Article
Y25S variant of Paracoccus pantotrophus cytochrome cd1 provides insight into anion binding by d1 heme and a rare example of a critical difference between solution and crystal structures.
The Journal of biological chemistry - 15 Jul 2005
Zajicek Richard S, Cheesman Myles R, Gordon Euan H J, Ferguson Stuart J
Abstract excerpt
Tyr25 is a ligand to the active site d1 heme in as isolated, oxidized cytochrome cd1 nitrite reductase from Paracoccus pantotrophus. This form of the enzyme requires reductive activation, a process that involves not only displacement of Tyr25 from the d1 heme but also switching of the ligands at...
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