Metalloporphyrins are widely used throughout the biosphere, and of these heme (iron
protoporphyrin IX, Figure 1) is one of the most abundant and widely used. Heme shuttles …

Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

This paper describes the current update on macromolecular model validation services that
are provided at the MolProbity website, emphasizing changes and additions since the …

Surprisingly, the frozen structures from ultra-high-resolution protein crystallography reveal a
prevalent, but subtle, mode of local backbone motion coupled to much larger, two-state …

This review describes the historical difficulties in devising a kinetically satisfactory
mechanism for the classical catalase after its identification as a unique catalytic entity in …

About thirty years ago the crystal structures of the heme catalases from Penicillium vitale
(PVC) and, a few months later, from bovine liver (BLC) were published. Both enzymes were …

Peroxidases, oxygenases and catalases have similar high-valent metal-ion intermediates in
their respective reaction cycles. In this review, haem-based examples will be discussed. The …

The MolProbity web service provides macromolecular model validation to help correct local
errors, for the structural biology community worldwide. Here we highlight new validation …

To gain insight into the protonation state of enzymatic ferryl species we have examined the
applicability of Badger's rule to heme and non-heme iron− oxygen bonds. Using density …

The review focuses on four issues that are critical for the understanding of monofunctional
catalases. How hydrogen peroxide (H2O2) reaches the active site and outcompetes water …