MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain.

[1]  H. R. Faber,et al.  1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin. , 1995, Structure.

[2]  M. Ubbink,et al.  Characterization of mutant Met100Lys of cytochrome c-550 from Thiobacillus versutus with lysine-histidine heme ligation. , 1994, Biochemistry.

[3]  U. Muller-eberhard,et al.  Proton NMR study of the heme complex of hemopexin. , 1994, Biochimica et biophysica acta.

[4]  J. L. Smith,et al.  Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. , 1994, Structure.

[5]  G. Loew,et al.  Determinants of the spin state of the resting state of cytochrome P450cam , 1993 .

[6]  S. Inglis,et al.  Identification of Lys79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c , 1993 .

[7]  W. Morgan,et al.  Characterization of hemopexin and its interaction with heme by differential scanning calorimetry and circular dichroism. , 1993, Biochemistry.

[8]  J. Alam,et al.  Identification of the histidine residues of hemopexin that coordinate with heme-iron and of a receptor-binding region. , 1993, The Journal of biological chemistry.

[9]  Ann Smith,et al.  Further characterization of structural determinants of rabbit hemopexin function , 1991, Journal of protein chemistry.

[10]  J. Gitlin,et al.  Rat hemopexin. Molecular cloning, primary structural characterization, and analysis of gene expression. , 1991, Biochemistry.

[11]  R. Hunt,et al.  Hemopexin joins transferrin as representative members of a distinct class of receptor-mediated endocytic transport systems. , 1990, European journal of cell biology.

[12]  G. Moore,et al.  Cytochromes c , 1990, Springer Series in Molecular Biology.

[13]  G. Moore,et al.  N.m.r., e.p.r. and magnetic-c.d. studies of cytochrome f. Identity of the haem axial ligands. , 1988, The Biochemical journal.

[14]  T. P. Conway,et al.  Use of hemopexin domains and monoclonal antibodies to hemopexin to probe the molecular determinants of hemopexin-mediated heme transport. , 1988, The Journal of biological chemistry.

[15]  F. Tatum,et al.  Importance of ligand-induced conformational changes in hemopexin for receptor-mediated heme transport. , 1988, The Journal of biological chemistry.

[16]  K. Wüthrich.  NMR of proteins and nucleic acids , 1988 .

[17]  A. Thomson,et al.  Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c. , 1987, The Biochemical journal.

[18]  B C Finzel,et al.  Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. , 1986, Biochemistry.

[19]  A. Mauk,et al.  Kinetics of hemoprotein reduction and interprotein heme transfer. , 1985, Biochemistry.

[20]  W. Morgan,et al.  Hemopexin-mediated heme transport to the liver. Evidence for a heme-binding protein in liver plasma membranes. , 1985, The Journal of biological chemistry.

[21]  P. Argos,et al.  The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology. , 1985, Nucleic acids research.

[22]  G. Palmer.  The electron paramagnetic resonance of metalloproteins. , 1985, Biochemical Society transactions.

[23]  F. S. Mathews,et al.  A spectroscopic investigation of the structure and redox properties of Escherichia coli cytochrome b-562. , 1985, Biochimica et biophysica acta.

[24]  K. Wüthrich,et al.  Amino acid sequence, haem-iron co-ordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes , 1985, Quarterly Reviews of Biophysics.

[25]  W. Morgan,et al.  Domain structure of rabbit hemopexin. Isolation and characterization of a heme-binding glycopeptide. , 1984, The Journal of biological chemistry.

[26]  G. Moore,et al.  Characterisation of ionisations that influence the redox potential of mitochondrial cytochrome c and photosynthetic bacterial cytochromes c2 , 1984 .

[27]  J. Salerno.  Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase. , 1984, The Journal of biological chemistry.

[28]  B. Katz,et al.  Low-spin ferric porphyrin complexes: analysis of the electronic structure based on single-crystal electron spin resonance measurements , 1983 .

[29]  A. Smith,et al.  Haem transport to the liver by haemopexin. Receptor-mediated uptake with recycling of the protein. , 1979, The Biochemical journal.

[30]  L. Vickery,et al.  Magnetic and natural circular dichroism of metalloporphyrin complexes of human and rabbit hemopexin. , 1978, The Journal of biological chemistry.

[31]  S. Sligar,et al.  Coupling of spin, substrate, and redox equilibria in cytochrome P450. , 1976, Biochemistry.

[32]  A. Bearden,et al.  Heme complexes of rabbit hemopexin, human hemopexin and human serum albumin: electron spin resonance and Mssbauer spectroscopic studies. , 1974, Biochemical and biophysical research communications.

[33]  Z. Hrkal,et al.  Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin. , 1974, European journal of biochemistry.

[34]  U. Muller-eberhard,et al.  Binding of porphyrins to rabbit hemopexin and albumin. , 1973, The Journal of biological chemistry.

[35]  S. H. Koenig,et al.  Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C. , 1971, Biochemical and biophysical research communications.

[36]  U. Muller-eberhard,et al.  Tissue localization of the heme-hemopexin complex in the rabbit and the rat as studied by light microscopy with the use of radioisotopes. , 1970, The Journal of laboratory and clinical medicine.

[37]  A. Thomson,et al.  Magnetic Circular Dichroism of Hemoproteins. , 1991 .

[38]  R. Schowen,et al.  [29] Solvent isotope effects on enzyme systems , 1982 .

[39]  Oleg Jardetzky,et al.  NMR in molecular biology , 1981 .

[40]  R. Shulman.  Biological applications of magnetic resonance , 1979 .