1hco Citations

The structure of human carbonmonoxy haemoglobin at 2.7 A resolution.

J Mol Biol 136 103-28 (1980)
Cited: 109 times
EuropePMC logo PMID: 7373648

Articles - 1hco mentioned but not cited (4)



Reviews citing this publication (2)

  1. Computer studies of interactions between macromolecules. Wodak SJ, De Crombrugghe M, Janin J. Prog Biophys Mol Biol 49 29-63 (1987)
  2. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Kroeger KS, Kundrot CE. Structure 5 227-237 (1997)

Articles citing this publication (103)

  1. Structure of human oxyhaemoglobin at 2.1 A resolution. Shaanan B. J Mol Biol 171 31-59 (1983)
  2. Structure and refinement of oxymyoglobin at 1.6 A resolution. Phillips SE. J Mol Biol 142 531-554 (1980)
  3. Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution. Takano T, Dickerson RE. J Mol Biol 153 79-94 (1981)
  4. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution. Kuriyan J, Wilz S, Karplus M, Petsko GA. J Mol Biol 192 133-154 (1986)
  5. 1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. Park SY, Yokoyama T, Shibayama N, Shiro Y, Tame JR. J Mol Biol 360 690-701 (2006)
  6. Quaternary structure of hemoglobin in solution. Lukin JA, Kontaxis G, Simplaceanu V, Yuan Y, Bax A, Ho C. Proc Natl Acad Sci U S A 100 517-520 (2003)
  7. Stereochemistry of cooperative effects in fish an amphibian haemoglobins. Perutz MF, Brunori M. Nature 299 421-426 (1982)
  8. Mechanisms of domain closure in proteins. Lesk AM, Chothia C. J Mol Biol 174 175-191 (1984)
  9. Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism. Gelin BR, Lee AW, Karplus M. J Mol Biol 171 489-559 (1983)
  10. Distal residues in the oxygen binding site of haemoglobin studied by protein engineering. Nagai K, Luisi B, Shih D, Miyazaki G, Imai K, Poyart C, De Young A, Kwiatkowsky L, Noble RW, Lin SH. Nature 329 858-860 (1987)
  11. Substituted benzaldehydes designed to increase the oxygen affinity of human haemoglobin and inhibit the sickling of sickle erythrocytes. Beddell CR, Goodford PJ, Kneen G, White RD, Wilkinson S, Wootton R. Br J Pharmacol 82 397-407 (1984)
  12. Free energy of burying hydrophobic residues in the interface between protein subunits. Vallone B, Miele AE, Vecchini P, Chiancone E, Brunori M. Proc Natl Acad Sci U S A 95 6103-6107 (1998)
  13. The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of alpha-helices. Perutz MF, Gronenborn AM, Clore GM, Fogg JH, Shih DT. J Mol Biol 183 491-498 (1985)
  14. Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins. Johnson MS, Sutcliffe MJ, Blundell TL. J Mol Evol 30 43-59 (1990)
  15. Deoxymyoglobin studied by the conformational normal mode analysis. I. Dynamics of globin and the heme-globin interaction. Seno Y, Go N. J Mol Biol 216 95-109 (1990)
  16. The T-to-R transformation in hemoglobin: a reevaluation. Srinivasan R, Rose GD. Proc Natl Acad Sci U S A 91 11113-11117 (1994)
  17. The iron-oxygen bond in human oxyhaemoglobin. Shaanan B. Nature 296 683-684 (1982)
  18. Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy. Moore JN, Hansen PA, Hochstrasser RM. Proc Natl Acad Sci U S A 85 5062-5066 (1988)
  19. The mutation beta 99 Asp-Tyr stabilizes Y--a new, composite quaternary state of human hemoglobin. Smith FR, Lattman EE, Carter CW. Proteins 10 81-91 (1991)
  20. Deoxymyoglobin studied by the conformational normal mode analysis. II. The conformational change upon oxygenation. Seno Y, Go N. J Mol Biol 216 111-126 (1990)
  21. Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin. Simplaceanu V, Lukin JA, Fang TY, Zou M, Ho NT, Ho C. Biophys J 79 1146-1154 (2000)
  22. NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin. Lukin JA, Simplaceanu V, Zou M, Ho NT, Ho C. Proc Natl Acad Sci U S A 97 10354-10358 (2000)
  23. Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin. Henry ER, Levitt M, Eaton WA. Proc Natl Acad Sci U S A 82 2034-2038 (1985)
  24. Structural basis for the root effect in haemoglobin. Mylvaganam SE, Bonaventura C, Bonaventura J, Getzoff ED. Nat Struct Biol 3 275-283 (1996)
  25. Physiological and x-ray studies of potential antisickling agents. Abraham DJ, Perutz MF, Phillips SE. Proc Natl Acad Sci U S A 80 324-328 (1983)
  26. Dynamic protein structures: infrared evidence for four discrete rapidly interconverting conformers at the carbon monoxide binding site of bovine heart myoglobin. Caughey WS, Shimada H, Choc MG, Tucker MP. Proc Natl Acad Sci U S A 78 2903-2907 (1981)
  27. Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobins. Derewenda Z, Dodson G, Emsley P, Harris D, Nagai K, Perutz M, Renaud JP. J Mol Biol 211 515-519 (1990)
  28. The structural and functional analysis of the hemoglobin D component from chicken. Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML. J Biol Chem 274 6411-6420 (1999)
  29. Computationally accessible method for estimating free energy changes resulting from site-specific mutations of biomolecules: systematic model building and structural/hydropathic analysis of deoxy and oxy hemoglobins. Burnett JC, Botti P, Abraham DJ, Kellogg GE. Proteins 42 355-377 (2001)
  30. Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli. Weickert MJ, Pagratis M, Curry SR, Blackmore R. Appl Environ Microbiol 63 4313-4320 (1997)
  31. Effect of malondialdehyde, a product of lipid peroxidation, on the function and stability of hemoglobin. Kikugawa K, Kosugi H, Asakura T. Arch Biochem Biophys 229 7-14 (1984)
  32. Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine. Braunstein D, Ansari A, Berendzen J, Cowen BR, Egeberg KD, Frauenfelder H, Hong MK, Ormos P, Sauke TB, Scholl R. Proc Natl Acad Sci U S A 85 8497-8501 (1988)
  33. NMR investigation of the dynamics of tryptophan side-chains in hemoglobins. Yuan Y, Simplaceanu V, Lukin JA, Ho C. J Mol Biol 321 863-878 (2002)
  34. Reaction pathway for the quaternary structure change in hemoglobin. Janin J, Wodak SJ. Biopolymers 24 509-526 (1985)
  35. Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary structure. Smith FR, Simmons KC. Proteins 18 295-300 (1994)
  36. Direct evidence for the role of haem doming as the primary event in the cooperative transition of haemoglobin. Franzen S, Lambry JC, Bohn B, Poyart C, Martin JL. Nat Struct Biol 1 230-233 (1994)
  37. Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces. Vásquez GB, Karavitis M, Ji X, Pechik I, Brinigar WS, Gilliland GL, Fronticelli C. Biophys J 76 88-97 (1999)
  38. Iron-carbon bond lengths in carbonmonoxy and cyanomet complexes of the monomeric hemoglobin III from Chironomus thummi thummi: a critical comparison between resonance Raman and x-ray diffraction studies. Yu NT, Benko B, Kerr EA, Gersonde K. Proc Natl Acad Sci U S A 81 5106-5110 (1984)
  39. The quaternary structure of carbonmonoxy hemoglobin ypsilanti. Janin J, Wodak SJ. Proteins 15 1-4 (1993)
  40. Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems. Luisi B, Shibayama N. J Mol Biol 206 723-736 (1989)
  41. Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan beta 37 mutant. Nagai M, Kaminaka S, Ohba Y, Nagai Y, Mizutani Y, Kitagawa T. J Biol Chem 270 1636-1642 (1995)
  42. The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers. Jewsbury P, Kitagawa T. Biophys J 67 2236-2250 (1994)
  43. Structural and functional studies indicating altered redox properties of hemoglobin E: implications for production of bioactive nitric oxide. Roche CJ, Malashkevich V, Balazs TC, Dantsker D, Chen Q, Moreira J, Almo SC, Friedman JM, Hirsch RE. J Biol Chem 286 23452-23466 (2011)
  44. A new mode for heme-heme interactions in hemoglobin associated with distal perturbations. Levy A, Sharma VS, Zhang L, Rifkind JM. Biophys J 61 750-755 (1992)
  45. Comparing short protein substructures by a method based on backbone torsion angles. Karpen ME, de Haseth PL, Neet KE. Proteins 6 155-167 (1989)
  46. Dynamic properties of oxy- and carbonmonoxyhemoglobin probed by optical spectroscopy in the temperature range of 300-20 K. Leone M, Cupane A, Vitrano E, Cordone L. Biopolymers 26 1769-1779 (1987)
  47. Hemoglobin San Diego/beta zero thalassemia in a Greek adult. Loukopoulos D, Poyart C, Delanoe-Garin J, Matsis C, Arous N, Kister J, Loutradi-Anagnostou A, Blouquit Y, Fessas P, Thillet J. Hemoglobin 10 143-159 (1986)
  48. Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of human hemoglobin alpha-chains. Dalvit C, Wright PE. J Mol Biol 194 329-339 (1987)
  49. Effects of crosslinking on the thermal stability of hemoglobins. II. The stabilization of met-, cyanomet-, and carbonmonoxyhemoglobins A and S with bis(3,5-dibromosalicyl) fumarate. Yang T, Olsen KW. Arch Biochem Biophys 261 283-290 (1988)
  50. Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin. Perutz MF, Fermi G, Shih TB. Proc Natl Acad Sci U S A 81 4781-4784 (1984)
  51. Identification of a nickel(II) binding site on hemoglobin which confers susceptibility to oxidative deamination and intramolecular cross-linking. Levine J, Weickert M, Pagratis M, Etter J, Mathews A, Fattor T, Lippincott J, Apostol I. J Biol Chem 273 13037-13046 (1998)
  52. Metastable photoproducts from carbon monoxide myoglobin. Rousseau DL, Argade PV. Proc Natl Acad Sci U S A 83 1310-1314 (1986)
  53. Sickle cell disease: the proportion of liganded haemoglobin needed to prevent crises. Franklin IM, Rosemeyer MA, Huehns ER. Br J Haematol 54 579-587 (1983)
  54. Structural and functional studies of hemoglobin Barcelona (alpha 2 beta 2 94 Asp (FG1) replaced by His). Consequences of altering an important intrachain salt bridge involved in the alkaline Bohr effect. Wajcman H, Aguilar i Bascompte JL, Labie D, Poyart C, Bohn B. J Mol Biol 156 185-202 (1982)
  55. Diving behaviour and haemoglobin function: the primary structure of the alpha- and beta-chains of the sea turtle (Caretta caretta) and its functional implications. Petruzzelli R, Aureli G, Lania A, Galtieri A, Desideri A, Giardina B. Biochem J 316 ( Pt 3) 959-965 (1996)
  56. Effect of T-R conformational change on sickle-cell hemoglobin interactions and aggregation. Vaiana SM, Rotter MA, Emanuele A, Ferrone FA, Palma-Vittorelli MB. Proteins 58 426-438 (2005)
  57. Crystallographic data for haemoglobin from the lanceolate fluke Dicrocoelium dendriticum. Smit JD, Winterhalter KH. J Mol Biol 146 641-647 (1981)
  58. Nanosecond time-resolved absorption studies of human oxyhemoglobin photolysis intermediates. Ghelichkhani E, Goldbeck RA, Lewis JW, Kliger DS. Biophys J 71 1596-1604 (1996)
  59. Resonance Raman studies of Co-O2 and O-O stretching vibrations in oxy-cobalt hemes. Mackin HC, Tsubaki M, Yu NT. Biophys J 41 349-357 (1983)
  60. Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata). Brix O, Condò SG, Bardgard A, Tavazzi B, Giardina B. Biochem J 271 509-513 (1990)
  61. Assignment of the 1511 cm(-1) UV resonance Raman marker band of hemoglobin to tryptophan. Zhao X, Chen R, Raj V, Spiro TG. Biopolymers 62 158-162 (2001)
  62. Hemoglobin allostery: new views on old players. Miele AE, Bellelli A, Brunori M. J Mol Biol 425 1515-1526 (2013)
  63. Ligand dynamics in the photodissociation of carboxyhemoglobin by subpicosecond transient infrared spectroscopy. Rothberg L, Jedju TM, Austin RH. Biophys J 57 369-373 (1990)
  64. Allosteric kinetics and equilibria differ for carbon monoxide and oxygen binding to hemoglobin. Zhang NQ, Ferrone FA, Martino AJ. Biophys J 58 333-340 (1990)
  65. Molecular characterization of hemoglobin alpha-D chains from Geochelone carbonaria and Geochelone denticulata land turtles. Melo MB, Bordin S, Duarte AS, Ogo SH, Torsoni MA, Saad ST, Costa FF. Comp Biochem Physiol B Biochem Mol Biol 134 389-395 (2003)
  66. Structures and oxygen affinities of crystalline human hemoglobin C (β6 Glu->Lys) in the R and R2 quaternary structures. Shibayama N, Sugiyama K, Park SY. J Biol Chem 286 33661-33668 (2011)
  67. Wavelength-dependent spectral changes accompany CN-hemin binding to human apohemoglobin. Vasudevan G, McDonald MJ. J Protein Chem 19 583-590 (2000)
  68. 1H resonances of proximal histidine in CO complexes of hemoglobins provide a sensitive probe of coordination geometry. Dalvit C, Tennant L, Wright PE. FEBS Lett 213 289-292 (1987)
  69. Allosteric free energy changes at the alpha 1 beta 2 interface of human hemoglobin probed by proton exchange of Trp beta 37. Mihailescu MR, Fronticelli C, Russu IM. Proteins 44 73-78 (2001)
  70. Direct measurement of carbon monoxide bound to different subunits of hemoglobin A in solution and in red cells by infrared spectroscopy. Potter WT, Hazzard JH, Kawanishi S, Caughey WS. Biochem Biophys Res Commun 116 719-725 (1983)
  71. One- and two-dimensional NMR investigations of the heme pocket in free alpha(CO) chains from human hemoglobin. Schaeffer C, Craescu CT, Mispelter J, Garel MC, Rosa J, Lhoste JM. Eur J Biochem 173 317-325 (1988)
  72. Oxygenation of hemoglobin. Correspondence of crystal and solution properties using diffusion coefficient measurements. Sanders AH, Purich DL, Cannell DS. J Mol Biol 147 583-595 (1981)
  73. Sequential assignment of the proton NMR spectrum of isolated alpha(CO) chains from human adult hemoglobin. Martineau L, Craescu CT. Eur J Biochem 205 661-670 (1992)
  74. Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R-->T transition without altering the free energies of oxygenation. Tsai CH, Simplaceanu V, Ho NT, Shen TJ, Wang D, Spiro TG, Ho C. Biophys Chem 100 131-142 (2003)
  75. Site-directed mutagenesis in hemoglobin: test of functional homology of the F9 amino acid residues of hemoglobin alpha and beta chains. Mawjood AH, Miyazaki G, Kaneko R, Wada Y, Imai K. Protein Eng 13 113-120 (2000)
  76. Allostery of the two-state model of hemoglobin studied by ECEPP energy minimization. Seno Y. J Comput Chem 27 701-710 (2006)
  77. Resonance Raman study of deoxy and ligated (O2 and CO) mesoheme IX-reconstituted myoglobin, hemoglobin and its alpha and beta subunits. Podstawka E, Proniewicz LM. J Inorg Biochem 98 1502-1512 (2004)
  78. Structural model for the trialkyltin binding site on cat hemoglobin. Chu AL, Taketa F, Mauk AG, Brayer GD. J Biomol Struct Dyn 3 579-584 (1985)
  79. Assignment of proton resonances in the NMR spectrum of carbonmonoxy hemoglobin beta subunit tetramers. Craescu CT, Mispelter J. Eur J Biochem 176 171-178 (1988)
  80. Soret spectral and bioinformatic approaches provide evidence for a critical role of the alpha -subunit in assembly of tetrameric hemoglobin. Vasudevan G, McDonald MJ. Protein J 25 45-56 (2006)
  81. Studies on cobalt myoglobins and hemoglobins, XIII. A consequence of the occurrence of glutamine at the E7 (58) site of alpha subunits in opossum hemoglobin. Imai K, Ikeda-Saito M, Yonetani T. J Mol Biol 144 551-565 (1980)
  82. The 'natural' hybrid haemoglobin from mule. Interrelationships with its parent haemoglobins from horse and donkey. Condò SG, Coletta M, Cicchetti R, Argentin G, Guerrieri P, Marini S, el-Sherbini S, Giardina B. Biochem J 282 ( Pt 2) 595-599 (1992)
  83. A new relaxed state in horse methemoglobin characterized by crystallographic studies. Sankaranarayanan R, Biswal BK, Vijayan M. Proteins 60 547-551 (2005)
  84. Conformation of the sebacyl beta1Lys82-beta2Lys82 crosslink in T-state human hemoglobin. Ji X, Braxenthaler M, Moult J, Fronticelli C, Bucci E, Gilliland GL. Proteins 30 309-320 (1998)
  85. Conformational Changes and Competitive Adsorption between Serum Albumin and Hemoglobin on Bioceramic Substrates. Gruian CM, Rickert C, Nicklisch SC, Vanea E, Steinhoff HJ, Simon S. Chemphyschem 18 634-642 (2017)
  86. Formation of cross-linked asymmetrical hybrid hemoglobins by double-headed aspirin. Kikugawa K, Adachi K, Kosugi H, Asakura T. Hemoglobin 7 533-553 (1983)
  87. Hemoglobin J Iran alpha 2 beta 2 77 (EF1) his----Asp in a Russian-Armenian family. Delanoe-Garin J, Rhoda MD, Craescu CT, Bardakjian J, Blouquit Y, Lacombe C, Arous N, Poyart C, Ganeval D, Girot R. Hemoglobin 10 365-378 (1986)
  88. Hemoglobins with multiple reactive sulphydryl groups: the reaction of pigeon hemoglobin with 5,5'-dithiobis (2-nitrobenzoic acid). Okonjo KO, Okia TO. J Protein Chem 12 639-646 (1993)
  89. Modeling conformational change in macromolecules as an elastic deformation. Andrews LC, Harrison RW. Proteins 10 162-170 (1991)
  90. Reversible reaction of 5,5'-dithiobis(2-nitrobenzoate) with the hemoglobins of the domestic cat: acetylation of NH3+ terminal group of the beta chain transforms the complex pH dependence of the forward apparent second order rate constant to a simple form. Okonjo KO, Fodeke AA. Biophys Chem 119 196-204 (2006)
  91. XANES spectroscopy sensitivity to small electronic changes. Case of carp azidomethemoglobin. Pin S, Le Tilly V, Alpert B, Cortes R. FEBS Lett 242 401-404 (1989)
  92. CO binding improves the structural, functional, physical and anti-oxidation properties of the PEGylated hemoglobin. Wang Q, Hu T, Sun L, Ji S, Zhao D, Liu J, Ma G, Su Z. Artif Cells Nanomed Biotechnol 43 18-25 (2015)
  93. Evidence for embryonic haemoglobins from Sparus aurata under normal and hypoxic conditions. Mania M, Bruschetta G, Avenoso A, D'Ascola A, Scuruchi M, Campo A, Acri G, Campo S. Fish Physiol Biochem 45 943-954 (2019)
  94. Molecular cloning and characterization of adult Sparus aurata hemoglobin genes. Campo S, Nastasi G, Fedeli D, D'Ascola A, Campo GM, Avenoso A, Ferlazzo A, Calatroni A, Falcioni G. OMICS 14 187-200 (2010)
  95. NMR characterization of a diamagnetic model of unliganded alpha chains from human hemoglobin. Martineau L, Pagnier J, Mispelter J, Craescu CT. Biochimie 74 845-851 (1992)
  96. Tertiary conformational transition in sheep hemoglobins induced by reaction with 5,5 -dithiobis(2-nitrobenzoate) and by binding of inositol hexakisphosphate. Okonjo KO, Adeogun IA, Babalola JO. Biophys Chem 146 65-75 (2010)
  97. Tyrosyl radical in haemoglobin and haptoglobin-haemoglobin complex: how does haptoglobin make haemoglobin less toxic? Svistunenko DA, Manole A. J Biomed Res 34 281-291 (2019)
  98. Binding of a spin-labeled phenylalanine analog to sickle hemoglobin: EPR and NMR studies. Lu HZ, Currie BL, Johnson ME. FEBS Lett 173 259-263 (1984)
  99. Configuron dependence on translation of specific codon pairs. I. Helical regions of human alpha and beta globins. Quinn LY, Krishnaswamy R, Quinn TR. Biochem Biophys Res Commun 97 868-874 (1980)
  100. Methylphenylmercury: a novel heavy atom reagent for protein crystallography. Abraham DJ, Phillips SE, Kennedy PE. J Mol Biol 170 249-252 (1983)
  101. Sequential assignment of proton resonances in the NMR spectrum of Zn-substituted alpha chains from human hemoglobin. Ligand-induced tertiary changes in the heme pocket. Martineau L, Craescu CT. Eur J Biochem 214 383-393 (1993)
  102. Symmetry distortion in the human hemoglobin tetramer induced by asymmetric ligation. Shibayama N. FEBS Lett 586 74-78 (2012)
  103. XANES of carboxy and cyanomet-myoglobin. The role of the distal histidine in the bent Fe-C-O configuration. Bianconi A, Congiu-Castellano A, Giovannelli A, Dell'Ariccia M, Burattini E, Durham PJ, Giacometti GM. Eur Biophys J 14 7-10 (1986)


Related citations provided by authors (1)