Mössbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting.
Open Access
- 1 June 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (11), 6833-6840
- https://doi.org/10.1016/s0021-9258(17)39803-4
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and optical spectroscopyFEBS Letters, 1983
- Heme P460 of Hydroxylamine Oxidoreductase of NitrosomonasEuropean Journal of Biochemistry, 1983
- A b i n i t i o MO studies of electronic states and Mössbauer spectra of high-, intermediate-, and low-spin Fe(II)-porphyrin complexesThe Journal of Chemical Physics, 1982
- Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 2. Moessbauer spectroscopyBiochemistry, 1982
- Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopyBiochemistry, 1982
- Reaction of oxygen with hydroxylamine oxidoreductase of NitrosomonasFEBS Letters, 1982
- Hydroxylamine oxidoreductase: a 20-heme, 200,000 molecular weight cytochrome c with unusual denaturation properties which forms a 63,000 molecular weight monomer after heme removalBiochemistry, 1981
- Studies on heme d1 extracted from Pseudomonas aeruginosa nitrite reductaseJournal of Inorganic Biochemistry, 1981
- Hydroxylamine oxidoreductase from Nitrosomonas: inactivation by hydrogen peroxideBiochemistry, 1977
- Moessbauer investigations of high-spin ferrous heme proteins. I. Cytochrome P-450Biochemistry, 1975