1H, 13C, and 15N resonance assignments for a ferrocytochrome c553 heme by multinuclear NMR spectroscopy.
A novel strategy has been used to assign the 1H, 13C, and 15N resonances of the heme in Anabaena 7120 ferrocytochrome c553. 13C[13C] double-quantum coherence spectroscopy was used to delineate the heme carbons, 1H[13C] single-bond correlation spectroscopy was used to define the attached protons, and 1H[15N] multiple-bond correlation spectroscopy was used to assign the nitrogens. 1H[13C] multiple-bond correlation spectroscopy confirmed many of the assignments. Proteins were labeled uniformly with 13C or 15N to obtain the required spectral sensitivity.
Zehfus
M H
MH
Biochemistry Department, College of Agricultural and Life Sciences, University of Wisconsin, Madison 53706.
Reily
M D
MD
Ulrich
E L
EL
Westler
W M
WM
Markley
J L
JL
D002247:Carbon Isotopes; D000458:Cyanobacteria / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009587:Nitrogen Isotopes; D010084:Oxidation-Reduction; D011485:Protein Binding
D002247:Carbon Isotopes; D003574:Cytochrome c Group; D009587:Nitrogen Isotopes; C083951:cytochrome c553; D006418:Heme; D006859:Hydrogen; C022302:cytochrome C-552