Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin
Journal Article
·
· Proc. Natl. Acad. Sci. U.S.A.; (United States)
A molecular dynamics simulation of the photodissociation of carbon monoxide from the alpha subunit of hemoglobin is described. To initiate photodissociation, trajectories of the liganded molecule were interrupted, the iron-carbon monoxide bond was broken, and the parameters of the iron-nitrogen bonds were simultaneously altered to produce a deoxyheme conformation. Heme potential functions were used that reproduce the energies and forces for the iron out-of-plane motion obtained from quantum mechanical calculations. The effect of the protein on the rate and extent of the displacement of the iron from the porphyrin plane was assessed by comparing the results with those obtained for an isolated complex of heme with imidazole and carbon monoxide. The half-time for the displacement of the iron from the porphyrin plane was found to be 50-150 fs for both the protein and the isolated complex. These results support the interpretation of optical absorption studies using 250-fs laser pulses that the iron is displaced from the porphyrin plane within 350 fs in both hemoglobin and a free heme complex in solution.
- Research Organization:
- National Institute of Arthritis, Bethesda, MD
- OSTI ID:
- 5646587
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 82:7; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
Similar Records
The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin
Photodissociation of carbon monoxide and dioxygen forms of synthetic heme complexes studied by using picosecond absorption spectroscopy. Evidence of a pseudo-four-coordinate intermediate
A comparative study of low-temperature and time resolved FTIR difference spectra of cytochrome oxidases
Journal Article
·
Thu Mar 31 23:00:00 EST 1988
· Proceedings of the National Academy of Sciences of the United States of America; (USA)
·
OSTI ID:6832540
Photodissociation of carbon monoxide and dioxygen forms of synthetic heme complexes studied by using picosecond absorption spectroscopy. Evidence of a pseudo-four-coordinate intermediate
Journal Article
·
Wed Oct 01 00:00:00 EDT 1986
· J. Am. Chem. Soc.; (United States)
·
OSTI ID:5057537
A comparative study of low-temperature and time resolved FTIR difference spectra of cytochrome oxidases
Conference
·
Tue Dec 30 23:00:00 EST 1997
·
OSTI ID:560208
Related Subjects
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400500 -- Photochemistry
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
CARBON COMPOUNDS
CARBON MONOXIDE
CARBON OXIDES
CARBOXYLIC ACIDS
CHALCOGENIDES
CHEMICAL REACTIONS
DECOMPOSITION
DISSOCIATION
DISSOCIATION ENERGY
ELEMENTS
ENERGY
GLOBIN
HEME
HEMOGLOBIN
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
IRON
MAMMALS
MAN
METALS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDES
OXYGEN COMPOUNDS
PHOTOCHEMICAL REACTIONS
PHOTOLYSIS
PIGMENTS
PORPHYRINS
PRIMATES
PROTEINS
SIMULATION
TRANSITION ELEMENTS
VERTEBRATES
400500 -- Photochemistry
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
CARBON COMPOUNDS
CARBON MONOXIDE
CARBON OXIDES
CARBOXYLIC ACIDS
CHALCOGENIDES
CHEMICAL REACTIONS
DECOMPOSITION
DISSOCIATION
DISSOCIATION ENERGY
ELEMENTS
ENERGY
GLOBIN
HEME
HEMOGLOBIN
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
IRON
MAMMALS
MAN
METALS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDES
OXYGEN COMPOUNDS
PHOTOCHEMICAL REACTIONS
PHOTOLYSIS
PIGMENTS
PORPHYRINS
PRIMATES
PROTEINS
SIMULATION
TRANSITION ELEMENTS
VERTEBRATES