Ascaris haemoglobin is a nitric oxide-activated ‘deoxygenase’
Dena M. Minning,
Andrew J. Gow,
Joseph Bonaventura,
Rod Braun,
Mark Dewhirst,
Daniel E. Goldberg and
Jonathan S. Stamler
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Dena M. Minning: Washington University School of Medicine
Andrew J. Gow: Washington University School of Medicine
Joseph Bonaventura: Duke University Medical Center
Rod Braun: Department of Medicine
Mark Dewhirst: Department of Medicine
Jonathan S. Stamler: Howard Hughes Medical Institute,
Nature, 1999, vol. 401, issue 6752, 497-502
Abstract:
Abstract The parasitic nematode Ascaris lumbricoides infects one billion people worldwide. Its perienteric fluid contains an octameric haemoglobin1,2,3 that binds oxygen nearly 25,000 times more tightly than does human haemoglobin4,5. Despite numerous investigations, the biological function of this molecule has remained elusive. The distal haem pocket contains a metal, oxygen and thiol6, all of which are known to be reactive with nitric oxide. Here we show that Ascaris haemoglobin enzymatically consumes oxygen in a reaction driven by nitric oxide, thus keeping the perienteric fluid hypoxic. The mechanism of this reaction involves unprecedented chemistry of a haem group, a thiol and nitric oxide. We propose that Ascaris haemoglobin functions as a ‘deoxygenase’, using nitric oxide to detoxify oxygen. The structural and functional adaptations of Ascaris haemoglobin suggest that the molecular evolution of haemoglobin can be rationalized by its nitric oxide related functions.
Date: 1999
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:401:y:1999:i:6752:d:10.1038_46822
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DOI: 10.1038/46822
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