Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: Comparison with the solution structure of the wild-type protein

Biochemistry

Volumn 35, Issue 18, 1996, Pages 5928-5936

  Bentrop, Detlef ^a   Bertini, Ivano ^a   Capozzi, Francesco ^b   Dikiy, Alexander ^a   Eltis, Lindsay ^c   Luchinat, Claudio ^b  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF BOLOGNA   (Italy)

^c UNIVERSITÉ LAVAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

IRON; SULFUR;

ARTICLE; BINDING AFFINITY; CHROMATIUM VINOSUM; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; THREE DIMENSIONAL IMAGING;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CHROMATIUM; CYSTEINE; IRON-SULFUR PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; POINT MUTATION; PROTEIN CONFORMATION; PROTONS; SERINE; SOLUTIONS; THERMODYNAMICS;

ALLOCHROMATIUM VINOSUM; CHROMATIUM;

EID: 0029974681     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9528513     Document Type: Review

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