Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 A resolution crystallographic study at pH 4.5.

Abstract:

:In the presence of ammonium sulfate the absorption spectra of a peroxidase from the fungus Arthromyces ramosus (ARP) showed that the low-spin component increased as the pH increased from 6.0 to 9.0, whereas in its absence ARP remained in the high-spin state in the pH range investigated. The crystal structure of ARP at pH 4.5 in the presence of ammonium sulfate at 1.8 A resolution showed that the electron density at the 6th position of the heme iron seen at pH 7.5 had disappeared and that the iron atom deviated markedly from the heme plane. These observations strongly suggest that under physiological conditions the heme of ARP is in the pentacoordinated high-spin state and that at a high pH the heme iron is able to bind ammonia, forming the low-spin state. The location of the water molecule at the distal side of the heme in peroxidases is also discussed.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kunishima N,Amada F,Fukuyama K,Kawamoto M,Matsunaga T,Matsubara H

doi

10.1016/0014-5793(95)01458-6

subject

Has Abstract

pub_date

1996-01-15 00:00:00

pages

291-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01458-6

journal_volume

378

pub_type

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