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Studies on heme binding in myoglobin, hemoglobin, and cytochromecby ion spray mass spectrometry

✍ Scribed by Y.-T. Li; Y.-L. Hsieh; J.D. Henion; B. Ganem

Book ID: 103995710
Publisher: Elsevier Science
Year: 1993
Tongue: English
Weight: 655 KB
Volume: 4
Category: Article
ISSN: 1044-0305
DOI: 10.1016/1044-0305(93)85027-u

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✦ Synopsis

The ion spray mass spectra of three representative heme-containing proteins were studied, with an emphasis on results obtained under neutral (pH 7) aqueous conditions. The noncovalently bound heme in myoglobin and hemoglobin may be readily distinguished from the covalently bound heme prosthetic group attached to cytochrome c by using collisioninduced dissociation in the free-jet expansion region of the mass spectrometer as well as in the collision quadrupole with premass selection. The charge state of iron in the expelled heme from myoglobin and hemoglobin appears to be 3+ but 2f for heme expelled from cytochrome c.

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