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Titolo:
SITE-DIRECTED MUTAGENESIS IMPROVES THE BIOCATALYTIC ACTIVITY OF ISO-1-CYTOCHROME-C IN POLYCYCLIC-HYDROCARBON OXIDATION
Autore:
TORRES E; SANDOVAL JV; ROSELL FI; MAUK AG; VAZQUEZDUHALT R;
Indirizzi:
UNAM,INST BIOTECHNOL,DEPT BIOENGN,ENVIRONM BIOTECHNOL LAB,APARTADO POSTAL 510-3 CUERNAVACA 62271 MORELOS MEXICO UNAM,INST BIOTECHNOL,DEPT BIOENGN,ENVIRONM BIOTECHNOL LAB CUERNAVACA 62271 MORELOS MEXICO UNIV BRITISH COLUMBIA,DEPT BIOCHEM & MOLEC BIOL VANCOUVER BC V5Z 1M9 CANADA
Titolo Testata:
Enzyme and microbial technology
fascicolo: 11, volume: 17, anno: 1995,
pagine: 1014 - 1020
SICI:
0141-0229(1995)17:11<1014:SMITBA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOCHROME-C; YEAST ISO-1-CYTOCHROME-C; AROMATIC-HYDROCARBONS; CONFORMATIONAL-CHANGES; LIGNINOLYTIC FUNGI; ELECTRON-TRANSFER; ORGANIC-SOLVENTS; BOND-CLEAVAGE; DEGRADATION; PHENYLALANINE-82;
Keywords:
CYTOCHROME; POLYCYCLIC AROMATIC HYDROCARBON; ORGANIC SOLVENT; ENZYMATIC OXIDATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
E. Torres et al., "SITE-DIRECTED MUTAGENESIS IMPROVES THE BIOCATALYTIC ACTIVITY OF ISO-1-CYTOCHROME-C IN POLYCYCLIC-HYDROCARBON OXIDATION", Enzyme and microbial technology, 17(11), 1995, pp. 1014-1020

Abstract

iso-1-Cytochrome c from Saccharomyces cerevisiae is able to oxidize polycyclic aromatic hydrocarbons (PAH) in the presence of hydrogen peroxide. Anthracene and pyrene are oxidized by yeast cytochrome c to formanthraquinone and 1,8-pyrenedione, respectively. Iso-1-cytochrome c from S. cerevisiae was modified by site-directed mutagenesis of Phe82 and Cys102. The Phe82 substitution significantly altered the kinetic behavior of the protein; Cys102 modification affected neither the kinetic nor the stability constant. The Gly82;Thr102 valiant was 10 times more active and showed a catalytic efficiency 10-fold greater than the wild-type iso-1-cytochrome c. However, Phe82 variants showed lower stability against inactivation by hydrogen peroxide than the wild-type protein. These site-directed mutations did not significantly alter the stability and activity of the hemoprotein in increasing concentrations of tetrahydrofuran.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 10:32:02