Key Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate Bias

Navigating the protein fitness landscape with Gaussian processes

(2013) P. A. Romero et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The role of active-site Phe87 in modulating the organic co-solvent tolerance of cytochrome P450 BM3 monooxygenase

(2012) Jochen Kuper et al.   Acta Crystallographica Section F-Structural Biology and Crystallization Communications

A Single Active Site Mutation Inverts Stereoselectivity of 16-Hydroxylation of Testosterone Catalyzed by Engineered Cytochrome P450 BM3

(2012) Harini Venkataraman et al.   CHEMBIOCHEM

Identification of Mutant Asp251Gly/Gln307His of Cytochrome P450 BM3 for the Generation of Metabolites of Diclofenac, Ibuprofen and Tolbutamide

(2012) Georgia E. Tsotsou et al.   CHEMISTRY-A EUROPEAN JOURNAL

Unusual Spectroscopic and Ligand Binding Properties of the Cytochrome P450-Flavodoxin Fusion Enzyme XplA

(2012) Soi H. Bui et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Olefin Cyclopropanation via Carbene Transfer Catalyzed by Engineered Cytochrome P450 Enzymes

(2012) P. S. Coelho et al.   SCIENCE

P450BM3(CYP102A1): connecting the dots

(2011) Christopher J. C. Whitehouse et al.   CHEMICAL SOCIETY REVIEWS

LigPlot+: Multiple Ligand–Protein Interaction Diagrams for Drug Discovery

(2011) Roman A. Laskowski et al.   Journal of Chemical Information and Modeling

Regio- and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution

(2011) Sabrina Kille et al.   Nature Chemistry

Laboratory Evolution of Stereoselective Enzymes: A Prolific Source of Catalysts for Asymmetric Reactions

(2010) Manfred T. Reetz   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: Implications for the mechanism of electron transfer in the P450 BM3 dimer

(2010) Hazel M. Girvan et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Structural Basis for the Properties of Two Single-Site Proline Mutants of CYP102A1 (P450BM3)

(2010) Christopher J. C. Whitehouse  et al.   CHEMBIOCHEM

Structural and Biochemical Characterization ofMycobacterium tuberculosisCYP142

(2010) Max D. Driscoll et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A Highly Active Single-Mutation Variant of P450BM3(CYP102A1)

(2009) Christopher J. C. Whitehouse et al.   CHEMBIOCHEM

A Panel of Cytochrome P450 BM3 Variants to Produce Drug Metabolites and Diversify Lead Compounds

(2009) Andrew M. Sawayama et al.   CHEMISTRY-A EUROPEAN JOURNAL

Altering the regioselectivity of the subterminal fatty acid hydroxylase P450 BM-3 towards γ- and δ-positions

(2008) Matthias Dietrich et al.   JOURNAL OF BIOTECHNOLOGY

Evolutionary History of a Specialized P450 Propane Monooxygenase

(2008) Rudi Fasan et al.   JOURNAL OF MOLECULAR BIOLOGY

Cytochrome P450 and Chemical Toxicology

(2007) F. Peter Guengerich   CHEMICAL RESEARCH IN TOXICOLOGY

Application of drug metabolising mutants of cytochrome P450 BM3 (CYP102A1) as biocatalysts for the generation of reactive metabolites

(2007) Micaela C. Damsten et al.   CHEMICO-BIOLOGICAL INTERACTIONS