Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X‐ray crystallographic analysis of the complex at 1.6 Å resolution

FEBS Letters

Itakura, Hiroyuki¹  Oda, Yutaka¹  Fukuyama, Keiichi¹ 

[1] Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560, Japan

关键词: Peroxidase;    Heme enzyme;    Benzhydroxamic acid;    X-ray crystallography;    Arthromyces ramosus;    ARP;    Arthromyces ramosus peroxidase;    BHA;    benzhydroxamic acid;    HRP;    horseradish peroxidase;    SHA;    salicylhydroxamic acid;    IP;    imaging plate;   

DOI  :  10.1016/S0014-5793(97)00751-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of Arthromyces ramosus peroxidase (ARP) in complex with benzhydroxamic acid (BHA) as determined by X-ray analysis at 1.6 Å shows unambiguously how BHA binds to ARP. BHA is located in the distal heme pocket. Its functional groups are held by three hydrogen bonds to His⁵⁶N_ϵ, Arg⁵²N_ϵ, and Pro¹⁵⁴O, but are too far away to interact with the heme iron. The aromatic ring of BHA is positioned at the entrance of the channel to the heme pocket, approximately parallel to the heme group. Most water molecules at the active site of the native enzyme are replaced by BHA, leaving a ligand, probably a water molecule, at the sixth position of the heme. Results are compared with spectroscopic data.

【 授权许可】

Unknown