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Titolo:
SITE-SPECIFIC MUTAGENESIS DEMONSTRATES THAT THE STRUCTURAL REQUIREMENTS FOR EFFICIENT ELECTRON-TRANSFER IN ANABAENA FERREDOXIN AND FLAVODOXIN ARE HIGHLY DEPENDENT ON THE REACTION PARTNER - KINETIC-STUDIES WITHPHOTOSYSTEM-I, FERREDOXIN-NADP(-C() REDUCTASE, AND CYTOCHROME)
Autore:
NAVARRO JA; HERVAS M; GENZOR CG; CHEDDAR G; FILLAT MF; DELAROSA MA; GOMEZMORENO C; CHENG H; XIA B; CHAE YK; YAN H; WONG B; STRAUS NA; MARKLEY JL; HURLEY JK; TOLLIN G;
Indirizzi:
UNIV ARIZONA,DEPT BIOCHEM TUCSON AZ 85721 UNIV ARIZONA,DEPT BIOCHEM TUCSON AZ 85721 UNIV SEVILLA,INST BIOQUIM VEGETAL & FOTOSINTESIS,APDO 1113 E-41080 SEVILLE SPAIN CSIC E-41080 SEVILLE SPAIN UNIV ZARAGOZA,FAC CIENCIAS,DEPT BIOQUIM & BIOL MOLEC & CELULAR E-50009 ZARAGOZA SPAIN UNIV WISCONSIN,DEPT BIOCHEM MADISON WI 53706 UNIV TORONTO,DEPT BOT TORONTO ON M5S 1A1 CANADA
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 1, volume: 321, anno: 1995,
pagine: 229 - 238
SICI:
0003-9861(1995)321:1<229:SMDTTS>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
FLASH ABSORPTION-SPECTROSCOPY; IONIC-STRENGTH DEPENDENCE; SP STRAIN PCC-7120; NADP+ REDUCTASE; ESCHERICHIA-COLI; RATE CONSTANTS; AMINO-ACID; SPINACH; GENE; SEQUENCE;
Keywords:
PROTEIN ELECTRON TRANSFER; REDOX REACTIONS; STOPPED-FLOW SPECTROPHOTOMETRY; LASER FLASH PHOTOLYSIS; PHOTOBIOCHEMISTRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
J.A. Navarro et al., "SITE-SPECIFIC MUTAGENESIS DEMONSTRATES THAT THE STRUCTURAL REQUIREMENTS FOR EFFICIENT ELECTRON-TRANSFER IN ANABAENA FERREDOXIN AND FLAVODOXIN ARE HIGHLY DEPENDENT ON THE REACTION PARTNER - KINETIC-STUDIES WITHPHOTOSYSTEM-I, FERREDOXIN-NADP(-C() REDUCTASE, AND CYTOCHROME)", Archives of biochemistry and biophysics, 321(1), 1995, pp. 229-238

Abstract

Electron transfer reactions involving site-specific mutants of Anabaena ferredoxin (Fd) and flavodoxin (Fld) modified at surface residues close to the prosthetic groups, with photoexcited P700 in spinach photosystem I (PSI) particles, ferredoxin:NADP(+) reductase (FNR), and horse cytochrome c (cytc), have been investigated by laser flash photolysis and stopped-how spectrophotometry, Nonconservative mutations in Fd at F65 and E94, which have been shown to result in very large inhibitions of electron transfer to FNR, were found to yield wild-type behaviorin reactions with PSI and cytc, In general, the effects of d mutagenesis on the PSI reactions were considerably smaller than those observedfor the FNR reaction, In the case of Fld, mutagenesis was found to have only small effects on both the FNR and PSI reactions, although the specific sites whose mutation caused changes in electron transfer properties differed for the two systems, In contrast, several of the Fld mutants showed appreciably larger effects on the nonphysiological reaction with cytc, We conclude from these studies that the structural requirements for efficient electron transfer involving the Fd and Fld molecules differ, depending upon the reactant with which these redox proteins interact, This is consistent with the multiple roles that these proteins have in vivo in biological electron transfer and implies that different conserved residues in these proteins have evolved to satisfy varying requirements of particular reaction partners. (C) 1995 Academic Press, Inc.

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Documento generato il 04/07/20 alle ore 13:50:22