Faculty Collaboration Database

Type 2 Cu2+ in pMMO from Methylomicrobium album BG8. Biophys J 1999 Apr;76(4):2223-9

Date

03/30/1999

Pubmed ID

10096917

Pubmed Central ID

PMC1300195

DOI

10.1016/S0006-3495(99)77378-9

Scopus ID

2-s2.0-0032586758 (requires institutional sign-in at Scopus site)   32 Citations

Abstract

EPR spectra were obtained for the type 2 Cu2+ site in particulate methane monooxygenase (pMMO) from Methylomicrobium album BG8 grown on K15NO3 and 63Cu(NO3)2. The concentration of the type 2 Cu2+ signal was approximately 200 microM per 25 mg/ml protein in packed cells and membrane fractions, a concentration that is consistent with its attribution to pMMO, and the EPR parameters were consistent with electron paramagnetic resonance (EPR) parameters previously assigned to pMMO. The superhyperfine structure due to nitrogen is better resolved because I = 1/2 for 15N whereas I = 1 for 14N and A(15N)/A(14N) = 1.4. Under these conditions, superhyperfine structure is resolved in the g region of the X-band spectrum. At low microwave frequency (S-band) the resolution of the nitrogen superhyperfine structure improves. Signals are attributed to type 2 Cu2+ in which cupric ion is bound to four (less likely three) nitrogen donor atoms.

Author List

Yuan H, Collins ML, Antholine WE

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Binding Sites
Biophysical Phenomena
Biophysics
Copper
Electron Spin Resonance Spectroscopy
Methylococcaceae
Models, Chemical
Molecular Sequence Data
Molecular Structure
Nitrogen
Oxygenases
Peptide Fragments