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1 H and 13 C NMR assignment and secondary structure of Chlorobium limicola f. thiosulfatophilum ferrocytochrome c 555
Author(s) -
Morelle Nathalie,
Simorre Jean-Pierre,
Caffrey Michael,
Meyer Terrance,
Cusanovich Michael,
Marion Dominique
Publication year - 1995
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(95)00450-n
Subject(s) - chemistry , crystallography , heme , stereochemistry , chemical shift , heteronuclear single quantum coherence spectroscopy , protein secondary structure , cytochrome c , helix (gastropod) , sulfur , nuclear magnetic resonance spectroscopy , biology , enzyme , ecology , biochemistry , organic chemistry , snail , mitochondrion
The 1 H resonances of the ferrocytochrome c 555 from the anaerobic green sulfur bacterium Chlorobium limicola f thiosulfatophilum (strain Tassajara) have been assigned. Identification of spin systems and sequential assignment of 1 H was accomplished by automated assignment computer programs followed by manual verification. In addition, 13 C resonances have been extensively assigned by HSQC experiments at natural abundance. As determined by short‐range NOE connectivities, 13 C α chemical shifts, and H N exchange experiments, the secondary structure consists of 3 helices ranging from residues 3–13, 43–53 and 70–86. Interestingly, the second helix is significantly longer than observed by X‐ray crystallography [1977, Proc. Natl. Acad. Sci. USA 74, 5244–5247]. A topological model of the cytochrome c 555 is presented based on a small number of long‐range NOE contacts. The helices are shown to pack onto the heme according to the pattern common to all class I cytochromes c .