Light‐induced oxidation of iron atoms in a photosensitive nitrile hydratase
- 20 April 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 301 (2) , 177-180
- https://doi.org/10.1016/0014-5793(92)81242-e
Abstract
The photoactivation process of a photosensitive nitrile hydratase (NHase) from Rhodococcus sp. N‐771 has been investigated by 57Fe Mössbauer spectroscopy and magnetic susceptibility measurements in order to clarify the behavior of iron atoms in the enzyme. Mössbauer spectra of inactive NHase gave two symmetric‐doublet components indicating the presence of two iron species, while that of the active NHase gave a single symmetric doublet indicating the presence of a single iron species. Magnetic susceptibility measurements of the inactive and active HNase both showed small effective magnetic moments. These results led us to conclude that one of the two iron atoms incorporated in the NHase is oxidized during photoactivation, namely from a low spin ferrous to a low spin ferric state. This is the first observation of an intramolecular photooxidation phenomena involving iron in a single protein molecule.Keywords
This publication has 9 references indexed in Scilit:
- Crystallization of a photosensitive nitrile hydratase from Rhodococcus sp. N-771Journal of Molecular Biology, 1991
- Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydrataseJournal of Bacteriology, 1990
- Purification of inactivated photoresponsive nitrile hydrataseBiochemical and Biophysical Research Communications, 1990
- PHOTOSENSITIVE PHENOMENA OF NITRILE HYDRATASE OF Rhodococcus sp. N‐771Photochemistry and Photobiology, 1990
- Nobel lecture. A structural basis of light energy and electron transfer in biology.The EMBO Journal, 1989
- Nitrile hydratase. The first non-heme iron enzyme with a typical low-spin iron(III)-active centerJournal of the American Chemical Society, 1987
- The magnetic susceptibility of native soybean lipoxygenase-1. Implications for the symmetry of the iron environmental and the possible coordination of dioxygen to Fe(II)Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Applications to Biological SystemsPublished by Springer Nature ,1984
- Proton Magnetic Resonance, Magnetic Susceptibility and Mössbauer Studies of Clostridium pasteurianum RubredoxinNature, 1970