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Formation of Nitric Oxide Myoglobin: Mechanisms of the Reaction with Various Reductants
Author(s) -
FOX J. B.,
ACKERMAN S. A.
Publication year - 1968
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1968.tb03631.x
Subject(s) - chemistry , metmyoglobin , myoglobin , nitric oxide , ascorbic acid , nitrite , inorganic chemistry , oxygen , ferrous , photochemistry , organic chemistry , food science , nitrate
SUMMARY– The concentration, temperature and pH dependences of the formation of nitric oxide myoglobin (NOMb) from metmyoglobin nitrite (MetMb·NO 2 ) were determined for nitrite and the reductants, ascorbic acid, cysteine, hydro‐quinone, nicotinamide adenine dinucleotide (NADH) and glyceraldehyde. The reaction for all reductants except glyceraldehyde involves the production of a nitroso‐reductant intermediate which breaks down to release nitric oxide. The latter forms a nitric oxide metheme complex (Fe +++ ) which is then reduced to the ferrous state (Fe ++ ). With cysteine and NADH there is a second pathway which probably involves the direct reduction of MetMb NO 2 . Ascorbate and hydro‐quinone form nitroso intermediates that are stabilized in alkali. The effects of oxygen, ethylenediaminetetraacetic acid and cytochrome c on the reaction were determined. Oxygen slows or inhibits the reaction, while the latter two have no effect on the reaction as studied.

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