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1 Laboratory of Cardiac
Energetics,
The oxygenation
state of myoglobin and the redox state of cytochrome
c provide information on the
PO2 in the cytosol and mitochondria,
respectively. An optical "window" from ~540 to 585 nm was found
in the pig heart in vivo that permitted the monitoring of myoglobin and
cytochrome c without interference from
Hb oxygenation or blood volume. Scanning reflectance spectroscopy was
performed on the surgically exposed left ventricle of pigs. Difference
spectra between control and a total left anterior descending coronary
artery occlusion revealed maxima and minima in this spectral region
consistent with myoglobin deoxygenation and cytochrome c and
b reduction. Comparison of in vivo
data with in vitro fractions of the heart, including Hb-free tissue
whole heart and homogenates, mitochondria, myoglobin, and pig red blood
cells, reveals minimal contributions of Hb in vivo. This conclusion was
confirmed by expanding the blood volume of the myocardium and
increasing mean Hb O2 saturation
with an intracoronary infusion of adenosine (20 µg · kg
1 · min
1),
which had no significant effect on the 540- to 585-nm region. These
results also suggested that myoglobin
O2 saturation was not blood flow
limited under these conditions in vivo. Work jump studies with
phenylephrine also failed to change cytochrome
c redox state or myoglobin
oxygenation. Computer simulations using recent physical data are
consistent with the notion that myoglobin O2 saturation is >92% under
basal conditions and does not change significantly with moderate
workloads. These studies show that reflectance spectroscopy can assess
myocardial oxygenation in vivo. Myoglobin
O2 saturation is very high and is
not labile to moderate changes in cardiac workload in the open-chest
pig model. These findings indicate that myoglobin does not contribute
significantly to O2 transport via
facilitated diffusion under these conditions.
oxygen; mitochondria; oxygen consumption; facilitated diffusion; pig; dog; cytochrome b; cytochrome c; diffusion; computer simulation; hemoglobin
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