Structural role of (bacterio)chlorophyll ligated in the energetically unfavorable β-position

Journal of Biological Chemistry

Volumn 281, Issue 15, 2006, Pages 10626-10634

  Garcia Martin, Adela ^a   Lee, Gyan Kwa ^a   Strohmann, Brigitte ^a   Robert, Bruno ^b   Holzwarth, Alfred R ^c   Braun, Paula ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b DIF   (France)

^c MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGICAL MEMBRANES; HYDROGEN BONDS; PROTEINS; THERMODYNAMIC STABILITY;

BACTERIOCHLOROPHYLL PROTEINS; MULTICOMPONENT CHLOROPHYLL PROTEINS; PHOTOSYSTEM;

CHLOROPHYLL;

APOPROTEIN; BACTERIOCHLOROPHYLL; BACTERIOCHLOROPHYLL B850; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; CHLOROPHYLL; PROTEIN;

ARTICLE; BACTERIAL MEMBRANE; BINDING SITE; HYDROGEN BOND; LIGATION; LIGHT HARVESTING SYSTEM; MEMBRANE STABILIZATION; MUTAGENESIS; PHOTOSYSTEM I; PHOTOSYSTEM II; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; RHODOBACTER SPHAEROIDES; STRUCTURE ANALYSIS; THERMOSTABILITY; AMINO ACID SEQUENCE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; CYTOPLASM; ESCHERICHIA COLI; GENE TRANSFER; HEAT; METABOLISM; MOLECULAR GENETICS; MUTATION; PLASMID; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; RHODOBACTER; SEQUENCE HOMOLOGY; STATISTICAL MODEL;

RHODOBACTER SPHAEROIDES;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIOCHLOROPHYLLS; CHLOROPHYLL; CIRCULAR DICHROISM; CYTOPLASM; ESCHERICHIA COLI; GENE TRANSFER TECHNIQUES; HEAT; HYDROGEN BONDING; MODELS, CHEMICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; MOLECULAR SEQUENCE DATA; MUTATION; PHOTOSYSTEM I PROTEIN COMPLEX; PHOTOSYSTEM II PROTEIN COMPLEX; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEINS; RHODOBACTER; SEQUENCE HOMOLOGY, AMINO ACID; SPECTRUM ANALYSIS, RAMAN;

EID: 33744505212     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M510731200     Document Type: Article

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