Journal of Biological Chemistry
Volume 276, Issue 32, 10 August 2001, Pages 30106-30110
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PROTEIN STRUCTURE AND FOLDING
Human Neuroglobin, a Hexacoordinate Hemoglobin That Reversibly Binds Oxygen*

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Neuroglobin is a newly discovered mammalian hemoglobin that is expressed predominately in the brain (Burmester, T., Welch, B., Reinhardt, S., and Hankeln, T. (2000) Nature407, 520–523). Neuroglobin has less than 25% identity with other vertebrate globins and shares less than 30% identity with the annelid nerve myoglobin it most closely resembles among known hemoglobins. Spectroscopic and kinetic experiments with the recombinant protein indicate that human neuroglobin is the first example of a hexacoordinate hemoglobin in vertebrates and is similar to plant and bacterial hexacoordinate hemoglobins in several respects. The ramifications of hexacoordination and potential physiological roles are explored in light of the determination of an O2 affinity that precludes neuroglobin from functioning in traditional O2 storage and transport.

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Published, JBC Papers in Press, June 27, 2001, DOI 10.1074/jbc.C100300200

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This work was supported by United States Department of Agriculture Award 99-35306-7833.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.