self-assembling peptide detergents stabilize isolated photosystem ion a dry surface for an extended time自组装肽洗涤剂稳定隔离光离子干表面在较长时间.pdfVIP

Open access, freely available online PLoS BIOLOGY Self-Assembling Peptide Detergents Stabilize Isolated Photosystem I on a Dry Surface for an Extended Time 1,2 1 3 2 3 1,4* Patrick Kiley , Xiaojun Zhao , Michael Vaughn , Marc A. Baldo , Barry D. Bruce , Shuguang Zhang 1 Center for Biomedical Engineering NE47–379, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America, 2 Department of Electrical Engineering and Computer Science, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America, 3 Center for Environmental Biotechnology and Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee, United States of America, 4 Center for Bits and Atoms, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America We used a class of designed peptide detergents to stabilize photosystem I (PS-I) upon extended drying under N2 on a gold-coated-Ni-NTA glass surface. PS-I is a chlorophyll-containing membrane protein complex that is the primary reducer of ferredoxin and the electron acceptor of plastocyanin. We isolated the complex from the thylakoids of spinach chloroplasts using a chemical detergent. The chlorophyll molecules associated with the PS-I complex provide an intrinsic steady-state emission spectrum between 650 and 800 nm at 196.15 8C that reflects the organization of the pigment-protein interactions. In the absence of detergents, a large blue shift of the fluorescence maxima from approximately 735 nm to approximately 685 nm indicates a disruption in light-harvesting subunit organization, thus revealin