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 Lettjournal_title
FEBS lettersauthors
Kunishima N,Amada F,Fukuyama K,Kawamoto M,Matsunaga T,Matsubara Hdoi
10.1016/0014-5793(95)01458-6subject
Has Abstractpub_date
1996-01-15 00:00:00pages
291-4issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(95)01458-6journal_volume
378pub_type
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