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Science 23 April 1993:
Vol. 260. no. 5107, pp. 539 - 541
DOI: 10.1126/science.8386393
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Articles

Science, Vol 260, Issue 5107, 539-541
Copyright © 1993 by American Association for the Advancement of Science

articles

Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect

JM Ribeiro, JM Hazzard, RH Nussenzveig, DE Champagne, and FA Walker

Department of Entomology, University of Arizona, Tucson 85721.

The bloodsucking bug Rhodnius prolixus has a salivary vasodilator, previously characterized as a nitrovasodilator, with salivary smooth muscle-relaxing and antiplatelet activity. Rhodnius salivary glands are bright red owing to the abundance of heme proteins. Electron paramagnetic resonance and optical spectroscopic experiments indicated that the salivary vasodilator is a nitrosylheme protein with an Fe(III) heme that binds nitric oxide (NO) reversibly. Dilution of the protein in neutral pH promoted NO release. This protein thus appears to be the NO carrier that helps R. prolixus to feed on blood.


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Molecular Cloning and Expression of an Avian Macrophage Nitric-oxide Synthase cDNA and the Analysis of the Genomic 5`-Flanking Region.
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Purification, Partial Characterization, and Cloning of Nitric Oxide-carrying Heme Proteins (Nitrophorins) from Salivary Glands of the Blood-sucking Insect Rhodnius prolixus.
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