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Investigation of the solution structures and mobility of oxidised and reduced cytochrome b 5 by 2D NMR spectroscopy
Author(s) -
Veitch Nigel C.,
Concar David W.,
Williams Robert J.P.,
Whitford David
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80223-0
Subject(s) - chemistry , cytochrome , cytochrome c , nuclear magnetic resonance spectroscopy , spectroscopy , crystallography , nuclear overhauser effect , electron transfer , redox , analytical chemistry (journal) , stereochemistry , inorganic chemistry , organic chemistry , biochemistry , physics , mitochondrion , enzyme , quantum mechanics
Two dimensional 1 H NMR spectroscopy is used to examine the structure and mobility of cytochrome b 5 in solution. The assignment of many residues and the interpretation of nuclear Overhauser effects (NOEs) in both redox states allow definition of secondary structural elements. Comparison with X‐ray diffraction data shows that differences between crystal and solution structures are small. The dynamics of the protein are examined and the protein is shown to be more mobile than cytochrome c . The relationship of the structure and dynamics to the electron transfer function of cytochrome b 5 is discussed.