Bacterial and archaeal globins - A revised perspective

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 9, 2013, Pages 1789-1800

  Vinogradov, Serge N ^a   Tinajero Trejo, Mariana ^b   Poole, Robert K ^b   Hoogewijs, David ^c  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF SHEFFIELD   (United Kingdom)

^c UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Archaea; Bacteria; Hemoglobin; Prokaryote

Indexed keywords

DIOXYGENASE; GLOBIN; MYOGLOBIN; NITRIC OXIDE; NITRIC OXIDE DIOXYGENASE; OXYGEN; PROTOGLOBIN; UNCLASSIFIED DRUG; CYTOGLOBIN; HEMOGLOBIN; NEUROGLOBIN; PROSTAGLANDIN B;

ACIDITHIOBACILLALES; ACIDOBACTERIA; ACTINOBACTERIA; ACTINOMYCETALES; AEROMONADALES; ALICYCLOBACILLACEAE; ALPHAPROTEOBACTERIA; ALTEROMONADALES; AMINO ACID SUBSTITUTION; ARCHAEAL GENOME; ARCHAEOGLOBALES; ARCHAEON; ARTICLE; BACILLACEAE; BACILLALES; BACILLALES INCERTAE SEDIS; BACILLI; BACTERIAL GENOME; BACTERIUM; BACTEROIDETES; BETAPROTEOBACTERIA; BIOINFORMATICS; BURKHOLDERIALES; CARDIOBACTERIALES; CHEMOTAXIS; CHROMATIALES; CLOSTRIDIA; CLOSTRIDIALES; CRENARCHAEOTA; DEINOCOCCI; DELTAPROTEOBACTERIA; DETOXIFICATION; ECOLOGICAL NICHE; ENTEROBACTERIALES; EPSILONPROTEOBACTERIA; ERYSIPELOTRICHI; EURYARCHAEOTA; FAMILY; FIBROBACTERES; FIRMICUTES; FUSOBACTERIA; GAMMAPROTEOBACTERIA; GEMMATIMONADETES; GENOME; GENOME SIZE; HALANAEROBIALES; HALOBACTERIALES; HYDROGENOPHILALES; IGNAVIBACTERIA; IN VIVO STUDY; KORARCHAEOTA; LACTOBACILLALES; LEGIONELLALES; LISTERIACEAE; MARINE SPECIES; METHANOCOCCALES; METHYLACIDIPHILUM; METHYLACIDIPHILUM INFERNORUM; METHYLOCOCCALES; METHYLOPHILALES; MOLECULAR PHYLOGENY; NATRANAEROBIALES; NEGATIVICUTES; NEISSERIALES; NITROSOMONADALES; NITROSPIRAE; NONHUMAN; OCEANOSPIRILLALES; OXYGEN CONCENTRATION; PAENIBACILLACEAE; PARVULARCULALES; PASTEURELLALES; PHYLOGENETIC TREE; PHYLOGENY; PLANCTOMYCETES; PLANCTOMYCETIA; PLANOCOCCACEAE; PRIORITY JOURNAL; PROCHLORALES; PROTEOBACTERIA; PSEUDOMONADALES; RHIZOBIALES; RHODOBACTERALES; RHODOCYCLALES; RICKETTSIALES; SALINISPHAERALES; SENSOR; SEQUENCE ALIGNMENT; SPHINGOMONADALES; SPOROLACTOBACILLACEAE; STAPHYLOCOCCACEAE; SULFOLOBALES; SYMBIONT; TAXON; THAUMARCHAEOTA; THERMALES; THERMOACTINOMYCETACEAE; THERMOANAEROBACTERIALES; THERMOCOCCALES; THERMOPLASMATALES; THERMOPROTEALES; THERMUS; THIOTRICHALES; VERRUMICROBIA; ADGB; ANDROGLOBIN; CYGB; FHB; FLAVOHAEMOGLOBIN; GBE; GBX; GBY; GCS; GENETICS; GLOBIN E; GLOBIN X; GLOBIN Y; GLOBIN-COUPLED SENSOR; HGT; HORIZONTAL GENE TRANSFER; LAST UNIVERSAL EUKARYOTE COMMON ANCESTOR; LECA; MB; MOLECULAR EVOLUTION; NGB; PROKARYOTE; SDGB; SENSOR SINGLE DOMAIN 3/3 GLOBIN RELATED TO THE N-TERMINAL OF GCSS.; SINGLE DOMAIN 3/3 GLOBIN RELATED TO THE N-TERMINAL OF FHBS; SSDGB;

AQUIFICAE; AQUIFICAE (CLASS); ARCHAEA; BACTERIA (MICROORGANISMS); PROKARYOTA;

ADGB; ANDROGLOBIN; ARCHAEA; BACTERIA; CYGB; CYTOGLOBIN; FHB; FLAVOHAEMOGLOBIN; GBE; GBX; GBY; GCS; GLOBIN E; GLOBIN X; GLOBIN Y; GLOBIN-COUPLED SENSOR; HAEMOGLOBIN; HB; HEMOGLOBIN; HGT; HORIZONTAL GENE TRANSFER; LAST UNIVERSAL EUKARYOTE COMMON ANCESTOR; LECA; MB; MYOGLOBIN; NEUROGLOBIN; NGB; PGB; PROKARYOTE; PROTOGLOBIN; SDGB; SENSOR SINGLE DOMAIN 3/3 GLOBIN RELATED TO THE N-TERMINAL OF GCSS.; SINGLE DOMAIN 3/3 GLOBIN RELATED TO THE N-TERMINAL OF FHBS; SSDGB;

ARCHAEA; BACTERIA; EVOLUTION, MOLECULAR; GENOME, ARCHAEAL; GENOME, BACTERIAL; GLOBINS; PHYLOGENY;

EID: 84884607622     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.03.021     Document Type: Article

References (131)

1. D. Keilin, Haemoglobin in fungi; occurrence of haemoglobin in yeast and the supposed stabilization of the oxygenated cytochrome oxidase, Nature 172 (1953) 390-393.
2. D. Keilin, J.F. Ryley, Haemoglobin in Protozoa, Nature 172 (1953) 451.
3. D. Keilin, A. Tissieres, Haemoglobin in moulds: Neurospora crassa and Penicillium notatum, Nature 172 (1953) 393-394.
4. R. Oshino, T. Asakura, K. Takio, N. Oshino, B. Chance, B. Hagihara, Purification and molecular properties of yeast hemoglobin, Eur. J. Biochem. 39 (1973) 581-590.
5. R. Oshino, N. Oshino, B. Chance, B. Hagihara, Studies on yeast hemoglobin - properties of yeast hemoglobin and its physiological function in cell, Eur. J. Biochem. 35 (1973) 23-33.
6. Y. Orii, D.A. Webster, Oxygenated cytochrome o (Vitreoscilla) formed by treating oxidized cytochrome with superoxide anion, Plant Cell Physiol. 18 (1977) 521-526.
7. D.A. Webster, Y. Orii, Oxygenated cytochrome o. An active intermediate observed in whole cells of Vitreoscilla, J. Biol. Chem. 252 (1977) 1834-1836. (Pubitemid 8077563)
8. D.A. Webster, Y. Orii, Physiological role of oxygenated cytochrome o: observations on whole-cell suspensions of Vitreoscilla, J. Bacteriol. 135 (1978) 62-67. (Pubitemid 8377429)
9. D.A. Webster, Y. Orii, Biphasic recombination of photodissociated CO compound of cytochrome o (s) from Vitreoscilla, J. Biol. Chem. 260 (1985) 15526-15529. (Pubitemid 16170089)
10. S. Wakabayashi, H. Matsubara, D.A. Webster, Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla, Nature 322 (1986) 481-483. (Pubitemid 16034023)
11. M.F. Perutz, A bacterial haemoglobin, Nature 322 (1986) 405.
12. S.G. Vasudevan, W.L. Armarego, D.C. Shaw, P.E. Lilley, N.E. Dixon, R.K. Poole, Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12, Mol. Gen. Genet. 226 (1991) 49-58.
13. M.T. Forrester, M.W. Foster, Protection from nitrosative stress: a central role for microbial flavohemoglobin, Free Radic. Biol. Med. 52 (2012) 1620-1633.
14. G. Wu, L.M. Wainwright, R.K. Poole, Microbial globins, Adv. Microb. Physiol. 47 (2003) 255-310. (Pubitemid 37214152)
15. M. Potts, S.V. Angeloni, R.E. Ebel, D. Bassam, Myoglobin in a cyanobacterium, Science 256 (1992) 1690-1691.
16. D.R. Hill, T.J. Belbin, M.V. Thorsteinsson, D. Bassam, S. Brass, A. Ernst, P. Boger, H. Paerl, M.E. Mulligan, M. Potts, GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp., J. Bacteriol. 178 (1996) 6587-6598. (Pubitemid 26374728)
17. M.A. Gilles-Gonzalez, G.S. Ditta, D.R. Helinski, A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti, Nature 350 (1991) 170-172. (Pubitemid 21912192)
18. J. Farres, M.P. Rechsteiner, S. Herold, A.D. Frey, P.T. Kallio, Ligand binding properties of bacterial hemoglobins and flavohemoglobins, Biochemistry 44 (2005) 4125-4134. (Pubitemid 40358066)
19. S. Hou, T. Freitas, R.W. Larsen, M. Piatibratov, V. Sivozhelezov, A. Yamamoto, E.A. Meleshkevitch, M. Zimmer, G.W. Ordal, M. Alam, Globin-coupled sensors: a class of heme-containing sensors in Archaea and Bacteria, Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 9353-9358. (Pubitemid 32743920)
20. S. Hou, R.W. Larsen, D. Boudko, C.W. Riley, E. Karatan, M. Zimmer, G.W. Ordal, M. Alam, Myoglobin-like aerotaxis transducers in Archaea and Bacteria, Nature 403 (2000) 540-544. (Pubitemid 30082198)
21. T.A. Freitas, S. Hou, E.M. Dioum, J.A. Saito, J. Newhouse, G. Gonzalez, M.A. Gilles-Gonzalez, M. Alam, Ancestral hemoglobins in Archaea, Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 6675-6680. (Pubitemid 38586033)
22. S.N. Vinogradov, D. Hoogewijs, X. Bailly, R. Arredondo-Peter, J. Gough, S. Dewilde, L. Moens, J.R. Vanfleteren, A phylogenomic profile of globins, BMC Evol. Biol. 6 (2006) 31.
23. S.N. Vinogradov, D. Hoogewijs, X. Bailly, R. Arredondo-Peter, M. Guertin, J. Gough, S. Dewilde, L. Moens, J.R. Vanfleteren, Three globin lineages belonging to two structural classes in genomes from the three kingdoms of life, Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 11385-11389. (Pubitemid 41153829)
24. A. Pesce, M. Couture, S. Dewilde, M. Guertin, K. Yamauchi, P. Ascenzi, L. Moens, M. Bolognesi, A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family, EMBO J. 19 (2000) 2424-2434. (Pubitemid 30323532)
25. D.A. Vuletich, J.T. Lecomte, A phylogenetic and structural analysis of truncated hemoglobins, J. Mol. Evol. 62 (2006) 196-210.
26. J.B. Wittenberg, M. Bolognesi, B.A. Wittenberg, M. Guertin, Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants, J. Biol. Chem. 277 (2002) 871-874. (Pubitemid 34968827)
27. J. Gough, K. Karplus, R. Hughey, C. Chothia, Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure, J. Mol. Biol. 313 (2001) 903-919. (Pubitemid 33063435)
28. J. Shi, T.L. Blundell, K. Mizuguchi, FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties, J. Mol. Biol. 310 (2001) 243-257. (Pubitemid 32619966)
29. S.F. Altschul, T.L. Madden, A.A. Schaffer, J. Zhang, Z. Zhang, W. Miller, D.J. Lipman, Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res. 25 (1997) 3389-3402. (Pubitemid 27359211)
30. A.A. Schaffer, L. Aravind, T.L. Madden, S. Shavirin, J.L. Spouge, Y.I. Wolf, E.V. Koonin, S.F. Altschul, Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements, Nucleic Acids Res. 29 (2001) 2994-3005. (Pubitemid 32685225)
31. R.C. Edgar, MUSCLE: multiple sequence alignment with high accuracy and high throughput, Nucleic Acids Res. 32 (2004) 1792-1797. (Pubitemid 38832724)
32. J.S. Papadopoulos, R. Agarwala, COBALT: constraint-based alignment tool for multiple protein sequences, Bioinformatics 23 (2007) 1073-1079. (Pubitemid 47050558)
33. K. Katoh, K. Kuma, H. Toh, T. Miyata, MAFFT version 5: improvement in accuracy of multiple sequence alignment, Nucleic Acids Res. 33 (2005) 511-518. (Pubitemid 40360980)
34. C.B. Do, M.S. Mahabhashyam, M. Brudno, S. Batzoglou, ProbCons: probabilistic consistency-based multiple sequence alignment, Genome Res. 15 (2005) 330-340. (Pubitemid 40309398)
35. P. Di Tommaso, S. Moretti, I. Xenarios, M. Orobitg, A. Montanyola, J.M. Chang, J.F. Taly, C. Notredame, T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension, Nucleic Acids Res. 39 (2011) W13-W17.
36. T. Lassmann, E.L. Sonnhammer, Automatic assessment of alignment quality, Nucleic Acids Res. 33 (2005) 7120-7128. (Pubitemid 43125080)
37. K. Tamura, D. Peterson, N. Peterson, G. Stecher, M. Nei, S. Kumar, MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods, Mol. Biol. Evol. 28 (2011) 2731-2739.
38. F. Ronquist, J.P. Huelsenbeck, MrBayes 3: Bayesian phylogenetic inference under mixed models, Bioinformatics 19 (2003) 1572-1574. (Pubitemid 37038874)
39. M.A. Miller, W. Pfeiffer, T. Schwartz, Creating the CIPRES Science Gateway for Inference of Large Phylogenetic Trees, Proceedings of the Gateway Computing Environments Workshop (GCE), New Orleans, LA, 2010, pp. 1-8.
40. X.C. Morgan, N. Segata, C. Huttenhower, Biodiversity and functional genomics in the human microbiome, Trends Genet. 29 (2013) 51-58.
41. S.N. Vinogradov, D. Hoogewijs, X. Bailly, K. Mizuguchi, S. Dewilde, L. Moens, J.R. Vanfleteren, A model of globin evolution, Gene 398 (2007) 132-142. (Pubitemid 47068897)
42. K. Liolios, K. Mavromatis, N. Tavernarakis, N.C. Kyrpides, The Genomes On Line Database (GOLD) in 2007: status of genomic and metagenomic projects and their associated metadata, Nucleic Acids Res. 36 (2008) D475-D479. (Pubitemid 351149769)
43. D. Wu, P. Hugenholtz, K. Mavromatis, R. Pukall, E. Dalin, N.N. Ivanova, V. Kunin, L. Goodwin, M. Wu, B.J. Tindall, S.D. Hooper, A. Pati, A. Lykidis, S. Spring, I.J. Anderson, P. D'Haeseleer, A. Zemla, M. Singer, A. Lapidus, M. Nolan, A. Copeland, C. Han, F. Chen, J.F. Cheng, S. Lucas, C. Kerfeld, E. Lang, S. Gronow, P. Chain, D. Bruce, E.M. Rubin, N.C. Kyrpides, H.P. Klenk, J.A. Eisen, A phylogeny-driven genomic encyclopaedia of Bacteria and Archaea, Nature 462 (2009) 1056-1060.
44. C. Mora, D.P. Tittensor, S. Adl, A.G. Simpson, B. Worm, How many species are there on Earth and in the ocean? PLoS Biol. 9 (2011) e1001127.
45. S.J. Giovannoni, H.J. Tripp, S. Givan, M. Podar, K.L. Vergin, D. Baptista, L. Bibbs, J. Eads, T.H. Richardson, M. Noordewier, M.S. Rappe, J.M. Short, J.C. Carrington, E.J. Mathur, Genome streamlining in a cosmopolitan oceanic bacterium, Science 309 (2005) 1242-1245. (Pubitemid 41170917)
46. J.W. Murray, O. Delumeau, R.J. Lewis, Structure of a nonheme globin in environmental stress signaling, Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17320-17325. (Pubitemid 41740864)
47. S.N. Vinogradov, I. Fernandez, D. Hoogewijs, R. Arredondo-Peter, Phylogenetic relationships of 3/3 and 2/2 hemoglobins in Archaeplastida genomes to bacterial and other eukaryote hemoglobins, Mol. Plant 4 (2011) 42-58.
48. D. Hoogewijs, S. Dewilde, A. Vierstraete, L. Moens, S.N. Vinogradov, A phylogenetic analysis of the globins in fungi, PLoS One 7 (2012) e31856.
49. S.N. Vinogradov, Tracing globin phylogeny using PSIBLAST searches based on groups of sequences, Methods Enzymol. 436 (2008) 571-583.
50. A.H. Teh, J.A. Saito, A. Baharuddin, J.R. Tuckerman, J.S. Newhouse, M. Kanbe, E.I. Newhouse, R.A. Rahim, F. Favier, C. Didierjean, E.H. Sousa, M.B. Stott, P.F. Dunfield, G. Gonzalez, M.A. Gilles-Gonzalez, N. Najimudin, M. Alam, Hell's Gate globin I: an acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin, FEBS Lett. 585 (2011) 3250-3258.
51. T. Burmester, M. Haberkamp, S. Mitz, A. Roesner, M. Schmidt, B. Ebner, F. Gerlach, C. Fuchs, T. Hankeln, Neuroglobin and cytoglobin: genes, proteins and evolution, IUBMB Life 56 (2004) 703-707. (Pubitemid 40515816)
52. D. Hoogewijs, B. Ebner, F. Germani, F.G. Hoffmann, A. Fabrizius, L. Moens, T. Burmester, S. Dewilde, J.F. Storz, S.N. Vinogradov, T. Hankeln, Androglobin: a chimeric globin in metazoans that is preferentially expressed in mammalian testes, Mol. Biol. Evol. 29 (2012) 1105-1114.
53. G.R. Stranzl, E. Santelli, L.A. Bankston, C. La Clair, A. Bobkov, R. Schwarzenbacher, A. Godzik, M. Perego, M. Grynberg, R.C. Liddington, Structural insights into inhibition of Bacillus anthracis sporulation by a novel class of non-heme globin sensor domains, J. Biol. Chem. 286 (2011) 8448-8458.
54. P. Lapierre, J.P. Gogarten, Estimating the size of the bacterial pan-genome, Trends Genet. 25 (2009) 107-110.
55. S.N. Vinogradov, D. Hoogewijs, J.R. Vanfleteren, S. Dewilde, L. Moens, T. Hankeln, Evolution of the Globin Superfamily and its Function, in: M. Nagai (Ed.), Hemoglobin: Recent Developments and Topics, Research Signpost, 2011, pp. 232-254.
56. S.N. Vinogradov, L. Moens, Diversity of globin function: enzymatic, transport, storage, and sensing, J. Biol. Chem. 283 (2008) 8773-8777.
57. P.R. Gardner, Hemoglobin, a nitric oxide dioxygenase, Scientifica 1 (2012).
58. A. Hausladen, A. Gow, J.S. Stamler, Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen, Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 10108-10112. (Pubitemid 32802982)
59. P.R. Gardner, Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases, J. Inorg. Biochem. 99 (2005) 247-266. (Pubitemid 39646484)
60. B.J. Smagghe, J.T. Trent III, M.S. Hargrove, NOdioxygenase activity inhemoglobins is ubiquitous in vitro, but limited by reduction in vivo, PLoS One 3 (2008) e2039.
61. C.G. Mowat, B. Gazur, L.P. Campbell, S.K. Chapman, Flavin-containing heme enzymes, Arch. Biochem. Biophys. 493 (2010) 37-52.
62. J.A. Saito, X. Wan, K.S. Lee, S. Hou, M. Alam, Globin-coupled sensors and protoglobins share a common signaling mechanism, FEBS Lett. 582 (2008) 1840-1846.
63. X. Wan, J.R. Tuckerman, J.A. Saito, T.A. Freitas, J.S. Newhouse, J.R. Denery, M.Y. Galperin, G. Gonzalez, M.A. Gilles-Gonzalez, M. Alam, Globins synthesize the second messenger bis-(3'-5')-cyclic diguanosine monophosphate in bacteria, J. Mol. Biol. 388 (2009) 262-270.
64. U. Ermler, R.A. Siddiqui, R. Cramm, B. Friedrich, Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 angstrom resolution, EMBO J. 14 (1995) 6067-6077.
65. A. Ilari, A. Bonamore, A. Farina, K.A. Johnson, A. Boffi, The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket, J. Biol. Chem. 277 (2002) 23725-23732. (Pubitemid 34952213)
66. C. Tarricone, A. Galizzi, A. Coda, P. Ascenzi, M. Bolognesi, Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp., Structure 5 (1997) 497-507. (Pubitemid 27191226)
67. M. Shepherd, V. Barynin, C. Lu, P.V. Bernhardt, G. Wu, S.R. Yeh, T. Egawa, S.E. Sedelnikova, D.W. Rice, J.L. Wilson, R.K. Poole, The single-domain globin from the pathogenic bacterium Campylobacter jejuni: novel D-helix conformation, proximal hydrogen bonding that influences ligand binding, and peroxidaselike redox properties, J. Biol. Chem. 285 (2010) 12747-12754.
68. M. Nardini, A. Pesce, L. Thijs, J.A. Saito, S. Dewilde, M. Alam, P. Ascenzi, M. Coletta, C. Ciaccio, L. Moens, M. Bolognesi, Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity, EMBO Rep. 9 (2008) 157-163. (Pubitemid 351223453)
69. W. Zhang, G.N. Phillips Jr., Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry, Structure 11 (2003) 1097-1110. (Pubitemid 37103071)
70. A. Pesce, L Thijs, M. Nardini, F. Desmet, L Sisinni, L Gourlay, A. Bolli, M. Coletta, S. Van Doorslaer, X. Wan, M. Alam, P. Ascenzi, L Moens, M. Bolognesi, S. Dewilde, HisE11 and HisF8 provide bis-histidyl heme hexa-coordination in the globin domain of Geobacter sulfurreducens globin-coupled sensor, J. Mol. Biol. 386 (2009) 246-260.
71. 2 diffusion to the heme, EMBOJ. 20 (2001) 3902-3909. (Pubitemid 32751806)
72. A. Ilari, P. Kjelgaard, C von Wachenfeldt, B. Catacchio, E. Chiancone, A. Boffi, Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus, Arch. Biochem. Biophys. 457 (2007) 85-94 (Pubitemid 44969279)
73. C.J. Falzone, B. Christie Vu, N.L Scott, J.T. Lecomte, The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state, J. Mol. Biol. 324 (2002) 1015-1029. (Pubitemid 41782990)
74. JA Hoy, S. Kundu, J.T. Trent III, S. Ramaswamy, M.S. Hargrove, The crystal structure of Synechocystis hemoglobin with a covalent heme linkage, J. Biol. Chem. 279 (2004) 16535-16542. (Pubitemid 38509353)
75. N.L. Scott, Y. Xu, G. Shen, DA Vuletich, C.J. Falzone, Z. Li, M. Ludwig, M.P. Pond, M.R. Preimesberger, DA Bryant, J.T. Lecomte, Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002, Biochemistry 49 (2010) 7000-7011.
76. M. Milani, P.Y. Savard, H. Ouellet, P. Ascenzi, M. Guertin, M. Bolognesi, A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O, Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 5766-5771. (Pubitemid 36576882)
77. L. Giangiacomo, A. Ilari, A. Boffi, V. Morea, E. Chiancone, The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties, J. Biol. Chem. 280 (2005) 9192-9202. (Pubitemid 40409609)
78. A. Bonamore, A. Ilari, L. Giangiacomo, A. Bellelli, V. Morea, A. Boffi, A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca, FEBS J. 272 (2005) 4189-4201. (Pubitemid 41160925)
79. M. Nardini, A. Pesce, M. Labarre, C. Richard, A. Bolli, P. Ascenzi, M. Guertin, M. Bolognesi, Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni, J. Biol. Chem. 281 (2006) 37803-37812. (Pubitemid 46043310)
80. HJ. Nothnagel, B.Y. Winer, DA Vuletich, M.P. Pond, J.T.J. Lecomte, Structural properties of 2/2 hemoglobins: the Group III protein from Helicobacter hepaticus, IUBMB Life 63 (2011) 197-205.
81. M.R. Preimesberger, M.P. Pond, A. Majumdar, J.T. Lecomte, Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002, J. Biol. Inorg. Chem. 17 (2012) 599-609.
82. R.K. Poole, N. Ioannidis, Y. Orii, 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. Biol. Sci. 255 (1994) 251-258. (Pubitemid 24102284)
83. S. McLean, LA Bowman, R.K. Poole, Peroxynitrite stress is exacerbated by flavohaemoglobin-derived oxidative stress in Salmonella typhimurium and is relieved by nitric oxide, Microbiology 156 (2010) 3556-3565.
84. N.J. Gilberthorpe, M.E. Lee, T.M. Stevanin, R.C. Read, R.K. Poole, NsrR: a key regulator circumventing Salmonella enterica serovar Typhimurium oxidative and nitrosative stress in vitro and in IFN-gamma-stimulated J774.2 macrophages, Microbiology 153 (2007) 1756-1771. (Pubitemid 46952506)
85. G. Wu, H. Corker, Y. Orii, R.K. Poole, Escherichia coli Hmp, an "oxygen-binding flavohaemoprotein", produces superoxide anion and self-destructs, Arch. Microbiol. 182 (2004) 193-203. (Pubitemid 39361996)
86. B.J. Reeder, DA Svistunenko, CE. Cooper, M.T. Wilson, Engineering tyrosine-based electron flow pathways in proteins: the case of aplysia myoglobin, J. Am. Chem. Soc. 134 (2012) 7741-7749.
87. V. Gonzales-Prevatt, DA Webster, Purification and properties of NADH-cytochrome o reductase from Vitreoscilla, J. Biol. Chem. 255 (1980) 1478-1482.
88. W. Jakob, DA Webster, P.M.H. Kroneck, NADH-dependent methemoglobin reductase from the obligate aerobe Vitreoscilla - improved method of purification and reexamination of prosthetic groups, Arch. Biochem. Biophys. 292 (1992) 29-33.
89. A.D. Frey, M. Shepherd, S. Jokipii-Lukkari, H. Haggman, P.T. Kallio, The singledomain globin of Vitreoscilla: augmentation of aerobic metabolism for biotechnological applications, Adv. Microb. Physiol. 58 (2011) 81-139.
90. B.C. Stark, K.L. Dikshit, K.R. Pagilla, Recent advances in understanding the structure, function, and biotechnological usefulness of the hemoglobin from the bacterium Vitreoscilla, Biotechnol. Lett 33 (2011) 1705-1714.
91. R.K. Poole, M.F. Anjum, J. Membrillo-Hernández, S.O. Kim, M.N. Hughes, V. Stewart, Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12, J. Bacteriol. 178 (1996) 5487-5492. (Pubitemid 26304384)
92. P.R. Gardner, A.M. Gardner, LA Martin, A.L. Salzman, Nitric oxide dioxygenase: an enzymic function for flavohemoglobin, Proc. Natl. Acad. Sci. U.S. A. 95 (1998) 10378-10383. (Pubitemid 28413075)
93. A. Hausladen, J.S. Stamler, Is the flavohemoglobin a nitric oxide dioxygenase? Free Rad. Biol. Med. 53 (2012) 1209-1210.
94. CE. Mills, S. Sedelnikova, B. Søballe, M.N. Hughes, R.K. Poole, 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 (2001) 207-213. (Pubitemid 32096927)
95. J. Membrillo-Hernandez, M.D. Coopamah, M.F. Anjum, T.M. Stevanin, A. Kelly, M.N. Hughes, R.K. Poole, 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 (1999) 748-754.
96. A.M. Gardner, P.R. Gardner, 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 (2002) 8166-8171. (Pubitemid 34968271)
97. M.T. Forrester, M.W. Foster, Response to 'Is flavohemoglobin a nitric oxide dioxygenase?', Free Rad. Biol. Med. 53 (2012) 1211-1212.
98. M.C. Justino, J.B. Vicente, M. Teixeira, LM. Saraiva, New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide, J. Biol. Chem. 280 (2005) 2636-2643. (Pubitemid 40189367)
99. L Svensson, M. Poljakovic, S. Save, N. Gilberthorpe, T. Schon, S. Strid, H. Corker, RK. Poole, K. Persson, Role of flavohemoglobin in combating nitrosative stress in uropathogenic Escherichia coli-implications for urinary tract infection, Microb. Pathog. 49 (2010) 59-66.
100. T.M. Stevanin, N. Ioannidis, CE. Mills, S.O. Kim, M.N. Hughes, R.K. Poole, Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo' or bd, from nitric oxide, J. Biol. Chem. 275 (2000) 35868-35875.
101. T.M. Stevanin, R.C. Read, R.K. Poole, The hmp gene encoding the NO-inducible flavohaemoglobin in Escherichia coli confers a protective advantage in resisting killing within macrophages, but not in vitro: links with swarming motility, Gene 398 (2007) 62-68. (Pubitemid 47068894)
102. H. Corker, R.K. Poole, Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp, J. Biol. Chem. 278 (2003) 31584-31592. (Pubitemid 37048336)
103. P.R. Gardner, G. Costantino, A.L. Salzman, Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase, J. Biol. Chem. 273 (1998) 26528-26533. (Pubitemid 28471662)
104. A. Hausladen, AJ. Gow, J.S. Stamler, Nitrosative stress: metabolic pathway involving the flavohemoglobin, Proc Natl. Acad. Sci. U. S. A. 95 (1998) 14100-14105. (Pubitemid 28549327)
105. L Svensson, B.I. Marklund, M. Poljakovic, K. Persson, Uropathogenic Escherichia coli and tolerance to nitric oxide: the role of flavohemoglobin, J. Urol. 175 (2006) 749-753. (Pubitemid 43067443)
106. E. Hernandez-Urzua, CE. Mills, G.P. White, M.L. Contreras-Zentella, E. Escamilla, S.G. Vasudevan, J. Membrillo-Hernandez, R.K. Poole, Flavohemoglobin Hmp, but not its individual domains, confers protection from respiratory inhibition by nitric oxide in Escherichia coli, J. Biol. Chem. 278 (2003) 34975-34982. (Pubitemid 37102258)
107. N.J. Gilberthorpe, R.K. Poole, Nitric oxide homeostasis in Salmonella typhimurium: roles of respiratory nitrate reductase and flavohemoglobin, J. Biol. Chem. 283 (2008) 11146-11154.
108. M.J. Crawford, D.E. Goldberg, Role for the Salmonella flavohemoglobin in protection from nitric oxide, J. Biol. Chem. 273 (1998) 12543-12547. (Pubitemid 28240629)
109. T.M. Stevanin, R.K. Poole, E.A. Demoncheaux, R.C. Read, Flavohemoglobin Hmp protects Salmonella enterica serovar typhimurium from nitric oxide-related killing by human macrophages, Infect Immun. 70 (2002) 4399-4405. (Pubitemid 34790950)
110. I.S. Bang, L Liu, A. Vazquez-Torres, M.L. Crouch, J.S. Stamler, F.C Fang, Maintenance of nitric oxide and redox homeostasis by the Salmonella flavohemoglobin hmp, J. Biol. Chem. 281 (2006) 28039-28047. (Pubitemid 44414517)
111. J.R. Laver, T.M. Stevanin, S.L. Messenger, A.D. Lunn, M.E. Lee, J.W. Moir, R.K. Poole, RC Read, Bacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: a novel mechanism of bacterial pathogenesis, FASEB J. 24 (2009) 286-295.
112. Y.M. Park, H.J. Park, Y.H. Joung, I.S. Bang, Nitrosative stress causes amino acid auxotrophy in hmp mutant Salmonella typhimurium, Microbiol. Immunol. 55 (2011) 143-147.
113. K.T. Elvers, G. Wu, N.J. Gilberthorpe, R.K. Poole, S.F. Park, Role of an inducible single-domain hemoglobin in mediating resistance to nitric oxide and nitrosative stress in Campylobacter jejuni and Campylobacter coli, J. Bacteriol. 186 (2004) 5332-5341. (Pubitemid 39038135)
114. M.S. Pittman, K.T. Elvers, L. Lee, M.A. Jones, R.K. Poole, S.F. Park, D.J. Kelly, Growth of Campylobacter jejuni on nitrate and nitrite: electron transport to NapA and NrfA via NrfH and distinct roles for NrfA and the globin Cgb in protection against nitrosative stress, Mol. Microbiol. 63 (2007) 575-590. (Pubitemid 46058941)
115. L.M. Wainwright, K.T. Elvers, S.F. Park, R.K. Poole, A truncated haemoglobin implicated in oxygen metabolism by the microaerophilic food-borne pathogen Campylobacter jejuni, Microbiology 151 (2005) 4079-4091. (Pubitemid 41829988)
116. R. Cramm, R.A. Siddiqui, B. Friedrich, Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus, J. Biol. Chem. 269 (1994) 7349-7354. (Pubitemid 24217931)
117. S. Favey, G. Labesse, V. Vouille, M. Boccara, Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937, Microbiology 141 (Pt 4) (1995) 863-871.
118. M. Boccara, C.E. Mills, J. Zeier, C. Anzi, C. Lamb, R.K. Poole, M. Delledonne, Flavohaemoglobin HmpX from Erwinia chrysanthemi confers nitrosative stress tolerance and affects the plant hypersensitive reaction by intercepting nitric oxide produced by the host, Plant J. 43 (2005) 226-237. (Pubitemid 41009340)
119. M.M. Nakano, Essential role of flavohemoglobin in long-term anaerobic survival of Bacillus subtilis, J. Bacteriol. 188 (2006) 6415-6418. (Pubitemid 44448585)
120. A. Rogstam, J.T. Larsson, P. Kjelgaard, C. von Wachenfeldt, Mechanisms of adaptation to nitrosative stress in Bacillus subtilis, J. Bacteriol. 189 (2007) 3063-3071. (Pubitemid 46697395)
121. H. Ouellet, Y. Ouellet, C. Richard, M. Labarre, B. Wittenberg, J. Wittenberg, M. Guertin, Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide, Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 5902-5907. (Pubitemid 34493237)
122. A.R. Richardson, P.M. Dunman, F.C. Fang, The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity, Mol. Microbiol. 61 (2006) 927-939. (Pubitemid 44137205)
123. V.L. Goncalves, L.S. Nobre, J.B. Vicente, M. Teixeira, L.M. Saraiva, Flavohemoglobin requires microaerophilic conditions for nitrosative protection of Staphylococcus aureus, FEBS Lett. 580 (2006) 1817-1821.
124. L.S. Nobre, V.L. Goncalves, L.M. Saraiva, Flavohemoglobin of Staphylococcus aureus, Methods Enzymol. 436 (2008) 203-216.
125. L.S. Nobre, S. Todorovic, A.F. Tavares, E. Oldfield, P. Hildebrandt, M. Teixeira, L.M. Saraiva, Binding of azole antibiotics to Staphylococcus aureus flavohemoglobin increases intracellular oxidative stress, J. Bacteriol. 192 (2010) 1527-1533.
126. Y. Wang, A.K. Dunn, J. Wilneff, M.J. McFall-Ngai, S. Spiro, E.G. Ruby, Vibrio fischeri flavohaemoglobin protects against nitric oxide during initiation of the squid-Vibrio symbiosis, Mol. Microbiol. 78 (2010) 903-915.
127. E. Meilhoc, Y. Cam, A. Skapski, C. Bruand, The response to nitric oxide of the nitrogen-fixing symbiont Sinorhizobium meliloti, Mol. Plant Microbe Interact. 23 (2010) 748-759.
128. B.W. Davies, R.W. Bogard, N.M. Dupes, T.A. Gerstenfeld, L.A. Simmons, J.J. Mekalanos, DNA damage and reactive nitrogen species are barriers to Vibrio cholerae colonization of the infant mouse intestine, PLoS Pathog. 7 (2011) e1001295.
129. A.M. Stern, A.J. Hay, Z. Liu, F.A. Desland, J. Zhang, Z. Zhong, J. Zhu, The NorR regulon is critical for Vibrio cholerae resistance to nitric oxide and sustained colonization of the intestines, MBio 3 (2012), (e00013-00012).
130. H. Arai, M. Hayashi, A. Kuroi, M. Ishii, Y. Igarashi, Transcriptional regulation of the flavohemoglobin gene for aerobic nitric oxide detoxification by the second nitric oxide-responsive regulator of Pseudomonas aeruginosa, J. Bacteriol. 187 (2005) 3960-3968. (Pubitemid 40827779)
131. E. Parrilli, M. Giuliani, D. Giordano, R. Russo, G. Marino, C. Verde, M.L. Tutino, The role of a 2-on-2 haemoglobin in oxidative and nitrosative stress resistance of Antarctic Pseudoalteromonas haloplanktis TAC125, Biochimie 92 (2010) 1003-1009.