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Titolo:
The active site of the plant alternative oxidase: structural and mechanistic considerations
Autore:
Affourtit, C; Albury, MS; Whitehouse, DG; Moore, AL;
Indirizzi:
Univ Sussex, Dept Biochem, Sch Biol Sci, Brighton BN1 9QG, E Sussex, England Univ Sussex Brighton E Sussex England BN1 9QG BN1 9QG, E Sussex, England
Titolo Testata:
PEST MANAGEMENT SCIENCE
fascicolo: 1, volume: 56, anno: 2000,
pagine: 31 - 38
SICI:
1526-498X(200001)56:1<31:TASOTP>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARUM-MACULATUM MITOCHONDRIA; AMINO-ACID-COMPOSITION; RIBONUCLEOTIDE REDUCTASE; METHANE MONOOXYGENASE; PARTIAL-PURIFICATION; ELECTRON-TRANSFER; ESCHERICHIA-COLI; IRON; PROTEINS; RESPIRATION;
Keywords:
plant alternative oxidase; active site; di-iron centre; molecular modelling; site-directed mutagenesis; reaction mechanism;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Moore, AL Univ Sussex, Dept Biochem, Sch Biol Sci, Brighton BN1 9QG, E Sussex, England Univ Sussex Brighton E Sussex England BN1 9QG E Sussex, England
Citazione:
C. Affourtit et al., "The active site of the plant alternative oxidase: structural and mechanistic considerations", PEST MAN SC, 56(1), 2000, pp. 31-38

Abstract

In the present review we seek to provide an up-to-date view on the molecular nature of the active site of the plant alternative oxidase which has been postulated to comprise of a binuclear iron centre. A three-dimensional model of the catalytic centre of the oxidase is presented which is based on the active site structure of the free radical component of ribonucleotide reductase and methane monooxygenase. The model indicates that a highly conserved carboxylate (Glu-270) occupies a central position within the proposed di-iron centre as it co-ordinates both iron atoms. The expression of an alternative oxidase protein in Schizosaccharomyces pombe in which Glu-270 was mutated to asparagine yields an inactive protein. The implications of this in relation to the structural model of the active site of the oxidase suggests that Glu-270 is essential for catalytic alternative oxidase activity. A kinetic mechanism is suggested which accounts for the full reduction of dioxygen to water catalysed by a single di-iron centre. (C) 2000 Society of Chemical Industry.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 00:54:59