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cyanometmyoglobin

Known as: cyano-met-myoglobin, met-cyanomyoglobin, metmyoglobin cyanide 
National Institutes of Health

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Metmyoglobin

Papers overview

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Highly Cited
1996
Highly Cited
1996
Magnetic Field Dependence of Nitrogen−Proton J Splittings in 15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar Coupling
One-bond 1JNH couplings have been measured in 15N-enriched human ubiquitin and range from 91.1 to 95.6 Hz. Measurements have been… 
Highly Cited
1990
Highly Cited
1990
Solution structural characteristics of cyanometmyoglobin: resonance assignment of heme cavity residues by two-dimensional NMR.
Steady-state nuclear Overhauser effects (NOE), two-dimensional (2D) nuclear Overhauser effect spectroscopy (NOESY), and 2D spin… 
1990
1990
Formation of methemoglobin and metmyoglobin using 8‐aminoquinoline derivatives or sodium nitrite and subsequent reaction with cyanide
The kinetics of the oxidation of hemoglobin (Hb) and myoglobin (Mb) by sodium nitrite, 8‐[(4‐amino‐1‐methylbutyl)amino]‐6‐methoxy… 
1978
1978
Axial ligand effects on myoglobin stability.
1977
1977
Titration behavior and tautomeric states of individual histidine residues of myoglobins. Application of natural abundance carbon 13 nuclear magnetic resonance spectroscopy.
1975
1975
Deuterium nuclear magnetic resonance of deuterium-labeled diacetyldeuterohemin incorporated into sperm whale myoglobin.
Highly Cited
1974
Highly Cited
1974
Assignments of the paramagnetically shifted heme methyl nuclear magnetic resonance peaks of cyanometmyoglobin by selective deuteration.
Highly Cited
1973
Highly Cited
1973
Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems: ferricytochrome c and metmyoglobin cyanide.
Highly Cited
1970
Highly Cited
1970
Nuclear magnetic resonance determination of ligand-induced conformational changes in myoglobin.
1969
1969
Nuclear magnetic resonances of reconstituted myoglobins.
In proton nuclear magnetic resonance spectra of paramagnetic heme proteins, the resonances of the heme groups are shifted away… 
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