TY - JOUR
T1 - Investigation of bioactive NO-scavenging role of myoglobin in myocardium
AU - Kreutzer, Ulrike
AU - Jue, Thomas
PY - 2006/4
Y1 - 2006/4
N2 - Because nitric oxide (NO) can react with myoglobin (Mb) to oxidize the heme Fe(II) to Fe(III), the appearance of metmyoglobin (metMb) during bradykinin stimulation underpins the hypothesis that Mb acts as an NO scavenger in the cell. Although some experiments have detected the reporter metMb signal in the -3.7 ppm spectral region, others have not corroborated the finding. Because metMb also has characteristic hyperfine-shifted signals in the 40-100 ppm spectral region, detection of these signals would confirm the presence of metMb. Perfused rat myocardium study has examined this spectral region in a range of bradykinin infusion protocols. Although bradykinin elicits a set of physiological responses, consistent with the induction of NO, the 1H nuclear magnetic resonance spectra in all experiments reveal no detectable metMb signals. Moreover, in the perfused myocardium model, the bradykinin-induced decline in myocardial oxygen consumption does not appear to arise only from NO binding to cytochrome oxidase.
AB - Because nitric oxide (NO) can react with myoglobin (Mb) to oxidize the heme Fe(II) to Fe(III), the appearance of metmyoglobin (metMb) during bradykinin stimulation underpins the hypothesis that Mb acts as an NO scavenger in the cell. Although some experiments have detected the reporter metMb signal in the -3.7 ppm spectral region, others have not corroborated the finding. Because metMb also has characteristic hyperfine-shifted signals in the 40-100 ppm spectral region, detection of these signals would confirm the presence of metMb. Perfused rat myocardium study has examined this spectral region in a range of bradykinin infusion protocols. Although bradykinin elicits a set of physiological responses, consistent with the induction of NO, the 1H nuclear magnetic resonance spectra in all experiments reveal no detectable metMb signals. Moreover, in the perfused myocardium model, the bradykinin-induced decline in myocardial oxygen consumption does not appear to arise only from NO binding to cytochrome oxidase.
KW - Bioenergetics
KW - NMR
KW - Oxidative phosphorylation
KW - Respiration
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U2 - 10.1007/s00424-005-0011-z
DO - 10.1007/s00424-005-0011-z
M3 - Article
C2 - 16468052
AN - SCOPUS:33645355901
VL - 452
SP - 36
EP - 42
JO - Pflugers Archiv European Journal of Physiology
JF - Pflugers Archiv European Journal of Physiology
SN - 0031-6768
IS - 1
ER -