Oxo-and hydroxo-bridged diiron active centers are common structural motifs found in a
variety of proteins in biology. The highly versatile oxo/hydroxo-bridged dimetallic centers …

The family of multiheme proteins constitutes one of the fascinating molecular machineries
designed by Nature to execute a large variety of functions. A high level of conservation …

A cobalt porphyrin dimer is constructed in which two Co (II) porphyrins are connected
covalently through a redox-active diethylpyrrole moiety via a flexible but “nonconjugated” …

We report an unexpected rearrangement, controlled by the nature of the bridge, leading to
the formation of novel, remarkably stable triply fused dinickel (II)/dicopper (II) chlorin …

Conjugated arrays composed of corrole macrocycles are increasingly more common, but
their chemistry still lags behind that of their porphyrin counterparts. Here, we report on the …

Here, we delineate a maiden example of a diiron (III) dication diradical porphyrin dimer as a
competent catalyst for the oxa-Diels–Alder type reaction of aldehydes with 1, 3-dienes …

Dinickel (II) and dicopper (II) porphyrin dimers have been constructed in which two
metalloporphyrin units are widely separated by a long unconjugated dipyrrole bridge. Two …

Diheme cytochromes, the simplest members in the multiheme family, play substantial
biochemical roles in enzymatic catalysis as well as in electron transfer. A series of diiron (III) …

The chemistry of oxo/hydroxo-bridged diheme centers, connected covalently through
bridges, has attracted much attention recently. Close approach of the two heme centers in …

We explore here the structure–function relationship of the diheme cytochrome c using
synthetic diheme analogs which serve as a convenient tool to investigate various aspects of …