1GZB

PEROXIDASE

Summary for 1GZB

• Entry DOI: 10.2210/pdb1gzb/pdb
• Descriptor: PEROXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, glycoprotein, peroxidase, heme
• Biological source: 'Arthromyces ramosus'
• Cellular location: Secreted: P28313
• Total number of polymer chains: 1
• Total formula weight: 36843.84

Authors

Fukuyama, K.,Kunishima, N.,Amada, F. (deposition date: 1996-11-13, release date: 1997-03-12, Last modification date: 2020-07-29)

Primary citation

Kunishima, N.,Amada, F.,Fukuyama, K.,Kawamoto, M.,Matsunaga, T.,Matsubara, H.
Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 A resolution crystallographic study at pH 4.5.
FEBS Lett., 378:291-294, 1996

PubMed 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.

PubMed: 8557120
DOI: 10.1016/0014-5793(95)01458-6

Experimental method

X-RAY DIFFRACTION (1.8 Å)