On the reaction of ferric heme proteins with nitrite and sulfite

Optical and EPR spectroscopy of ferric heme proteins of the porphyrin, oxyporphyrin, and isobacteriochlorin classes has indicated that nitrite reacts with these proteins at the heme iron. Sulfite has been conclusively proven to react only with proteins containing the isobacteriochlorin macrocycle. Q...

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Bibliographic Details
Published in:Biochemistry (Easton) 1988-04, Vol.27 (8), p.2790-2800
Main Authors: Young, Lawrence J, Siegel, Lewis M
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Electron Spin Resonance Spectroscopy
Fundamental and applied biological sciences. Psychology
heme
Heme - metabolism
Hemeproteins - metabolism
Hemoproteins
Kinetics
Metalloproteins
nitrite
Nitrites - metabolism
Oxidation-Reduction
Proteins
Spectrophotometry
sulfite
Sulfites - metabolism
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Summary:Optical and EPR spectroscopy of ferric heme proteins of the porphyrin, oxyporphyrin, and isobacteriochlorin classes has indicated that nitrite reacts with these proteins at the heme iron. Sulfite has been conclusively proven to react only with proteins containing the isobacteriochlorin macrocycle. Quantitative EPR spectroscopy of these nitrite and sulfite adducts showed that most contained a substantial quantity of undetectable heme. It is suggested that protein-induced autoreduction of nitrite (but not sulfite) and a strained and/or uniaxial g-tensor are the principal ways by which the silent state is produced.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00408a020