S K Chapman

Summary

Affiliation: University of Edinburgh
Country: UK

Publications

  1. ncbi request reprint Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3
    T W Ost
    Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, UK
    Biochemistry 40:13430-8. 2001
  2. ncbi request reprint Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3
    T W Ost
    Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, UK
    Biochemistry 40:13421-9. 2001
  3. pmc Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration
    E H Gordon
    Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK
    Biochem J 349:153-8. 2000
  4. ncbi request reprint Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
    K L Turner
    Department of Chemistry, University of Edinburgh, Scotland
    Biochemistry 38:3302-9. 1999
  5. ncbi request reprint Control of electron transfer in neuronal NO synthase
    S Daff
    Department of Chemistry, University of Edinburgh, The King s Buildings, West Mains Road, Edinburgh EH9 3JJ, U K
    Biochem Soc Trans 29:147-52. 2001
  6. ncbi request reprint Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase
    C G Mowat
    Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, UK
    Biochemistry 40:12292-8. 2001
  7. ncbi request reprint Catalysis in fumarate reductase
    G A Reid
    Institute of Cell and Molecular Biology, University of Edinburgh, UK
    Biochim Biophys Acta 1459:310-5. 2000
  8. pmc Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase
    C Leadbeater
    Department of Chemistry, Joseph Black Building, University of Edinburgh, The King s Buildings, West Mains Road, Edinburgh EH9 3JJ, U K
    Biochem J 352:257-66. 2000
  9. pmc The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b2
    P White
    Department of Chemistry, University of Edinburgh, Scotland
    Biochem J 291:89-94. 1993
  10. ncbi request reprint Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina
    S L Pealing
    Department of Chemistry, University of Edinburgh, Edinburgh, Scotland, United Kingdom
    J Struct Biol 127:76-8. 1999

Collaborators

Detail Information

Publications11

  1. ncbi request reprint Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3
    T W Ost
    Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, UK
    Biochemistry 40:13430-8. 2001
    ....
  2. ncbi request reprint Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3
    T W Ost
    Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, UK
    Biochemistry 40:13421-9. 2001
    ....
  3. pmc Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration
    E H Gordon
    Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK
    Biochem J 349:153-8. 2000
    ....
  4. ncbi request reprint Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
    K L Turner
    Department of Chemistry, University of Edinburgh, Scotland
    Biochemistry 38:3302-9. 1999
    ..0 and 24 degrees C and are comparable to those determined by redox potentiometry...
  5. ncbi request reprint Control of electron transfer in neuronal NO synthase
    S Daff
    Department of Chemistry, University of Edinburgh, The King s Buildings, West Mains Road, Edinburgh EH9 3JJ, U K
    Biochem Soc Trans 29:147-52. 2001
    ..Despite its very different flavin redox potentials, the BM3 reductase domain was able to support low levels of CaM-dependent NO synthesis, whereas the NOS reductase domain did not effectively substitute for that of cytochrome P450 BM3...
  6. ncbi request reprint Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase
    C G Mowat
    Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, UK
    Biochemistry 40:12292-8. 2001
    ....
  7. ncbi request reprint Catalysis in fumarate reductase
    G A Reid
    Institute of Cell and Molecular Biology, University of Edinburgh, UK
    Biochim Biophys Acta 1459:310-5. 2000
    ..Substitutions of Arg402 lead to a dramatic loss of activity whereas neither of the two active site histidine residues is required for catalysis...
  8. pmc Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase
    C Leadbeater
    Department of Chemistry, Joseph Black Building, University of Edinburgh, The King s Buildings, West Mains Road, Edinburgh EH9 3JJ, U K
    Biochem J 352:257-66. 2000
    ....
  9. pmc The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b2
    P White
    Department of Chemistry, University of Edinburgh, Scotland
    Biochem J 291:89-94. 1993
    ..From these and other kinetic parameters, including kinetic isotope effects with [2-2H]lactate, we conclude that the hinge plays a crucial role in allowing efficient electron transfer between the two domains of flavocytochrome b2...
  10. ncbi request reprint Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina
    S L Pealing
    Department of Chemistry, University of Edinburgh, Edinburgh, Scotland, United Kingdom
    J Struct Biol 127:76-8. 1999
    ..359 A, b = 88.051 A, c = 77.473 A, and beta = 104.499 degrees. Anomalous data have also been collected from the NCIMB400 crystal allowing the heme iron positions to be identified...
  11. ncbi request reprint The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella
    C Schwalb
    Institute of Cell and Molecular Biology, University of Edinburgh, The King s Buildings, Mayfield Road, Edinburgh EH9 3JR, Scotland, UK
    Biochem Soc Trans 30:658-62. 2002
    ..Potentiometric studies suggest that there are two pairs of haems with potentials of -175 and -261 mV and that 'CymA is an efficient electron donor for the soluble fumarate reductase, flavocytochrome c(3)...