Crystallization and initial spectroscopic characterization of the heme-containing dehaloperoxidase from the marine polychaete Amphitrite ornata.
The heme-containing dehaloperoxidase from Amphitrite ornata was crystallized from an unbuffered solution containing 30% PEG 8000 and 200 mM ammonium sulfate by the hanging-drop vapor-diffusion method. Dark-red bipyramidal crystals are orthorhombic in space group P2(1)2(1)2(1) with unit-cell dimensions a = 68.5, b = 68.4 and c = 61.1 A. The asymmetric unit contains two subunits related by a non-crystallographic twofold axis. The crystals scatter beyond 2 A resolution. The native data have been collected and one single-site mercury derivative has been found. SIRAS phasing was used to determine the positions of the heme Fe atoms and structure determination is in progress. A preliminary spectroscopic investigation indicates that the heme is protoporphyrin IX and its coordination sphere resembles that of a typical heme peroxidase, i.e. histidine ligated. Detailed spectroscopic and electrochemical studies are now under way.
Department of Chemistry and Biochemistry, University of South Carolina, Columbia 29208, USA.
E
E
Zhang
Y P
YP
Chen
M P
MP
Roach
D E
DE
Lincoln
C R
CR
Lovell
S A
SA
Woodin
J H
JH
Dawson
L
L
Lebioda