Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

Non-heme iron enzymes catalyze a wide range of O 2 reactions, paralleling those of heme systems. Non-heme iron active sites are, however, much more difficult to study because they do not exhibit the intense spectral features characteristic of the porphyrin ligand. A spectroscopic methodology was developed that provides significant mechanistic insight into the reactivity of non-heme ferrous active sites. These studies reveal a general mechanistic strategy used by these enzymes and differences in substrate and cofactor interactions dependent on their requirement for activation by iron. Contributions to O 2 activation have been elucidated for non-heme relative to heme ligand sets, and major differences in reactivity are defined with respect to the heterolytic and homolytic cleavage of O—O bonds.

Bibliography

Solomon, E. I., Decker, A., & Lehnert, N. (2003). Non-heme iron enzymes: Contrasts to heme catalysis. Proceedings of the National Academy of Sciences, 100(7), 3589–3594.

Dates
Type When
Created 22 years, 5 months ago (April 1, 2003, 2:25 p.m.)
Deposited 3 years, 4 months ago (April 12, 2022, 8:47 a.m.)
Indexed 2 weeks, 4 days ago (Aug. 19, 2025, 7:05 a.m.)
Issued 22 years, 6 months ago (Feb. 21, 2003)
Published 22 years, 6 months ago (Feb. 21, 2003)
Published Online 22 years, 6 months ago (Feb. 21, 2003)
Published Print 22 years, 5 months ago (April 1, 2003)
Funders 0

None

@article{Solomon_2003, title={Non-heme iron enzymes: Contrasts to heme catalysis}, volume={100}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0336792100}, DOI={10.1073/pnas.0336792100}, number={7}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Solomon, Edward I. and Decker, Andrea and Lehnert, Nicolai}, year={2003}, month=feb, pages={3589–3594} }