Mutagenesis of residues 27 and 78 modulates heme orientation in cytochrome b 5

[1]  F. Muskett,et al.  The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods. , 1996, Journal of molecular biology.

[2]  P. Shewry,et al.  Expression of a biologically active plant cytochrome b5 in Escherichia coli. , 1994, The Biochemical journal.

[3]  W. Funk,et al.  Recombinant human erythrocyte cytochrome b5. , 1994, Biochemistry.

[4]  H. Stunnenberg,et al.  Improved method for PCR-mediated site-directed mutagenesis. , 1994, Nucleic acids research.

[5]  D. Whitford,et al.  The expression of bovine microsomal cytochrome b5 in Escherichia coli and a study of the solution structure and stability of variant proteins. , 1993, Protein engineering.

[6]  L. Waskell,et al.  The function of tyrosine 74 of cytochrome b5. , 1993, Archives of biochemistry and biophysics.

[7]  M. Rivera,et al.  Gene synthesis, bacterial expression, and 1H NMR spectroscopic studies of the rat outer mitochondrial membrane cytochrome b5. , 1992, Biochemistry.

[8]  I. Kuntz,et al.  Sequence-specific 1H and 15N resonance assignments for both equilibrium forms of the soluble heme binding domain of rat ferrocytochrome b5. , 1992, Biochemistry.

[9]  S. Sligar,et al.  1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5. , 1990, Biochemistry.

[10]  N. C. Veitch,et al.  An analysis of pseudocontact shifts and their relationship to structural features of the redox states of cytochrome b 5 , 1990, FEBS letters.

[11]  F. S. Mathews,et al.  Molecular structure of flavocytochrome b2 at 2.4 A resolution. , 1990, Journal of molecular biology.

[12]  I. Kuntz,et al.  Structural studies of cytochrome b5: complete sequence-specific resonance assignments for the trypsin-solubilized microsomal ferrocytochrome b5 obtained from pig and calf. , 1990, Biochemistry.

[13]  N. C. Veitch,et al.  Investigation of the solution structures and mobility of oxidised and reduced cytochrome b 5 by 2D NMR spectroscopy , 1988, FEBS letters.

[14]  B. Hanquet,et al.  Effect of heme orientation on the reduction potential of cytochrome b5. , 1988, Journal of the American Chemical Society.

[15]  G. L. La Mar,et al.  1H-NMR assignments and the dynamics of interconversion of the isomeric forms of cytochrome b5 in solution. , 1986, Biochimica et biophysica acta.

[16]  F. Lederer,et al.  On the presence of a heme‐binding domain homologous to cytochrome b5 in Neurospora crassa assimilatory nitrate reductase , 1983, The EMBO journal.

[17]  F. Lederer,et al.  Two homologous cytochromes b5 in a single cell. , 1983, European journal of biochemistry.

[18]  P. Strittmatter,et al.  Proton magnetic resonance determination of the relative heme orientations in disordered native and reconstituted ferricytochrome b5. Assignment of heme resonances by deuterium labeling. , 1981, The Journal of biological chemistry.

[19]  K. Wüthrich,et al.  Structural study of the heme crevice in cytochrome b5 based on individual assignments of the 1H-NMR lines of the heme group and selected amino acid residues. , 1980, Biochimica et biophysica acta.

[20]  F. Lederer,et al.  The "cytochrome b5 fold": structure of a novel protein superfamily. , 1979, Journal of molecular biology.

[21]  F. Lederer,et al.  Amino acid sequence of the 'b5-like' heme-binding domain from chicken sulfite oxidase. , 1979, European journal of biochemistry.

[22]  K. Rajagopalan,et al.  Tryptic cleavage of rat liver sulfite oxidase. Isolation and characterization of molybdenum and heme domains. , 1977, The Journal of biological chemistry.

[23]  F. Lederer,et al.  The "b5-like" domain from chicken-liver sulfite oxidase: a new case of common ancestral origin with liver cytochrome b5 and bakers' yeast cytochrome b2 core. , 1977, European journal of biochemistry.

[24]  P. Strittmatter,et al.  The isolation and properties of microsomal cytochrome. , 1956, The Journal of biological chemistry.

[25]  F. S. Mathews,et al.  Refinement and structural analysis of bovine cytochrome b5 at 1.5 A resolution. , 1996, Acta crystallographica. Section D, Biological crystallography.

[26]  F. Lederer The cytochrome b5-fold: an adaptable module. , 1994, Biochimie.

[27]  S. Sligar,et al.  Relationship between heme binding site structure and heme orientations of two ferrocytochrome b5s. A study in prosthetic group recognition , 1990 .