Six‐coordinated heme groups are involved in a large variety of electron transfer reactions
because of their ability to exist in both the ferrous (Fe2+) and ferric (Fe3+) state without any …

The last decades have witnessed a steady increase of the social and political awareness for
the need of monitoring and controlling environmental and industrial processes. In the case …

The DsrMKJOP transmembrane complex has a most important function in dissimilatory
sulfur metabolism, not only in many sulfur-oxidizing organisms but also in sulfate-reducing …

The interaction of ferriheme proteins with nitrite has recently attracted interest as a source for
NO or other nitrogen oxides in mammalian physiology. However, met-hemoglobin (metHb) …

Recently, the conversion of nitrite into NO by certain heme proteins, in particular
hemoglobin, gained much interest as a physiologically important source of NO in human …

Cytochrome c (cyt c), required for electron transport in mitochondria, possesses a covalently
attached heme cofactor. Attachment is catalyzed by holocytochrome c synthase (HCCS) …

Cytochromes of the c type with histidine− methionine (His-Met) heme axial ligation play
important roles in electron-transfer reactions and in enzymes. In this work, two series of …

The cytochrome cd 1 nitrite reductases are enzymes that catalyse the reduction of nitrite to
nitric oxide (NO) in the bacterial energy conversion denitrification process. These enzymes …

Nitrite reductase (cd1NIR) from Pseudomonas aeruginosa, which catalyses the reduction of
nitrite to nitric oxide (NO), contains a c-heme as the electron acceptor and a d1-heme where …

Proton delivery to the prosthetic group is a crucial step to sustain the activity of nitrite
reductase. An iron N-confused porphyrin (NCP) complex, which is capable of relaying …