Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus
UNSPECIFIED. (2006) Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus. STRUCTURE, 14 (1). pp. 107-117. ISSN 0969-2126Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.str.2005.09.011
Bacterial cytochrome c peroxidases contain an electron transferring (E) heme domain and a peroxidatic (P) heme domain. All but one of these enzymes are isolated in an inactive oxidized state and require reduction of the E heme by a small redox donor protein in order to activate the P heme. Here we present the structures of the inactive oxidized and active mixed valence enzyme from Paracoccus pantotrophus. Chain flexibility in the former, as expressed by the crystallographic temperature factors, is strikingly distributed in certain loop regions, and these coincide with the regions of conformational change that occur in forming the active mixed valence enzyme. On the basis of these changes, we postulate a series of events that occur to link the trigger of the electron entering the E heme from either pseudoazurin or cytochrome C-550 and the dissociation of a coordinating histidine at the P heme, which allows substrate access.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||STRUCTURE|
|Number of Pages:||11|
|Page Range:||pp. 107-117|
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