Myoglobin reaction with

Compared with Molsidomine, both SIN-1 and SIN-1A are reported to induce similar, but more rapid hypotensive action [95, 96]. SIN-1A, after undergoing oxidation in the presence of oxygen or, in vivo, possibly by redox-active enzymes such as cytochrome C [97, 98] or by reaction with ferric myoglobin formed during reperfusion injury [99], releases NO through an intermediate radical cation. 

Antonini, E., Brunori, M. Hemoglobin and Myoglobin in their Reactions with Ligands. Amsterdam North-Holland 1971. 

E. Antonini and M. Brunori, Hemoglobin and Myoglobin in Their Reactions with Ligands, North-Holland Publishing, Amsterdam, 1971. 

Antonioni, E. Brunori, M. Hemoglobins and Myoglobins and Their Reactions with Ligands North Holland Pubhshing Co. Amsterdam, 1971. 

Antonini E, Brunori M (1971) In Hemoglobins and myoglobins in their reactions with ligands, North-Holland, Amsterdam, chap 4... 

Both siroheme enzymes form ferroheme-NO complexes in which the g value anisotropy appears somewhat smaller than in the corresponding complexes of most other enzymes. The EPR spectra of the complexes somewhat resemble the spectra of the high-temperature myoglobin-NO complexes. The hyperfine splitting from the NO nitrogen nucleus is evident at intermediate g values but is not well resolved. These enzymes are capable of reducing NO to ammonia if supplied with low potential reducing equivalents. Other heme proteins also catalyze oxidation reduction reactions with NO. 

Fox, J. B., and Ackerman, S. A. (1968). Formation of nitric oxide myoglobin Mechanisms of the reaction with various reductants. J. Food Set. 33, 364-370. 

Perutz, M.F. (1989) Myoglobin and haemoglobin role of distal residues in reactions with haem ligands. Trends Biochem. Sci. 14, 42 4. 

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