.K. (96) The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo. FEBS Lett. 382, 141-144.
91. Milani, M., Pesce, A., Bolognesi, M. and Ascenzi, P. (2001a) Truncated hemoglobins: trimming the classical "three-over-three" globin fold to a minimal size. Biochem. Molec. Biol. Edu. 29, 123-125.
92. 2 diffusion to the heme. EMBO J. 20, 3902-3909.
93. Mills, C.E., Sedelnikova, S., Soballe, B., Hughes, M.N. and Poole, R.K. (2001) Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide. Biochem. J. 353, 207-213.
94. Minning, D.M., Gow, A.J., Bonaventura, J., Braun, R., Dewhirst, M., Goldberg, D.E. and Stamler, J.S. (1999) Ascaris haemoglobin is a nitric oxide-activated 'deoxygenase'. Nature 401, 497-502.
95. Moens, L., Vanfleteren, J., Vandepeer, Y., Peeters, K., Kapp, O., Czeluzniak, J., Goodman, M., Blaxter, M. and Vinogradov, S. (1996) Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships. Mol. Biol. Evol. 13, 324-333.
96. Mukai, M., Savard, P.Y., Ouellet, H., Guertin, M. and Yeh, S.-R. (2002) Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis. Biochemistry 41, 3897-3905.
97. Mukai, M., Mills, C.E., Poole, R.K. and Yeh, S.R. (2001) Flavohemoglobin, a globin with a peroxidase-like catalytic site. J. Biol. Chem. 276, 7272-7277.
98. Nakano, M.M. (2002) Induction of ResDE-dependent gene expression in Bacillus subtilis in response to nitric oxide and nitrosative stress. J. Bacteriol. 184, 1783-1787.
99. Nie, X. and Hill, R.D. (1997) Mitochondrial respiration and hemoglobin gene expression in barley aleurone tissue. Plant Physiol 114, 835-840.
100. Ollesch, G., Kaunzinger, A., Juchelka, D., SchubertZsilavecz, M. and Ermler, U. (1999) Phospholipid bound to the flavohemoprotein from Alcaligenes eutrophus. Eur. J. Biochem. 262, 396-405.
101. Orii, Y. and Webster, D.A. (1986) Photodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation. J. Biol. Chem. 261, 3544-3547.
102. Oshino, R., Asakura, T., Takio, K., Oshino, N., Chance, B. and Hagihara, B. (1973b) Purification and molecular properties of yeast hemoglobin. Eur J Biochem 39, 581-590.
103. Oshino, R., Asakura, T., Tamura, M., Oshino, N. and Chance, B. (1972) Yeast hemoglobin-reductase complex. Biochem. Biophys. Res. Commun. 46, 1055-1060.
104. Oshino, R., Oshino, N. and Chance, B. (1971) The oxygen equilibrium of yeast hemoglobin. FEBS Lett. 19, 96-100.
105. Oshino, R., Oshino, N., Chance, B. and Hagihara, B. (1973a) Studies on yeast hemoglobin. The properties of yeast hemoglobin and its physiological function in the cell. Eur. J. Biochem. 35, 23-33.
106. Ouellet, H., Ouellet, Y., Richard, C., Labarre, M., Wittenberg, B.A., Wittenberg, J.B. and Guertin, M. (2002) Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide. Proc. Natl. Acad. Sci. USA. 99, 5902-5907.
107. Park, K.W., Kim, K.J., Howard, A.J., Stark, B.C. and Webster, D.A. (2002) Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases. J. Biol. Chem. 277, 33334-33337.
108. Pathania, R., Navani, N.K., Gardner, A.M., Gardner, P.R. and Dikshit, K.L. (2002b) Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli. Molec. Microbiol. 45(5), 1303-1314.
109. Pathania, R., Navani, N.K., Rajamohan G. and Dikshit, K.L. (2002a) Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli. J. Biol. Chem. 277, 15293-15302.
110. Perutz, M. (1986) A bacterial haemoglobin. Nature 322, 405.
111. Pesce, A., Couture, M., Dewilde, S., Guertin, M., Yamauchi, K., Ascenzi, P., Moens, L. and Bolognesi, M. (2000) A novel two-over-two α-helical sandwich fold is characterstic of the truncated hemoglobin family. EMBO J 19, 2424-2434.
112. Pomposiello, P.J., Bennik, M.H.J. and Demple, B. (2001) Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J. Bacteriol. 183, 3890-3902.
113. Poole, R.K. (1983) Bacterial cytochrome oxidases. A structurally and functionally distinct group of electron transfer proteins. Biochim. Biophys. Acta 726, 205-243.
114. Poole, R.K. (1988) Bacterial cytochrome oxidases. In: Anthony C (ed.) Bacterial Energy Transduction, pp 231-291. Academic Press, London.
115. Poole, R.K., Rogers, N.J., D'mello, R.A.M., Hughes, M.N. and Orii, Y. (1997) Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen. Microbiology 143, 1557-1565.
116. Poole, R.K. (1994) Oxygen reactions with bacterial oxidases and globins: binding, reduction and regulation. Ant. van Leeuw. Int. J. Gen. Mol. Microbiol. 65, 289-310.
117. Poole, R.K. and Cook, G.M. (2000) Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation In: Poole, R.K. (ed.) Advances in Microbial Physiology. Vol. 43 pp. 165-224, Academic Press, London
118. Poole, R.K. and Hughes, M.N. (2000) New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress. Mol. Microbiol. 36, 775-783.
119. Poole, R.K., Anjum, M.F., Membrillo-Hernández, J., Kim, S.O., Hughes, M.N. and Stewart, V. (1996b) Nitric oxide, nitrite, and fnr regulation of hmp (Flavohemoglobin) gene expression in Escherichia coli K-12. J. Bacteriol. 178, 5487-5492.
120. Poole, R.K., D'mello, R., Hill, S., Ioannidis, N., Leung, D. and Wu, G.H. (1994a) The oxygen reactivity of bacterial respiratory haemoproteins: oxidases and globins. Biochim. Biophys. Acta 1187, 226-231.
121. Poole, R.K., Ioannidis, N. and Orii, Y. (1994b) Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing. Proc. Roy. Soc. Lond. Ser. B Biol. Sci. 255, 251-258.
122. Poole, R.K., Ioannidis, N. and Orii, Y. (1996a) Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH and near-micromolar oxygen: oxygen affinity of NADH oxidase activity. Microbiology 142, 1141-1148.
123. Potts, M., Angeloni, S.V., Ebel, R.E. and Bassam, D. (1992) Myoglobin in a cyanobacterium. Science 256, 1690-1692.
124. Probst, I. and Schlegel, H.G. (1976) Respiratory components and oxidase activities in Alcaligenes eutrophus. Biochim. Biophys. Acta 440, 412-428.
125. Probst, I., Wolf, G. and Schlegel, H.G. (1979) An oxygen-binding flavohemoprotein from Alcaligenes eutrophus. Biochim. Biophys. Acta 576, 471-478.
126. Ramandeep, Hwang, K.W., Raje, M., Kim, K.J., Stark, B.C., Dikshit, K.L. and Webster, D.A. (2001) Vitreoscilla hemoglobin. Intracellular localization and binding to membranes. J. Biol. Chem. 276, 24781-24789.
127. Roos, V., Andersson, C.I., Arfvidsson, C., Wahlund, K.G. and Bulow, L. (2002) Expression of double Vitreoscilla hemoglobin enhances growth and alters ribosome and tRNA levels in Escherichia coli. Biotech Prog 18, 652-656.
128. Santana, M.A., PihakaskiMaunsbach, K., Sandal, N., Marcker, K.A. and Smith, A.G. (1998) Evidence that the plant host synthesizes the heme moiety of leghemoglobin in root nodules. Plant Physiol. 116, 1259-1269.
129. Sartori, G., Aldegheri, L., Mazzotta, G., Lanfranchi, G., Tournu, H., Brown, A.J.P. and Carignani, G. (1999) Characterization of a new hemoprotein in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 274, 5032-5037.
130. Savage, D.C. (1977) Microbial ecology of the gastrointestinal tract. Ann. Rev. Microbiol. 31, 107-133.
131. Schmidt, M., Gießl, A., Laufs, T., Hankeln, T., Wolfrum, U. and Burmester, T. (2002) How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina. J. Biol. Chem. 278, 1932-1935.
132. Scott, N.L., Falzone, C.J., Vuletich, T.J., Zhao, J., Bryant, D.A. and Lecomte, J.T.J. (2002) Truncated hemoglobin from the cyanobacterium Synechocystis sp. PCC7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein. Biochemistry 41, 6902-6910.
133. Spiro, S. and Guest, J. (1991) Adaptive responses to oxygen limitation in Escherichia coli. Trends Biochem Sci 16, 310-314.
134. Stevanin, T., Poole, R.K., Demoncheaux, E.A.G. and Read, R.C. (2002) Flavohemoglobin (Hmp) protects Salmonella enterica serovar typhimurium from nitric oxide-related killing by human macrophages. Infect Immun 70, 4399-4405.
135. Stevanin, T.M., Ioannidis, N., Mills, C.E., Kim, S.O., Hughes, M.N. and Poole, R.K. (2000) Flavohemoglobin (hmp) affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo ' or bd, from nitric oxide. J. Biol. Chem. 275, 35868-35875.
136. Takagi, T. (1993) Hemoglobins from single-celled organisms. Curr. Opin. Struct. Biol. 3, 413-418.
137. Takaya, N. and Shoun, H. (2002) Genetic engineering using fungal flavohemoglobin for constructing Pseudomonas stutzeri strain emitting less nitrous oxide. J. Biosc. Bioeng. 94, 282-284.
138. Tarricone, C., Calogero, S., Galizzi, A., Coda, A., Ascenzi, P. and Bolognesi, M. (1997a) Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria. Proteins 27, 154-156.
139. Tarricone, C., Galizzi, A., Coda, A., Ascenzi, P. and Bolognesi, M. (1997b) Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp. Structure 5, 497-507.
140. Thorsteinsson, M.V., Bevan, D.R., Ebel, R.E., Weber, R.E. and Potts, M. (1996) Spectroscopical and functional characterization of the hemoglobin of Nostoc commmune UTEX 584 (Cyanobacteria). Biochim. Biophys. Acta. 1292, 1333-1339.
141. Thorsteinsson, M.V., Bevan, D.R., Potts, M., Dou, Y., Eich, R.F., Hargrove, M.S., Gibson, Q.H. and Olson, J.S. (1999) A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties. Biochemistry 38, 2117-2126.
142. Tjepkema, J.D., Cashon, R.E., Beckwith, J. and Schwintzer, C.R. (2002) Hemoglobin in Frankia, a nitrogen-fixing actinomycete. Appl. Environ. Micobiol. 68, 2629-2631.
143. Trent, J.T. and Hargrove, M.S. (2002) A ubiquitously expressed human hexacoordinate hemoglobin. J. Biol. Chem. 277(22), 19538-19545.
144. Tsai, P.S., Kallio, P.T. and Bailey, J.E. (1995) Fnr, a global transcriptional regulator of Escherichia coli, activates the Vitreoscilla hemoglobin (VHb) promoter and intracellular VHb expression increases cytochrome d promoter activity. Biotechnol Prog 11, 288-293.
145. Tyree, B. and Webster, D.A. (1978) The binding of cyanide and carbon monoxide to cytochrome o purified from Vitreoscilla. Evidence for subunit interaction in the reduced protein. J. Biol. Chem. 253, 6988-6991.
146. Vasudevan, S.G., Armarego, W.L.F., Shaw, D.C., Lilley, P.E., Dixon, N.E. and Poole, R.K. (1991) Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12. Mol. Gen. Genet. 226, 49-58.
147. Vasudevan, S.G., Tang, P., Dixon, N.E. and Poole, R.K. (1995) Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli. FEMS Microbiol. Lett. 125, 219-224.
148. Visca, P., Fabozzi, G., Petrucca, A., Ciaccio, C., Coletta, M., De Sanctis, G., Bologesi, M., Milani, M. and Ascenzi, P. (2002) The trunctated hemoglobin from Mycobacterium leprae. Biochem. Biophys. Res. Com. 294, 1064-1070.
149. Wakabayashi, S., Matsubara, H. and Webster, D.A. (1986) Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla. Nature 322, 481-483.
150. Watts, R.A., Hunt, P.W., Hvitved, A.N., Hargrove, M.S., Peacock, W.J. and Dennnis, E.S. (2001) A hemoglobin from plants homologous to truncated hemoglobins of microorganisms. Proc. Natl. Acad. Sci. USA 98, 10119-10124.
151. Weber, R.E. and Vinogradov, S.N. (2001) Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol Rev 81, 569-628.
152. Webster, D.A. (1975) The formation of hydrogen peroxide during the oxidation of reduced nicotinamide adenine dinucleotide by cytochrome o from Vitreoscilla. J. Biol. Chem. 250, 4955-4958.
153. Webster, D.A. (1987) Structure and function of bacterial hemoglobin and related protein. In: Eichhorn GL and Marzilli LG (ed.) Advances in Inorganic Biochemistry, Vol. 7, pp. 245-265, Elsevier, New York.
154. Wei, M.L., Webster, D.A. and Stark, B.C. (1998) Genetic engineering of Serratia marcescens with bacterial hemoglobin gene: effects on growth, oxygen utilization, and cell size. Biotech Bioeng 57, 477-483.
155. Wittenberg, J.B. and Wittenberg, B.A. (1990) Mechanisms of cytoplasmic hemoglobin and myoglobin function. Annu Rev Biophys Biophys Chem 19, 217-241.
156. Wittenberg, J.B., Bolognesi, M., Wittenberg, B.A. and Guertin, M. (2002) Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J. Biol. Chem. 277, 871-874.
157. Wu, G., Wainwright, L.M. and Poole, R.K. (2003) Bacterial haemoglobins: old proteins with 'new' functions? Roles in respiratory and nitric oxide metabolism. In: Respiration in Archaea and Bacteria (D. Zannoni, ed.) Kluwer, in the press.
158. Yang, J., Kloek, A.P., Goldberg, D.E., Membrillo-Hernández, J. and Mathews, F.S. (1995) The structure of Ascaris hemogobin domain I at 2.2 Å resolution: molecular features of oxygen avidity. Proc. Natl. Acad. Sci. USA 92, 4224-4228.
159. 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune. Biochemistry 39, 1389-1399.
160. Yeh, S.R., Couture, M., Ouellet, Y., Guertin, M. and Rousseau, D.L. (2000a) A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis: stabilisation of heme ligands by a distal tyrosine residue. J. Biol. Chem. 275, 1679-1684.
161. Yeh, S.R., Couture, M., Ouellet, Y., Guertin, M. and Rousseau, D.L. (2000) A cooperative oxygen finding hemoglobin from Mycobacterium tuberculosis - stabilization of heme ligands by a distal tyrosine residue. J. Biol. Chem. 275, 1679-1684.
162. Yu, H., Sato, E.F., Nagata, K., Nishikawa, M., Kashiba, M., Arakawa, T., Kobayashi, K., Tamura, T. and Inoue, M. (1997) Oxygen-dependent regulation of the respiration and growth of Escherichia coli by nitric oxide. FEBS Lett. 409, 161-165.
163. Zhao, X.-J., Raitt, D., Burke, P.V., Clewell, A.S., Kwast, K.E. and Poyton, R.O. (1996) Function and expression of flavohemoglobin in Saccharomyces cerevisiae. Evidence for a role in the oxidative stress response. J. Biol. Chem. 271, 25131-25138.