Ligand binding in the ferric and ferrous states of Paramecium hemoglobin

Biochemistry

Volumn 39, Issue 46, 2000, Pages 14330-14340

  Das, T K ^a   Weber, R E ^b   Dewilde, S ^c   Wittenberg, J B ^a   Wittenberg, B A ^a   Yamauchi, K ^d   Van Hauwaert, M L ^c   Moens, L ^c   Rousseau, D L ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b AARHUS UNIVERSITY   (Denmark)

^c UNIVERSITY OF ANTWERP   (Belgium)

^d SHIZUOKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

FERRIC ION; FERROUS ION; HEMOGLOBIN; MYOGLOBIN;

AMINO ACID COMPOSITION; ARTICLE; DISSOCIATION; HYDROGEN BOND; LIGAND BINDING; MOLECULAR STABILITY; NONHUMAN; OXIDATION; OXYGEN AFFINITY; OXYGEN SUPPLY; PARAMECIUM; PKA; PRIORITY JOURNAL; RAMAN SPECTROMETRY;

AMINO ACID SEQUENCE; ANIMALS; CARBON MONOXIDE; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HEMOGLOBINS; HUMANS; KINETICS; LIGANDS; METHEMOGLOBIN; MOLECULAR SEQUENCE DATA; OXYGEN; OXYHEMOGLOBINS; PARAMECIUM; PROTEIN BINDING; SPECTRUM ANALYSIS, RAMAN;

CETACEA; INVERTEBRATA; OXY; PARAMECIUM; PARAMECIUM CAUDATUM; PHYSETER CATODON; PROTOZOA;

EID: 0034700261     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi001681d     Document Type: Article

References (76)

1. Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
2. Mechanisms of cytoplasmic hemoglobin and myoglobin function
3. Globins in nonvertebrate species: Dispersal by horizontal gene transfer and evolution of the structure-function relationships
4. Plant hemoglobins
5. Role for the Salmonella flavohemoglobin in protection from nitric oxide
6. Nitric oxide dioxygenase: An enzymic function for flavohemoglobin
7. Ascaris haemoglobin is a nitric oxide-activated 'deoxygenase'
8. 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
9. Altering hemoglobin levels changes energy status in maize cells under hypoxia
10. Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heine
11. The heme environment in barley hemoglobin
12. Chlamydomonas chloroplast ferrous hemoglobin. Heine pocket structure and reactions with ligands
13. Distal interactions in the cyanide complex of ferric Chlamydomonas hemoglobin
14. A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties
15. Origin of the anomalous Fe-CO stretching mode in the CO complex of Ascaris hemoglobin
16. Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin
17. The tyrosine B10 hydroxyl is crucial for oxygen avidity of Ascaris hemoglobin
18. A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis
19. A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins (Ascaris suum and Lucina pectinata)
20. Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29→Tyr sperm whale myoglobin mutant
21. Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands
22. Hemoglobins of the Lucina pectinata/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins
23. A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family
24. Nonvertebrate hemoglobins: Structural bases for reactivity
25. The structure of Ascaris hemoglobin domain I at 2.2 A resolution: Molecular features of oxygen avidity
26. Protozoan myoglobin from Paramecium caudatum. Its unusual amino acid sequence
27. The unique structure of the Paramecium caudatum hemoglobin gene: The presence of one intron in the middle of the coding region
28. Structure and evolution of Paramecium hemoglobin genes
29. Nuclear genes encoding chloroplast hemoglobins in the unicellular green alga Chlamydomonas eugametos
30. Synthesis of a gene for human growth hormone and its expression in Escherichia coli
31. Structural, functional and genetic characterization of Gastrophilus hemoglobin
32. 2 affinity in lugworm erythrocruorin
33. Use of ionic and zwitterionic (Tris/BisTris and HEPES) buffers in studies on hemoglobin function
34. Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands
35. Studies on the reaction of isocyanides with haemproteins. I. Equilibria and kinetics of the binding to the isolated chains of human haemoglobin
36. Preliminary observations on isolated Paramecium hemoglobin
37. Oxygen binding to myoglobins and their cobalt analogues
38. Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
39. The heme protein structure and the iron histidine stretching mode
40. Transient and cryogenic studies of photodissociated hemoglobin and myoglobin
41. Resonance Raman scattering: A probe of heme protein-bound nitric oxide
42. Confirmation of the assignment of the iron-histidine stretching mode in myoglobin
43. Time-resolved resonance Raman spectroscopy as a probe of structure, dynamics and reactivity of hemoglobin
44. Temperature-dependent quaternary state relaxation in sol-gel encapsulated hemoglobin
45. Protozoan myoglobin from Paramecium caudatum. Its autoxidation reaction and hemichrome formation
46. Observation of a new oxygen-isotope-sensitive Raman band for oxyhemoproteins and its implications in heine pocket structures
47. Structural characterization of oxidized dimeric Scapharca inaequivalvis hemoglobin by resonance Raman spectroscopy
48. Functional differentiation in trematode hemoglobin isoforms
49. Oxygen equilibrium studies of the radular muscle myoglobins of the gastropod molluscs, Buccinum undatum L. and Busycon canaliculatum L
50. Nonvertebrate hemoglobins: Functions and molecular adaptations
51. Characterization of the myoglobin and its coding gene of the mollusk Biomphalaria glabrata
52. Trematode myoglobins, functional molecules with a distal tyrosine
53. Structural characterization of an Ascaris myoglobin
54. 2-binding kinetics of a recombinant protein synthesized in Escherichia coli
55. The iron-proximal histidine linkage and protein control of oxygen binding in hemoglobin. A transient Raman study
56. Resonance Raman scattering studies of the quaternary structure transition in hemoglobin
57. A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue
58. Evidence for hydrogen bonding effects in the iron ligand vibrations of carbonmonoxy myoglobin
59. Ligand binding to heme proteins. II. Transitions in the heme pocket of myoglobin
60. Spectroscopic studies of myoglobin at low pH: Heme structure and ligation
61. Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin
62. Bound CO as a molecular probe of electrostatic potential in the distal pocket of myoglobin
63. How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models
64. 13CO-labeled species
65. Identification of the iron-carbonyl stretch in distal histidine mutants of carbonmonoxymyoglobin
66. Identification of the overtone of the Fe-CO stretching mode in heme proteins: A probe of the heme active site
67. Functions of cytoplasmic hemoglobins and myohemerythrin
68. On the significance of the retention of ligand by protein
69. Rates of reaction of Ascaris haemoglobins with ligands
70. The kinetics of ligand binding to plant hemoglobins. Structural implications
71. Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine
72. The role of the distal histidine in myoglobin and haemoglobin
73. Trematode hemoglobins show exceptionally high oxygen affinity
74. Two hemoglobin genes in Arabidopsis thaliana: The evolutionary origins of leghemoglobins