1C8I

BINDING MODE OF HYDROXYLAMINE TO ARTHROMYCES RAMOSUS PEROXIDASE

Summary for 1C8I

• Entry DOI: 10.2210/pdb1c8i/pdb
• Descriptor: PROTEIN (PEROXIDASE), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose, ... (7 entities in total)
• Functional Keywords: oxidoreductase, glycoprotein, peroxidase
• Biological source: 'Arthromyces ramosus'
• Cellular location: Secreted: P28313
• Total number of polymer chains: 1
• Total formula weight: 37057.03

Authors

Wariishi, H.,Nonaka, D.,Johjima, T.,Nakamura, N.,Naruta, Y.,Kubo, K.,Fukuyama, K. (deposition date: 2000-05-08, release date: 2001-01-17, Last modification date: 2024-10-09)

Primary citation

Wariishi, H.,Nonaka, D.,Johjima, T.,Nakamura, N.,Naruta, Y.,Kubo, S.,Fukuyama, K.
Direct binding of hydroxylamine to the heme iron of Arthromyces ramosus peroxidase. Substrate analogue that inhibits compound I formation in a competetive manner.
J.Biol.Chem., 275:32919-32924, 2000

PubMed Abstract: The interaction of hydroxylamine (HA) with Arthromyces ramosus peroxidase (ARP) was investigated by kinetic, spectroscopic, and x-ray crystallographic techniques. HA inhibited the reaction of native ARP with H(2)O(2) in a competitive manner. Electron absorption and resonance Raman spectroscopic studies indicated that pentacoordinate high spin species of native ARP are converted to hexacoordinate low spin species upon the addition of HA, strongly suggesting the occurrence of a direct interaction of HA with ARP heme iron. Kinetic analysis exhibited that the apparent dissociation constant is 6.2 mm at pH 7.0 and that only one HA molecule likely binds to the vicinity of the heme. pH dependence of HA binding suggested that the nitrogen atom of HA could be involved in the interaction with the heme iron. X-ray crystallographic analysis of ARP in complex with HA at 2.0 A resolution revealed that the electron density ascribed to HA is located in the distal pocket between the heme iron and the distal His(56). HA seems to directly interact with the heme iron but is too far away to interact with Arg(52). In HA, it is likely that the nitrogen atom is coordinated to the heme iron and that hydroxyl group is hydrogen bonded to the distal His(56).

PubMed: 10915789
DOI: 10.1074/jbc.M004223200

Experimental method

X-RAY DIFFRACTION (2 Å)