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Volumn 120, Issue 34, 1998, Pages 8875-8884

Solution 1H NMR investigation of the molecular and electronic structure of the active site of substrate-bound human heme oxygenase: The nature of the distal hydrogen bond donor to bound ligands

Author keywords

[No Author keywords available]

Indexed keywords

HEME OXYGENASE;

EID: 0032475409     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9815475     Document Type: Article
Times cited : (44)

References (66)
  • 1
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    • note
    • Abbreviations used: hHO, human heme oxygenase-1; rHO, rat heme oxygenase-1; HO-1, heme oxygenase isoform 1; TOCSY, 2D total correlation spectroscopy; NOESY, 2D nuclear Overhauser spectroscopy; Mb, myoglobin; PH, protohemin IX; WEFT, water-eliminated Fourier transform.
  • 2
    • 0014670945 scopus 로고
    • Tenhunen, R.; Marver, H. S.; Schmid, R. J. Biol. Chem. 1969, 244, 6388-6394. Schacter, B. A.; Nelson, E. B.; Marver, H. S.; Masters, B. S. S. J. Biol. Chem. 1972, 247, 3601-3607.
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  • 4
    • 0017850764 scopus 로고
    • Yoshida, T.; Kikuchi, G. J. Biol. Chem. 1978, 253, 4224-4229. Yoshida, T.; Kikuchi, G. J. Biol. Chem. 1979, 254, 4487-4491.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4224-4229
    • Yoshida, T.1    Kikuchi, G.2
  • 5
    • 0018786841 scopus 로고
    • Yoshida, T.; Kikuchi, G. J. Biol. Chem. 1978, 253, 4224-4229. Yoshida, T.; Kikuchi, G. J. Biol. Chem. 1979, 254, 4487-4491.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4487-4491
    • Yoshida, T.1    Kikuchi, G.2
  • 7
  • 33
    • 3543053141 scopus 로고    scopus 로고
    • note
    • 18 exhibits spectroscopic and catalytic properties similar to those of the wild-type enzyme. His 132 thus appears not to be a critical catalytic residue.
  • 50
    • 3543131541 scopus 로고    scopus 로고
    • note
    • Four additional, inconsequentially relaxed, partially resolved labile protons in the 10-12-ppm window similarly are involved in H-bond interactions which are pairwise pseudosymmetric in shifts and dipolar contacts (not shown). The nature of these pseudosymmetric H-bond interactions is not known, but since at least one of these residues, His 132, is completely conserved, it is likely that the interactions are important in stabilizing the structure required for catalysis.
  • 51
    • 3543123199 scopus 로고    scopus 로고
    • note
    • αH with a strong, low-field shift even in diamagnetic hHO, and hence can be assumed to represent the same residue. Similar comparison between hHO and hHO-PH-CN for other aromatic rings failed to provide any additional convincing correlations.
  • 60
    • 3543116341 scopus 로고
    • La Mar, G. N., Horrocks, W. D., Jr., Holm, R. H., Eds.; Academic Press: New York, Chapter 2
    • αH, the contact shift is only about one-half as large as that for a methyl for the same pyrrole carbon π spin density (La Mar, G. N. In NMR of Paramagnetic Molecules; La Mar, G. N., Horrocks, W. D., Jr., Holm, R. H., Eds.; Academic Press: New York, 1973; Chapter 2).
    • (1973) NMR of Paramagnetic Molecules
    • La Mar, G.N.1
  • 64
    • 0001052034 scopus 로고
    • Rajarathnam, K.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. J. Am. Chem. Soc. 1992, 114, 9048-9058. Rajarathnam, K.; Qin, J.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Biochemistry 1993, 32, 5670-5680. Rajarathnam, K.; Qin, J.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Biochemistry 1994, 33, 5493-5501.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9048-9058
    • Rajarathnam, K.1    La Mar, G.N.2    Chiu, M.L.3    Sligar, S.G.4
  • 65
    • 0027245807 scopus 로고
    • Rajarathnam, K.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. J. Am. Chem. Soc. 1992, 114, 9048-9058. Rajarathnam, K.; Qin, J.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Biochemistry 1993, 32, 5670-5680. Rajarathnam, K.; Qin, J.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Biochemistry 1994, 33, 5493-5501.
    • (1993) Biochemistry , vol.32 , pp. 5670-5680
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  • 66
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    • Rajarathnam, K.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. J. Am. Chem. Soc. 1992, 114, 9048-9058. Rajarathnam, K.; Qin, J.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Biochemistry 1993, 32, 5670-5680. Rajarathnam, K.; Qin, J.; La Mar, G. N.; Chiu, M. L.; Sligar, S. G. Biochemistry 1994, 33, 5493-5501.
    • (1994) Biochemistry , vol.33 , pp. 5493-5501
    • Rajarathnam, K.1    Qin, J.2    La Mar, G.N.3    Chiu, M.L.4    Sligar, S.G.5


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