高铁细胞色素c的碱性异构化：赖氨酸配体的鉴定
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
作者信息
Wilgus H, Stellwagen E
出版信息
Proc Natl Acad Sci U S A. 1974 Jul;71(7):2892-4. doi: 10.1073/pnas.71.7.2892.
Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65.peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the heme iron upon isomerization of ferricytochrome c and that the ligand in the horse heart protein is one of the eight lysine residues in the 66-104 segment of the polypeptide, most likely lysine 79.
将马心细胞色素c血肽1 - 65、肽66 - 104及其胍基化对应物的复合物的可见吸收光谱变化与天然和完全胍基化的高铁细胞色素c在pH值7至11范围内的特征光谱进行比较。随着pH值升高，胍基化血肽1 - 65.肽66 - 104复合物中的甲硫氨酸配体被强场配体取代。相比之下，血肽1 - 65.胍基化肽66 - 104中的甲硫氨酸配体被弱场配体取代。这些结果表明，高铁细胞色素c异构化时，赖氨酸13不与血红素铁配位，并且马心蛋白中的配体是多肽66 - 104片段中的八个赖氨酸残基之一，最有可能是赖氨酸79。
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