Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1

W. Minor, J. Steczko, J. T. Bolin, Z. Otwinowski, B. Axelrod

Research output: Contribution to journalArticle

130 Citations (Scopus)

Abstract

Five ligands of the active site iron atom in soybean lipoxygenase L-1 have been identified from the electron density map of the crystallized enzyme. The position of the iron atom can be readily and independently located from an anomalous difference electron density map. The ligands identified are His- 499, His-504, His-690, Asn-694, and Ile-839, the carboxy-terminal residue. Our previous view that these three histidines are essential for activity and binding of iron, based on site-specific mutation studies, is confirmed. A sixth protein ligand is not present, and the sixth coordination site opens into a wide cleft. The structure of the soybean lipoxygenase was solved by multiple anomalous isomorphous replacements.

Original languageEnglish (US)
Pages (from-to)6320-6323
Number of pages4
JournalBiochemistry
Volume32
Issue number25
StatePublished - 1993

Fingerprint

Catalytic Domain
Iron
Ligands
Carrier concentration
Electrons
Atoms
Lipoxygenase
Soybeans
Histidine
Mutation
Enzymes
lipoxygenase L-1
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Minor, W., Steczko, J., Bolin, J. T., Otwinowski, Z., & Axelrod, B. (1993). Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. Biochemistry, 32(25), 6320-6323.

Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. / Minor, W.; Steczko, J.; Bolin, J. T.; Otwinowski, Z.; Axelrod, B.

In: Biochemistry, Vol. 32, No. 25, 1993, p. 6320-6323.

Research output: Contribution to journalArticle

Minor, W, Steczko, J, Bolin, JT, Otwinowski, Z & Axelrod, B 1993, 'Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1', Biochemistry, vol. 32, no. 25, pp. 6320-6323.
Minor, W. ; Steczko, J. ; Bolin, J. T. ; Otwinowski, Z. ; Axelrod, B. / Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. In: Biochemistry. 1993 ; Vol. 32, No. 25. pp. 6320-6323.
@article{9bd9741833744a23b78bd6f9b60c8b57,
title = "Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1",
abstract = "Five ligands of the active site iron atom in soybean lipoxygenase L-1 have been identified from the electron density map of the crystallized enzyme. The position of the iron atom can be readily and independently located from an anomalous difference electron density map. The ligands identified are His- 499, His-504, His-690, Asn-694, and Ile-839, the carboxy-terminal residue. Our previous view that these three histidines are essential for activity and binding of iron, based on site-specific mutation studies, is confirmed. A sixth protein ligand is not present, and the sixth coordination site opens into a wide cleft. The structure of the soybean lipoxygenase was solved by multiple anomalous isomorphous replacements.",
author = "W. Minor and J. Steczko and Bolin, {J. T.} and Z. Otwinowski and B. Axelrod",
year = "1993",
language = "English (US)",
volume = "32",
pages = "6320--6323",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "25",

}

TY - JOUR

T1 - Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1

AU - Minor, W.

AU - Steczko, J.

AU - Bolin, J. T.

AU - Otwinowski, Z.

AU - Axelrod, B.

PY - 1993

Y1 - 1993

N2 - Five ligands of the active site iron atom in soybean lipoxygenase L-1 have been identified from the electron density map of the crystallized enzyme. The position of the iron atom can be readily and independently located from an anomalous difference electron density map. The ligands identified are His- 499, His-504, His-690, Asn-694, and Ile-839, the carboxy-terminal residue. Our previous view that these three histidines are essential for activity and binding of iron, based on site-specific mutation studies, is confirmed. A sixth protein ligand is not present, and the sixth coordination site opens into a wide cleft. The structure of the soybean lipoxygenase was solved by multiple anomalous isomorphous replacements.

AB - Five ligands of the active site iron atom in soybean lipoxygenase L-1 have been identified from the electron density map of the crystallized enzyme. The position of the iron atom can be readily and independently located from an anomalous difference electron density map. The ligands identified are His- 499, His-504, His-690, Asn-694, and Ile-839, the carboxy-terminal residue. Our previous view that these three histidines are essential for activity and binding of iron, based on site-specific mutation studies, is confirmed. A sixth protein ligand is not present, and the sixth coordination site opens into a wide cleft. The structure of the soybean lipoxygenase was solved by multiple anomalous isomorphous replacements.

UR - http://www.scopus.com/inward/record.url?scp=0027260861&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027260861&partnerID=8YFLogxK

M3 - Article

C2 - 8518276

AN - SCOPUS:0027260861

VL - 32

SP - 6320

EP - 6323

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 25

ER -