The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme

Proteins: Structure, Function and Genetics

Volumn 46, Issue 3, 2002, Pages 268-277

  Kundu, Suman ^a   Snyder, Barry ^a   Das, Kaustuv ^a   Chowdhury, Pramit ^a   Park, Jaehun ^a   Petrich, Jacob W ^a   Hargrove, Mark S ^a  

^a IOWA STATE UNIVERSITY   (United States)

Author keywords

F helix; Geminate recombination; Leghemoglobin; Ligand binding; Oxygen dissociation; Proximal heme pocket

Indexed keywords

HEME; HEMOGLOBIN; HISTIDINE; LEGHEMOGLOBIN; MYOGLOBIN;

BINDING AFFINITY; CONFERENCE PAPER; LIGAND BINDING; MUTAGENESIS; MUTATION; NONHUMAN; OXYGEN AFFINITY; OXYGEN DISSOCIATION CURVE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN STABILITY; PROTEIN STRUCTURE; REGULATORY MECHANISM; SOYBEAN; SPECTROSCOPY; STRUCTURE ANALYSIS; WHALE;

ANIMALS; CARBON MONOXIDE; HEME; IRON; KINETICS; LEGHEMOGLOBIN; LIGANDS; MODELS, MOLECULAR; MUTATION; MYOGLOBIN; OXYGEN; WHALES;

CETACEA; GLYCINE MAX; PHYSETER CATODON;

EID: 0037083579     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10048     Document Type: Conference Paper

References (56)

1. Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution
2. Nitric oxide dioxygenase: An enzymatic function for flavohemoglobin
3. Crystal structure of a nonsymbiotic plant hemoglobin
4. A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family
5. The kinetics of ligand binding to plant hemoglobins: Structural implications
6. Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin: Site-directed mutagenesis of the distal histidine
7. Mechanisms of ligand recognition in myoglobin
8. The structure of deoxy- and oxyleghaemoglobin from lupin
9. Studies on cobalt myoglobins and hemoglobins: The interaction of molecular oxygen with leghemoglobin
10. Role of hydrogen bonding to bound dioxygen in soybean leghemoglobin
11. Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants
12. Stereochemistry of cooperative effects in haemoglobin
13. 2 and CO binding to α and β subunits within R-and T-state human hemoglobin
14. The stereochemical mechanism of the co-operative effects in hemoglobin revisited
15. Trans-substitution of the proximal hydrogen bond in myoglobin. I. Structural consequences of hydrogen bond deletion
16. Distal ligand reactivity and quaternary structure studies of proximally detached hemoglobins
17. Waterproofing the heme pocket: Role of proximal amino acid side chains in preventing hemin loss from myoglobin
18. Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93→Gly
19. Functional cavities in proteins: A general method for proximal ligand substitution in myoglobin
20. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
21. Structure of myoglobin refined at 2.0 Å resolution. II. Structure of deoxymyoglobin from sperm whale
22. NMR studies of the conformations of leghemoglobins from soybean and lupin
23. Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin
24. Electrostatic modification of the active site of myoglobin: Characterization of the proximal Ser92Asp variant
25. Functional implications of the proximal hydrogen-bonding network in myoglobin: A resonance raman and kinetic study of leu89, ser92, his97, and F-helix swap mutants
26. Trans-substitution of the proximal hydrogen bond in myoglobin. II. Energetics, functional consequences, and implications for hemoglobin allostery
27. 2, NO, and CO by electrostatic interactions with the bound ligand
28. A kinetic description of ligand binding to sperm whale myoglobin
29. Kinetic pathways and barriers for ligand binding to myoglobin
30. Heme protein dynamics revealed by geminate nitric oxide recombination in mutants of iron and cobalt myoglobin
31. Ligand binding and protein relaxation in heme proteins: A room temperature analysis of NO geminate recombination
32. Ultrafast measurements of geminate recombination of NO with site-specific mutants of human myoglobin
33. Dependence of NO recombination dynamics in horse myoglobin on solution glycerol content
34. Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobin
35. Rate theories and puzzles of hemeprotein kinetics
36. Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques
37. Comparison of the dynamics of myoglobin in different crystal forms
38. High-level expression of sperm whale myoglobin in Escherichia coli
39. Cooperativity in the dissociation of nitric oxide from hemoglobin
40. Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells
41. Structural and functional effects of apolar mutations of the distal valine in myoglobin
42. A flash photolysis method to characterize hexacoordinate hemoglobin kinetics
43. Hypericin, hypocrellin, and model compounds: Primary photo-processes of light-induced antiviral agents
44. His64(E7)→Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation
45. Spectroscopic study of Ser92 mutants of human myoglobin: Hydrogen bonding effect of Ser92 to proximal His93 on structure and property of myoglobin
46. Influence of proximal side mutations on the molecular and electronic structure of cyanomet myoglobin: An 1H NMR study
47. Hydrogen bonding modulates binding of exogenous ligands in a myoglobin proximal cavity mutant
48. A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin
49. Leghemoglobin: An electron paramagnetic resonance and optical spectral study of the free protein and its complexes with nicotinate and acetate
50. Distal pocket residues affect picosecond ligand recombination in myoglobin: An experimental and molecular dynamics study of position 29 mutants
51. A comparison of the geminate recombination kinetics of several monomeric heme proteins
52. Quaternary structure regulates hemin dissociation from human hemoglobin
53. The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin
54. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
55. Structural factors governing hemin dissociation from metmyoglobin