Tahirov T H, Misaki S, Meyer T E, Cusanovich M A, Higuchi Y, Yasuoka N
Department of Life Science, Faculty of Science, Himeji Institute of Technology, Hyogo, Japan.
Nat Struct Biol. 1996 May;3(5):459-64. doi: 10.1038/nsb0596-459.
We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c'. This is the first example of a ligand-bound structure of a class IIa cytochrome c. Compared with the structure of native cytochrome c', there are significant conformational changes of amino acid residues in the haem vicinity, accompanied by a rearrangement of the hydrogen bonding pattern. The results suggest that rearrangements resulting from ligand binding could drive dimer dissociation in some species and also that the haem propionate may participate in proton transfer.
我们已经确定了正丁基异腈结合的荚膜红细菌细胞色素c'的结构。这是IIa类细胞色素c配体结合结构的首个实例。与天然细胞色素c'的结构相比，血红素附近的氨基酸残基发生了显著的构象变化，同时氢键模式也发生了重排。结果表明，配体结合导致的重排可能会促使某些物种中的二聚体解离，并且血红素丙酸酯可能参与质子转移。
