When an amide is more like histidine than imidazole: The role of axial ligands in heme catalysis

被引:48
作者
Goodin, DB
机构
[1] Department of Molecular Biology, Scripps Research Institute, San Diego, CA 92037
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 1996年 / 1卷 / 04期
关键词
axial ligands; peroxidases; heme enzymes; imidazole; electron transfer;
D O I
10.1007/s007750050065
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Of the many subtle protein-cofactor interactions which facilitate oxidative catalysis by heme enzymes, the role of the axial ligand has for some time appeared to be fairly well understood. Recent studies from several laboratories, however, have provided good reason to reemphasize the importance of secondary interactions between the axial ligand and protein, as the results suggest that simple ligand identity is neither necessary nor sufficient for function. It has been widely proposed that the strong hydrogen bond between a proximal carboxylate and the histidine ligand of peroxidases assists O-O bond heterolysis and stabilizes the Fe(IV) = O center that is produced. Recent replacements of the axial ligand in a number of heme proteins have produced a few surprises, suggesting that the subtle interactions between the ligand and protein may in some cases be more important than the actual identity of the ligand.
引用
收藏
页码:360 / 363
页数:4
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