A Short Fe-Fe Distance in Peroxodiferric Ferritin: Control of Fe Substrate Versus Cofactor Decay?-Reference-Cited by-同舟云学术

A Short Fe-Fe Distance in Peroxodiferric Ferritin: Control of Fe Substrate Versus Cofactor Decay?

Published:2000-01-07 Issue:5450 Volume:287 Page:122-125
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Hwang Jungwon¹,Krebs Carsten²,Huynh Boi Hanh²,Edmondson Dale E.³,Theil Elizabeth C.⁴,Penner-Hahn James E.¹

Affiliation:

1. Department of Chemistry, University of Michigan, Ann Arbor, MI 48109–1055, USA.

2. Department of Physics,

3. Departments of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA.

4. Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609–1673, USA.

Abstract

The reaction of oxygen with protein diiron sites is important in bioorganic syntheses and biomineralization. An unusually short Fe-Fe distance of 2.53 angstroms was found in the diiron (μ-1,2 peroxodiferric) intermediate that forms in the early steps of ferritin biomineralization. This distance suggests the presence of a unique triply bridged structure. The Fe-Fe distances in the μ-1,2 peroxodiferric complexes that were characterized previously are much longer (3.1 to 4.0 angstroms). The 2.53 angstrom Fe-Fe distance requires a small Fe-O-O angle (∼106° to 107°). This geometry should favor decay of the peroxodiferric complex by the release of H 2 O 2 and μ-oxo or μ-hydroxo diferric biomineral precursors rather than by oxidation of the organic substrate. Geometrical differences may thus explain how diiron sites can function either as a substrate (in ferritin biomineralization) or as a cofactor (in O 2 activation).

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference54 articles.

1. Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters

2. Reactions of Non-Heme Iron(II) Centers with Dioxygen in Biology and Chemistry

3. ; G. S. Waldo and E. C. Theil in Bioinorganic Systems vol. 5 of Comprehensive Supramolecular Chemistry K. S. Suslick Ed. (Pergamon Oxford 1996) pp. 65–89.

4. Animals produce H- L- and M-type ferritin subunits; the H and M types have a functional diiron site. The subunits coassemble to form cell-specific mixtures. Although the functional significance of the subunit ratio is not fully understood this ratio is controlled precisely and is fixed at the time of cell differentiation. Plants and bacteria appear to have only a single ferritin subunit of the H type which contains a functional diiron site.

5. Direct Spectroscopic and Kinetic Evidence for the Involvement of a Peroxodiferric Intermediate during the Ferroxidase Reaction in Fast Ferritin Mineralization

Cited by 179 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Mechanistic Insights into the N‐Hydroxylations Catalyzed by the Binuclear Iron Domain of SznF Enzyme: Key Piece in the Synthesis of Streptozotocin;Chemistry – A European Journal;2024-01-29

2. Extension Peptide of Plant Ferritin from Setaria italica Presents a Novel Fold;Journal of Agricultural and Food Chemistry;2022-12-28

3. Distinct structural characteristics define a new subfamily of Mycoplasma ferritin;Chinese Chemical Letters;2022-11

4. Emergence of Function from Nonheme Diiron Oxygenases: A Quantum Mechanical/Molecular Mechanical Study of Oxygen Activation and Organophosphonate Catabolism Mechanisms by PhnZ;ACS Catalysis;2022-01-21

5. Enzymatic deamination of the epigenetic nucleoside N6-methyladenosine regulates gene expression;Nucleic Acids Research;2021-11-24