A 1H NMR study of bovine cytochrome oxidase. Paramagnetically shifted resonances of haem a.
Dimeric and monomeric forms of mitochondrial cytochrome oxidase (EC 1.9.3.1) have been examined using 1H NMR spectroscopy. Paramagnetically shifted resonances were detected in spectra of the monomeric protein. Studies of this protein in a number of oxidation and ligation states have assigned these resonances to ferrihaem a. The temperature and pH dependence of this new probe of haem a environment is reported.
Rigby
S E
SE
School of Chemical Sciences, University of East Anglia, Norwich, England.
Alleyne
T A
TA
Wilson
M T
MT
Moore
G R
GR
D000818:Animals; D002417:Cattle; D003576:Electron Transport Complex IV; D006418:Heme; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008929:Mitochondria, Heart / Q000201:enzymology; D011487:Protein Conformation; D013816:Thermodynamics
D006418:Heme; D006859:Hydrogen; D003576:Electron Transport Complex IV