The primary structure of cytochrome P460 ofNitrosomonas europaea: Presence of ac-heme binding motif
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)01072-2/fullpdf
Reference23 articles.
1. P460 of hydroxylamine oxidoreductase of Nitrosomonas europaea: Soret resonance Raman evidence for a novel heme-like structure
2. Mössbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting.
3. Evidence for the structure of the active site heme P460 in hydroxylamine oxidoreductase of Nitrosomonas
4. Localization and concentration of hydroxylamine oxidoreductase and cytochromes c-552, c-554, cm-553, cm-552 and a in Nitrosomonas europaea
5. Preliminary characterization of a variant co-binding heme protein from Nitrosomonas
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