UNSPECIFIED. (2006) Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus. STRUCTURE, 14 (1). pp. 107-117. ISSN 0969-2126

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Abstract

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
Publisher:	CELL PRESS
ISSN:	0969-2126
Date:	January 2006
Volume:	14
Number:	1
Number of Pages:	11
Page Range:	pp. 107-117
Identification Number:	10.1016/j.str.2005.09.011
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/33978

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