Spectroscopic and Mutational Analysis of the Blue-Light Photoreceptor AppA: A Novel Photocycle Involving Flavin Stacking with an Aromatic Amino Acid

The flavoprotein AppA is a blue-light photoreceptor that functions as an antirepressor of photosynthesis gene expression in the purple bacterium Rhodobacter sphaeroides. Heterologous expression studies show that FAD binds to a 156 amino acid N-terminal domain of AppA and that this domain is itself p...

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Veröffentlicht in:	Biochemistry (Easton) 2003-06, Vol.42 (22), p.6726-6734
Hauptverfasser:	Kraft, Brian J, Masuda, Shinji, Kikuchi, Jun, Dragnea, Vladimira, Tollin, Gordon, Zaleski, Jeffrey M, Bauer, Carl E
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins Circular Dichroism Flavin-Adenine Dinucleotide - chemistry Flavin-Adenine Dinucleotide - metabolism Flavoproteins - chemistry Flavoproteins - genetics Fluorescence Magnetic Resonance Spectroscopy Molecular Sequence Data Mutagenesis, Site-Directed Photochemistry Photolysis Protein Binding Protein Structure, Tertiary Sequence Alignment Sequence Homology, Amino Acid Spectrophotometry, Ultraviolet Tyrosine - chemistry Tyrosine - genetics
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Zusammenfassung:	The flavoprotein AppA is a blue-light photoreceptor that functions as an antirepressor of photosynthesis gene expression in the purple bacterium Rhodobacter sphaeroides. Heterologous expression studies show that FAD binds to a 156 amino acid N-terminal domain of AppA and that this domain is itself photoactive. A pulse of white light causes FAD absorption to be red shifted in a biphasic process with a fast phase occurring in
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi030055o