Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Isolation and spectroscopic characterization of a recombinant bell pepper hydroperoxide lyase
Autore:
Psylinakis, E; Davoras, EM; Ioannidis, N; Trikeriotis, M; Petrouleas, V; Ghanotakis, DF;
Indirizzi:
Univ Crete, Dept Chem, Iraklion 71409, Crete, Greece Univ Crete Iraklion Crete Greece 71409 hem, Iraklion 71409, Crete, Greece NCSR Demokritos, Inst Mat Sci, Aghia Paraskevi 15310, Greece NCSR Demokritos Aghia Paraskevi Greece 15310 hia Paraskevi 15310, Greece
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
fascicolo: 2, volume: 1533, anno: 2001,
pagine: 119 - 127
SICI:
1388-1981(20010928)1533:2<119:IASCOA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-PARAMAGNETIC RESONANCE; FERRIC CYTOCHROME P-450-CAM; SITE-DIRECTED MUTAGENESIS; LIPOXYGENASE PATHWAY; NITRIC-OXIDE; THIOLATE LIGATION; PARTIAL-PURIFICATION; PROXIMAL HISTIDINE; LIGAND COMPLEXES; CLEAVING ENZYME;
Keywords:
hydroperoxide lyase; thiolate ligation; cytochrome P450; electron paramagnetic resonance spectroscopy;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Ghanotakis, DF Univ Crete, Dept Chem, POB 1470, Iraklion 71409, Crete, Greece Univ Crete POB 1470 Iraklion Crete Greece 71409 ete, Greece
Citazione:
E. Psylinakis et al., "Isolation and spectroscopic characterization of a recombinant bell pepper hydroperoxide lyase", BBA-MOL C B, 1533(2), 2001, pp. 119-127

Abstract

Fatty acid hydroperoxide (HPO) lyase is a component of the oxylipin pathway and holds a central role in elicited plant defense. HPO lyase from bell pepper has been identified as a heme protein which shares 40% homology with allene oxide synthase, a cytochrome P450 (CYP74A). HPO lyase of immature bell pepper fruits was expressed in Escherichia coli and the enzyme was purified and characterized by spectroscopic techniques. The electronic structureand ligand coordination properties of the heme were investigated by using a series of exogenous ligands. The various complexes were characterized by using UV-visible absorption and electron paramagnetic resonance spectroscopy. The spectroscopic data demonstrated that the isolated recombinant HPO lyase has a pentacoordinate, high-spin heme with thiolate ligation. Addition of the neutral ligand imidazole or the anionic ligand cyanide results in the formation of hexacoordinate adducts that retain thiolate ligation. The striking similarities between both the ferric and ferrous HPO lyase-NO complexes with the analogous P450 complexes, suggest that the active sites of HPOlyase and P450 share common structural features. (C) 2001 Elsevier ScienceBN. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 09:48:04