This page shows some interactive JSmol views of catalase and peroxidase.
[Catalase 1] shows the tetrameric structure of (human) ctalase.
Each subunit conains one heme group,
the protein also contains some (bound) NADPH molecules, probably for receipt/delivery of reducing equivalents (H+).
[Catalase 2] shows the reduced (FeIII) resting state - which is 5-coordinate.
Note the Tyr residue coordinated to the iron, the water molecule and conserved distal His above the active site,
and the H-bonds linking them.
[Catalase 3] shows "Compound I of catalase", containing a ferryl-oxo (FeIV=O) group.
This is characterised by a very short Fe-O distance (here 1.76 Å) and by high reactivity.
Peroxidases are generally momomeric, again with one heme group per unit. This set of figures shows a ferrous form (photoreduced by X-rays) and the corresponding Compound I and Compound II - all for Cytochrome c peroxidase. The Fe-O distances are given below, Compound I is clearly shorter than Compound II, and it is suggested that Compound II contains FeIV-OH (ferryl hydroxide), with a single Fe-O bond.