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