Heme Peroxidases

[1]  M. W. van der Kamp,et al.  Visualizing the protons in a metalloenzyme electron proton transfer pathway , 2020, Proceedings of the National Academy of Sciences.

[2]  K. Fisher,et al.  Rewiring the “Push-Pull” Catalytic Machinery of a Heme Enzyme Using an Expanded Genetic Code , 2020, ACS catalysis.

[3]  Moritz Pott,et al.  A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold. , 2018, Journal of the American Chemical Society.

[4]  J. Groves,et al.  Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins , 2017, Chemical reviews.

[5]  P. Moody,et al.  Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme , 2016, Nature Communications.

[6]  Donald Hilvert,et al.  A Chemically Programmed Proximal Ligand Enhances the Catalytic Properties of a Heme Enzyme. , 2016, Journal of the American Chemical Society.

[7]  T. Poulos,et al.  Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer , 2016, Proceedings of the National Academy of Sciences.

[8]  P. Moody,et al.  Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase , 2014, Science.

[9]  T. Poulos Heme enzyme structure and function. , 2014, Chemical reviews.

[10]  T. Poulos,et al.  High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase. , 2003, Biochemistry.

[11]  M. Mewies,et al.  Crystal structure of the ascorbate peroxidase–ascorbate complex , 2003, Nature Structural Biology.

[12]  J. Hajdu,et al.  The catalytic pathway of horseradish peroxidase at high resolution , 2002, Nature.

[13]  D. J. Schuller,et al.  Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography. , 1998, Biochemistry.

[14]  D B Goodin,et al.  Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. , 1989, Science.