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. 1988 Nov;85(22):8492–8496. doi: 10.1073/pnas.85.22.8492

Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin.

P Ormos 1, D Braunstein 1, H Frauenfelder 1, M K Hong 1, S L Lin 1, T B Sauke 1, R D Young 1
PMCID: PMC282484  PMID: 3186739

Abstract

Fourier transform infrared spectroscopy of the CO stretch bands in carbonmonoxymyoglobin (MbCO) reveals three major bands implying that MbCO exists in three major substates, A0, A1, and A3. After photolysis at low temperatures the CO is in the heme pocket, and the resulting CO stretch bands represent the B substates. Photoselection experiments determine the orientation of CO in the A (bound) and B (photolyzed) substates: Small fractions of MbCO are photolyzed at 10 K with linearly polarized light at 540 nm. The resulting linear dichroism in the A and B IR bands yields the tilt angle between the heme normal and CO. The average angles are as follows: alpha (A0) = 15 degrees +/- 3 degrees; alpha (A1) = 28 degrees +/- 2 degrees, and alpha (A3) = 33 degrees +/- 4 degrees. The A bands are inhomogeneously broadened; the angle alpha shows a wavenumber dependence within the A bands. The wavenumber dependence is interpreted as a distribution of the tilt angle within the individually inhomogeneous A substates, thus providing a structural parameter to characterize the distribution of the conformational substates. The B substates exhibit no induced linear dichroism; in the photolyzed substates the ligand is randomly oriented with respect to the heme plane. The present results together with earlier data on static and kinetic properties of CO binding to Mb establish relations among spectroscopic, structural, energetic, and functional parameters.

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Selected References

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  1. Alben J. O., Beece D., Bowne S. F., Doster W., Eisenstein L., Frauenfelder H., Good D., McDonald J. D., Marden M. C., Moh P. P. Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures. Proc Natl Acad Sci U S A. 1982 Jun;79(12):3744–3748. doi: 10.1073/pnas.79.12.3744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alberding N., Chan S. S., Eisenstein L., Frauenfelder H., Good D., Gunsalus I. C., Nordlund T. M., Perutz M. F., Reynolds A. H., Sorensen L. B. Binding of carbon monoxide to isolated hemoglobin chains. Biochemistry. 1978 Jan 10;17(1):43–51. doi: 10.1021/bi00594a007. [DOI] [PubMed] [Google Scholar]
  3. Ansari A., Berendzen J., Bowne S. F., Frauenfelder H., Iben I. E., Sauke T. B., Shyamsunder E., Young R. D. Protein states and proteinquakes. Proc Natl Acad Sci U S A. 1985 Aug;82(15):5000–5004. doi: 10.1073/pnas.82.15.5000. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ansari A., Berendzen J., Braunstein D., Cowen B. R., Frauenfelder H., Hong M. K., Iben I. E., Johnson J. B., Ormos P., Sauke T. B. Rebinding and relaxation in the myoglobin pocket. Biophys Chem. 1987 May 9;26(2-3):337–355. doi: 10.1016/0301-4622(87)80034-0. [DOI] [PubMed] [Google Scholar]
  5. Austin R. H., Beeson K. W., Eisenstein L., Frauenfelder H., Gunsalus I. C. Dynamics of ligand binding to myoglobin. Biochemistry. 1975 Dec 2;14(24):5355–5373. doi: 10.1021/bi00695a021. [DOI] [PubMed] [Google Scholar]
  6. Caughey W. S., Shimada H., Choc M. G., Tucker M. P. Dynamic protein structures: infrared evidence for four discrete rapidly interconverting conformers at the carbon monoxide binding site of bovine heart myoglobin. Proc Natl Acad Sci U S A. 1981 May;78(5):2903–2907. doi: 10.1073/pnas.78.5.2903. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Coughey W. S., Alben J. O., McCoy S., Boyer S. H., Charache S., Hathaway P. Differences in the infrared stretching frequency of carbon monoxide bound to abnormal hemoglobins. Biochemistry. 1969 Jan;8(1):59–62. doi: 10.1021/bi00829a009. [DOI] [PubMed] [Google Scholar]
  8. Eaton W. A., Hofrichter J. Polarized absorption and linear dichroism spectroscopy of hemoglobin. Methods Enzymol. 1981;76:175–261. doi: 10.1016/0076-6879(81)76126-3. [DOI] [PubMed] [Google Scholar]
  9. Frauenfelder H., Parak F., Young R. D. Conformational substates in proteins. Annu Rev Biophys Biophys Chem. 1988;17:451–479. doi: 10.1146/annurev.bb.17.060188.002315. [DOI] [PubMed] [Google Scholar]
  10. Frauenfelder H., Petsko G. A., Tsernoglou D. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics. Nature. 1979 Aug 16;280(5723):558–563. doi: 10.1038/280558a0. [DOI] [PubMed] [Google Scholar]
  11. Heidner E. J., Ladner R. C., Perutz M. F. Structure of horse carbonmonoxyhaemoglobin. J Mol Biol. 1976 Jul 5;104(3):707–722. doi: 10.1016/0022-2836(76)90130-3. [DOI] [PubMed] [Google Scholar]
  12. Huber R., Epp O., Formanek H. Structures of deoxy- and carbonmonoxy-erythrocruorin. J Mol Biol. 1970 Sep 14;52(2):349–354. doi: 10.1016/0022-2836(70)90035-5. [DOI] [PubMed] [Google Scholar]
  13. Kuriyan J., Wilz S., Karplus M., Petsko G. A. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution. J Mol Biol. 1986 Nov 5;192(1):133–154. doi: 10.1016/0022-2836(86)90470-5. [DOI] [PubMed] [Google Scholar]
  14. Makinen M. W., Houtchens R. A., Caughey W. S. Structure of carboxymyoglobin in crystals and in solution. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6042–6046. doi: 10.1073/pnas.76.12.6042. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Moore J. N., Hansen P. A., Hochstrasser R. M. Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy. Proc Natl Acad Sci U S A. 1988 Jul;85(14):5062–5066. doi: 10.1073/pnas.85.14.5062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Norvell J. C., Nunes A. C., Schoenborn B. P. Neutron diffraction analysis of myoglobin: structure of the carbon monoxide derivative. Science. 1975 Nov 7;190(4214):568–570. doi: 10.1126/science.1188354. [DOI] [PubMed] [Google Scholar]
  17. Peng S. M., Ibers J. A. Stereochemistry of carbonylmetalloporphyrins. The structure of (pyridine)(carbonyl)(5, 10, 15, 20-tetraphenylprophinato)iron(II). J Am Chem Soc. 1976 Dec 8;98(25):8032–8036. doi: 10.1021/ja00441a025. [DOI] [PubMed] [Google Scholar]
  18. Szabo A. Kinetics of hemoglobin and transition state theory. Proc Natl Acad Sci U S A. 1978 May;75(5):2108–2111. doi: 10.1073/pnas.75.5.2108. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tsubaki M., Hiwatashi A., Ichikawa Y. Effects of cholesterol and adrenodoxin binding on the heme moiety of cytochrome P-450scc: a resonance Raman study. Biochemistry. 1986 Jun 17;25(12):3563–3569. doi: 10.1021/bi00360a014. [DOI] [PubMed] [Google Scholar]
  20. Uno T., Nishimura Y., Tsuboi M., Makino R., Iizuka T., Ishimura Y. Two types of conformers with distinct Fe-C-O configuration in the ferrous CO complex of horseradish peroxidase. Resonance Raman and infarared spectroscopic studies with native and deuteroheme-substituted enzymes. J Biol Chem. 1987 Apr 5;262(10):4549–4556. [PubMed] [Google Scholar]
  21. Yu N. T., Kerr E. A., Ward B., Chang C. K. Resonance Raman detection of Fe-CO stretching and Fe-C-O bending vibrations in sterically hindered carbonmonoxy "strapped hemes". A structural probe of Fe-C-O distortion. Biochemistry. 1983 Sep 13;22(19):4534–4540. doi: 10.1021/bi00288a028. [DOI] [PubMed] [Google Scholar]

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