Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 292, Issue 4, Pages 812-818Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/bbrc.2002.6730
Keywords
hemoglobin; nitric oxide; allostery; time-resolved absorption spectroscopy
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Funding
- NHLBI NIH HHS [HL58091, R29 HL058091] Funding Source: Medline
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Despite earlier work indicating otherwise, some recent reports have suggested that nitric oxide (NO) binds to hemoglobin cooperatively. In particular, it has been suggested that, under physiological conditions, NO binds to the high-affinity R-state hemoglobin as much as 100 times faster than to the low-affinity T-state hemoglobin. This rapid NO binding could provide a means of preserving NO bioactivity. However, using a flash-flow photolysis technique, we have determined that the rate of NO binding to normal adult R-state hemoglobin is (2.1 +/- 0.1) x 10(7) (s(-1) M-1 which is essentially the same as that reported for T-state NO binding. (C) 2002 Elsevier Science (USA).
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