Dioxygen-dependent Heme Enzymes

Dioxygen Binding and Activation Mediated by Transition Metal Porphyrinoid Complexes; Design and Engineering
of Heme Enzymes With O2-dependent Catalytic Activity; Myoglobin Derivatives Reconstituted with Modified Metal Porphyrinoids as Structural and Functional Models of the Cytochrome P450 Enzymes; Investigating Heme Enzymes with Expanded Genetic Codes; What Drives the Ratedetermining Step for Oxygen Atom Transfer by Heme Compound I?; Cytochrome P450 Decarboxylases; Oxygen Activation and Long-range Electron Transfer in MauG; Biological Heme Degradation; Structure, Function and Regulation of Human Heme-based Dioxygenases; Modeling O2-dependent Heme Enzymes: A Quick Guide for Non-experts; Structures of Human Cytochrome P450 Enzymes: Variations on a Theme; Controlling the Regio- and Stereoselectivity of Cytochrome P450 Monooxygenases by Protein Engineering; Conformational Changes in Cytochrome P450cam and the Effector Role of Putidaredoxin; Oxygen Reduction and Proton Translocation by Respiratory Cytochrome c Oxidase; Structure and Function of Membrane-bound Bacterial Nitric Oxide Reductases; Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins