C. S. Miles

发表

Molecular cooking: physical transformations in Chinese ‘century’ eggs

C. MacPhee, E. Eiser, N. Geerts, 2009 .

Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain.

S. Daff, A. Welland, Maki Kitamura, 2008, Biochemistry.

NMR solution structure of theu subunit of DNA polymerase III fromEscherichia coli

N. Dixon, H. Berthon, M. Keniry, 2022 .

Oxygen activation and electron transfer in flavocytochrome P450 BM3.

Jonathan P. Clark, T. Ost, M. Walkinshaw, 2003, Journal of the American Chemical Society.

NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli

N. Dixon, M. Keniry, C. S. Miles, 2008, Protein science : a publication of the Protein Society.

Roles of key active-site residues in flavocytochrome P450 BM3.

A. Munro, M. Noble, S. Chapman, 1999, The Biochemical journal.

Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance.

Susan E. Brown, C. Neylon, N. Dixon, 2000, Biochemistry.

Protein engineering of cytochromes P-450.

T. Ost, A. Munro, M. Noble, 2000, Biochimica et biophysica acta.

NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer.

J Weigelt, G Otting, N. Dixon, 1999, Structure.

P450 BM3: the very model of a modern flavocytochrome.

K. R. Marshall, T. Ost, P. Dutton, 2002, Trends in biochemical sciences.

Redox behaviour of the haem domain of flavocytochrome c 3 from Shewanella frigidimarina probed by NMR

S. Chapman, R. Louro, D. Turner, 2004, FEBS letters.

Tuning of functional heme reduction potentials in Shewanella fumarate reductases.

S. Chapman, R. Louro, D. Turner, 2009, Biochimica et biophysica acta.

Probing domain mobility in a flavocytochrome.

M. Walkinshaw, S. Chapman, G. Reid, 2004, Biochemistry.

Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina.

M. Walkinshaw, S. Chapman, G. Reid, 2003, Biochemistry.

Engineering water to act as an active site acid catalyst in a soluble fumarate reductase.

M. Walkinshaw, S. Chapman, D. Leys, 2002, Biochemistry.

Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina.

M. Walkinshaw, S. Chapman, D. Leys, 2002, Biochemistry.

Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study.

P. Taylor, M. Doherty, M. Walkinshaw, 2000, Biochemistry.

Tyr-143 facilitates interdomain electron transfer in flavocytochrome b2.

F. Lederer, S. Chapman, N. Rouvière-Fourmy, 1992, The Biochemical journal.

Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC.

J M Carazo, M. Radermacher, N. Dixon, 1998, Structure.

Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

Katy J. Drewette, Paul Taylor, Lisa McIver, 2004, Nature Structural &Molecular Biology.

Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.

T. Ost, A. Munro, S. Chapman, 2001, Biochemistry.

Catalytic properties of key active site mutants of flavocytochrome P-450 BM3

A. Munro, M. Noble, S. Chapman, 1999 .

A Proton Delivery Pathway in the Soluble Fumarate Reductase from Shewanella frigidimarina*

M. Walkinshaw, F. Armstrong, S. Chapman, 2006, Journal of Biological Chemistry.

Rational re‐design of the substrate binding site of flavocytochrome P450 BM3

T. Ost, A. Munro, S. Chapman, 2000, FEBS letters.

Flavocytochrome P450 BM3 substrate selectivity and electron transfer in a model cytochrome P450.

T. Ost, A. Munro, M. Noble, 2000, Sub-cellular biochemistry.

Backbone NMR Assignments and Secondary Structure of the N-terminal Domain of DnaB Helicase from E. Coli

N. Dixon, J. Weigelt, G. Otting, 1998, Journal of biomolecular NMR.

Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy.

N. Dixon, J. Weigelt, G. Otting, 1997, Biochemical and biophysical research communications.

Substitution of a haem-iron axial ligand in flavocytochrome b2.

S. Chapman, F. Manson, G. Reid, 1993, Biochimica et biophysica acta.

Catalysis in fumarate reductase.

S. Chapman, R. Moysey, G. Reid, 2000, Biochimica et biophysica acta.

The role of Thr268 and Phe393 in cytochrome P450 BM3.

Jonathan P. Clark, M. Walkinshaw, S. Daff, 2006, Journal of inorganic biochemistry.

Oxygen activation in neuronal NO synthase: resolving the consecutive mono-oxygenation steps.

S. Daff, C. Bruckmann, D. Papale, 2012, The Biochemical journal.

Changing the heme ligation in flavocytochrome b2: substitution of histidine-66 by cysteine

A. Munro, S. Chapman, L. Quaroni, 2000, JBIC Journal of Biological Inorganic Chemistry.

Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain.

S. Daff, A. Welland, Maki Kitamura, 2008, Biochemistry.

Probing intramolecular electron transfer within flavocytochrome b2 with a monoclonal antibody.

F. Lederer, K. Lê, C. S. Miles, 1998, Biochemistry.