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Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X‐ray crystallographic analysis of the complex at 1.6 Å resolution
Author(s) -
Itakura Hiroyuki,
Oda Yutaka,
Fukuyama Keiichi
Publication year - 1997
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/s0014-5793(97)00751-5
Subject(s) - heme , chemistry , hydrogen bond , molecule , peroxidase , ligand (biochemistry) , crystallography , stereochemistry , resolution (logic) , crystal structure , ring (chemistry) , active site , enzyme , biochemistry , receptor , organic chemistry , artificial intelligence , computer science
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 His 56 N ϵ , Arg 52 N ϵ , and Pro 154 O, 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.