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Titolo:
Life as aerobes: are there simple rules for activation of dioxygen by enzymes?
Autore:
Klinman, JP;
Indirizzi:
Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 pt Chem, Berkeley, CA 94720 USA Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 ll Biol, Berkeley, CA 94720 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
fascicolo: 1, volume: 6, anno: 2001,
pagine: 1 - 13
SICI:
0949-8257(200101)6:1<1:LAAATS>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
COPPER AMINE OXIDASE; TYROSINE-HYDROXYLASE REACTION; GLUCOSE-OXIDASE; SOYBEAN LIPOXYGENASE-1; ASPERGILLUS-NIGER; CRYSTAL-STRUCTURE; CATALYTIC MECHANISM; OXYGEN ACTIVATION; ELECTRON-TRANSFER; ESCHERICHIA-COLI;
Keywords:
dioxygen; enzymes; proton transfer; electron transfer;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Klinman, JP Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 keley, CA 94720 USA
Citazione:
J.P. Klinman, "Life as aerobes: are there simple rules for activation of dioxygen by enzymes?", J BIOL I CH, 6(1), 2001, pp. 1-13

Abstract

Numerous biological systems involve reaction with dioxygen in the absence of readily accessible spectroscopic signals. We have begun to develop a setof "generic" strategies that will allow us to probe the mechanisms of dioxygen activation. In particular, we wish to understand the nature of the dioxygen binding step, the degree to which electron transfer to dioxygen is rate limiting, whether reactive species accumulate during turnover and, finally, whether proton and electron transfer to dioxygen occur as coupled processes. Our strategy will be introduced for an enzyme system that uses only an organic cofactor in dioxygen activation (glucose oxidase). Two key features emerge from studies of glucose oxidase: (1) that formation of the superoxide anion is a major rate-limiting step and (2) that electrostatic stabilization of the superoxide anion plays a key role in catalysis. Similar themes emerge when our protocols are applied to enzymes containing both an active site metal center and an organic cofactor. Finally, enzymes that rely solely on metal centers for substrate functionalization will be discussed. In no instance, thus far, has evidence been found for a direct coupling of proton to electron transfer in the reductive activation of dioxygen.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 06:44:55