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J. Biol. Chem., Vol. 263, Issue 5, 2316-2323, 02, 1988
J Goretski and TC Hollocher
A spectrophotometric method has been developed that uses extracellular
hemoglobin (Hb) to trap nitric oxide (NO) released during denitrification
as nitrosyl hemoglobin (HbNO). The rate of complexation of NO with Hb is
about at the diffusion controlled limit for protein molecules and the
product, HbNO, is essentially stable. Hb was added to an anaerobic
bacterial suspension and denitrification was initiated with either KNO2 or
KNO3. HbNO formation was observed for six species of denitrifying bacteria
and showed isosbestic points at 544, 568, and 586 nm. Cellular NO
production, presumably by nitrite reductase, was kinetically distinct from
the much slower chemical reaction of Hb with KNO2 to form methemoglobin and
HbNO. The rate of HbNO formation was proportional to cell density,
essentially independent of pH from 6.8 to 7.4, nearly zero order in [Hb]
and, at least with Paracoccus denitrificans, strongly inhibited by rotenone
and antimycin A. The Cu chelator, diethyldithiocarbamate, had no effect on
HbNO formation by Pa. denitrificans, but abolished that by Achromobacter
cycloclastes which uses a Cu-containing nitrite reductase known to be
inactivated by the chelator. HbNO formation did not occur with
non-denitrifying bacteria. The stoichiometry at high [Hb] for conversion of
Hb to HbNO was 1.3-1.8 KNO2 per Hb for Pa. denitrificans, Pseudomonas
aeruginosa, and A. cycloclastes and about 3.4 for Pseudomonas stutzeri. The
former range of values corresponds to a partition of about 2 N atoms in 3
toward trapping and 1 in 3 toward reduction on the pathway to N2. Nitrogen
not trapped appeared largely as N2O in presence of acetylene. The results
are consistent with a model in which NO is a freely diffusible intermediate
between nitrite and N2O, providing that nitric oxide reductase is or nearly
is a diffusion controlled enzyme.
Trapping of nitric oxide produced during denitrification by extracellular hemoglobin
Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254.
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