The measured and calculated affinity of methyl-and methoxy-substituted benzoquinones for the Q A site of bacterial reaction centers

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 12, 2010, Pages 2638-2654

  Zheng, Zhong ^a   Dutton, P Leslie ^b   Gunner, M R ^a  

^a CITY COLLEGE OF NEW YORK   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Bacterial reaction center; Binding affinity; Docking; Photosynthesis; Q A; Quinone

Indexed keywords

BENZOQUINONE DERIVATIVE;

ARTICLE; BINDING AFFINITY; BINDING SITE; HYDROGEN BOND; MONTE CARLO METHOD; PHOTOSYNTHESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; PROTON TRANSPORT; RHODOBACTER SPHAEROIDES; STATIC ELECTRICITY;

ANIMALS; BENZOQUINONES; BINDING SITES; DATABASES, FACTUAL; HYDROGEN BONDING; LIGANDS; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; PROTEIN CONFORMATION; RHODOBACTER SPHAEROIDES; SOFTWARE; STATIC ELECTRICITY;

BACTERIA (MICROORGANISMS); RHODOBACTER SPHAEROIDES;

EID: 77955804573     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22779     Document Type: Article

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