Structure of the Heme d ofPenicillium vitaleandEscherichia coliCatalases

Garib N. Murshudov, Albina I. Grebenko, Vladimir Barynin, Zbigniew Dauter, Keith S. Wilson, Boris K. Vainshtein, William Melik-Adamyan, Jerónimo Bravo, José M. Ferrán, Juan C. Ferrer, Jack Switala, Peter C. Loewen (+1 others)
1996 Journal of Biological Chemistry  
A heme d prosthetic group with the configuration of a cis-hydroxychlorin ␥-spirolactone has been found in the crystal structures of Penicillium vitale catalase and Escherichia coli catalase hydroperoxidase II (HPII). The absolute stereochemistry of the two heme d chiral carbon atoms has been shown to be identical. For both catalases the heme d is rotated 180 degrees about the axis defined by the ␣-␥-meso carbon atoms, with respect to the orientation found for heme b in beef liver catalase. Only
more » ... six residues in the heme pocket, preserved in P. vitale and HPII, differ from those found in the bovine catalase. In the crystal structure of the inactive N201H variant of HPII catalase the prosthetic group remains as heme b, although its orientation is the same as in the wild type enzyme. These structural results confirm the observation that heme d is formed from protoheme in the interior of the catalase molecule through a self-catalyzed reaction.
doi:10.1074/jbc.271.15.8863 pmid:8621527 fatcat:vwqbrrzfvrchtigp3wxoh55h54