Is the CO adduct of myoglobin bent, and does it matter?

Accounts of Chemical Research

Volumn 34, Issue 2, 2001, Pages 137-144

  Spiro, T G ^a   Kozlowski, P M ^b  

^a PRINCETON UNIVERSITY   (United States)

^b UNIVERSITY OF LOUISVILLE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; HEMOPROTEIN; MYOGLOBIN;

ARTICLE; BINDING AFFINITY; CHEMICAL STRUCTURE; ELECTRICITY; HYDROGEN BOND; LIGAND BINDING; MOLECULAR DYNAMICS; MUTATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STEREOSPECIFICITY; STRUCTURE ANALYSIS; THERMODYNAMICS;

CARBON MONOXIDE; ELECTROSTATICS; HYDROGEN BONDING; MOLECULAR STRUCTURE; MUTATION; MYOGLOBIN; THERMODYNAMICS;

EID: 0035110522     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar000108j     Document Type: Article

References (57)

1. A mechanism essential to life
2. Will the real FeCO please stand up?
3. 2 and CO
4. Deformability of Fe(II)CO and Fe(III)CN groups in heme protein models: Nonlocal density functional theory calculations
5. Modulating carbon monoxide binding affinity and kinetics in myoglobin: The roles of the distal histidine and the heme pocket docking site
6. Myoglobin and CO: Structure, energetics, and disorder
7. 2, NO, and CO by electrostatic interactions with the bound ligand
8. Synthetic models for hemoglobin and myoglobin
9. Mechanisms of ligand recognition in myoglobin
10. 2 and CO binding to metalloporphyrins and heme proteins
11. 2 binding to heme from vibrational spectroscopy and DFT analysis
12. Steric contributions to CO binding in heme proteins: A density functional analysis of FeCO vibrations and deformability
13. X-ray structure and refinement of carbon-monoxy Fe(II)-myoglobin at 1.5 Å resolution
14. Neutron diffraction study of carbon monoxymyoglobin
15. How far can proteins bend the FeCO Unit? Distal polar and steric effects in heme proteins and models
16. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
17. Crystal structures of CO-, deoxy- and met-myoglobins at various Ph values
18. A steric mechanism for inhibition of CO binding to heme proteins
19. Crystal structures of myoglobin-ligand complexes at near-atomic resolution
20. Structural characterization of a sterically encumbered iron(III) porphyrin CO complex
21. Structure of a carbon-monoxide adduct of a capped porphyrin - FE(C2-CAP)(CO)(1-Methylimidazole)
22. Synthetic heme dioxygen complexes
23. Structural characterization of five sterically protected porphyrins
24. Is bound CO linear or bent in heme-proteins - Evidence from resonance Raman and infrared spectroscopic data
25. Iron-57 NMR chemical shifts and mossbauer quadrupole splittings in metalloporphyrins, ferrocytochrome c, and myoglobins: A density functional theory investigation
26. 57Fe mossbauer and infrared spectroscopies
27. Determination of CO orientation in myoglobin by single-crystal infrared linear dichroism
28. Infrared crystalography: Structural refinement through spectroscopy
29. Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin
30. Iron carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared-spectroscopy
31. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O
32. Vibrational stark spectroscopy in proteins: A probe and calibration for electrostatic fields
33. Discordant results on FeCO deformability in heme proteins reconciled by density functional theory
34. Application of molecular-dynamics and free-energy perturbation-methods to metalloporphyrin-ligand systems. 2. CO and dioxygen binding to myoglobin
35. Deformability of heme protein CO adducts: FT-IR assignment of the FeCO bending mode
36. Carbonyl tilting and bending potential energy surface of carbon monoxyhemes
37. Stereochemistry of carbon-monoxide binding to myoglobin and hemoglobin
38. Stereochemistry of carbon-monoxide binding to myoglobin and hemoglobin
39. Nature of the iron-oxygen bond in oxyhaemoglobin
40. Neutron-diffraction reveals oxygen-histidine hydrogenbond in oxymyoglobin
41. NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin
42. Evidence for hydrogen bonding effects in the iron ligand vibrations of carbonmonoxy myoglobin
43. Bound CO is a molecular probe of electrostatic potential in the distal pocket of myoglobin
44. 2 by myoglobin
45. nd generation force-field for the simulation of proteins, nucleic-acids, and organic-molecules
46. Solvent isotope effects on NMR spectral parameters in high-spin ferric hemoproteins - An indirect probe for distal hydrogen-bonding
47. Identification of conformational substrates involved in nitric oxide binding to ferric and ferrous myoglobin through difference Fourier Transform Infrared Spectroscopy (FTIR)
48. Photolysis-induced structural-changes in single-crystals of carbonmonoxy myoglobin at 40K
49. Crystal-structure of photolyzed carbonmonoxy-myoglobin
50. Analysis of the kinetic barriers for ligand-binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques
51. Kinetic pathways and barriers for ligand binding to myoglobin
52. New light on allostery: Dynamic resonance Raman spectroscopy of hemoglobin kempsey