Flavin photochemistry in the analysis of electron transfer reactions: Role of charged and hydrophobic residues at the carboxyl terminus of ferredoxin-NADP+ reductase in the interaction with its substrates

Bioelectrochemistry

Volumn 56, Issue 1-2, 2002, Pages 19-21

  Faro, Merche ^a   Hurley, John K ^b   Medina, Milagros ^a   Tollin, Gordon ^b   Gómez Moreno, Carlos ^a  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b UNIVERSITY OF ARIZONA   (United States)

Author keywords

Electron transfer; Ferredoxin; NADP+

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; ELECTRONS; ENZYMES; PHOTOLYSIS; SUBSTRATES;

ELECTRON TRANSFER;

PHOTOCHEMICAL REACTIONS;

AMINO ACID; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVODOXIN; MUTANT PROTEIN; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

BIOSYNTHESIS; CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; CRYSTALLOGRAPHY; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; HYDROPHOBICITY; PHOTOCHEMISTRY; PHOTOLYSIS; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REDUCTION; SITE DIRECTED MUTAGENESIS; WILD TYPE;

CIRCULAR DICHROISM; ELECTRONS; FERREDOXIN-NADP REDUCTASE; FLAVINS; KINETICS; PHOTOCHEMISTRY; SPECTROPHOTOMETRY, ULTRAVIOLET; SUBSTRATE SPECIFICITY;

EID: 0037094166     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1567-5394(02)00039-7     Document Type: Conference Paper

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12. A redox-dependent interaction between two electron-transfer partners intervening in photosynthesis