Assignment of the 1511 cm(-1) UV resonance Raman marker band of hemoglobin to tryptophan

Biopolymers
X ZhaoT G Spiro

Abstract

New UV resonance Raman (UVRR) data provide convincing evidence that a characteristic 1511 cm(-1) band in the T - R difference spectra of hemoglobin is due to the overtone of the Trp W18 fundamental at 756 cm(-1). Measured isotope shifts for 2-H and 15-N substitution at the indole NH group are twice as large for the 1511 cm(-1) band as for W18, and the 1511 cm(-1) intensity scales with that of W18 in the difference spectrum. Moreover, the UVRR excitation profile of the 1511 cm(-1) band tracks that of another tryptophan band, W16. Both are redshifted in hemoglobin, relative to aqueous tryptophan, reflecting H bonding within a hydrophobic environment in the protein. The 2xW18 assignment had been thrown into question by the observation of remnant 1511 cm(-1) intensity in the T - R spectra of hemoglobin labeled with tryptophan-d(5), a substitution that shifts W18 over 50 cm(-1). However, reexamination of the data suggests that this remnant intensity may result from a subtraction artifact arising from the downshift of another difference band, W3, from 1549 cm(-1) in unlabeled protein to 1522 cm(-1) in labeled protein. Restoration of the 2xW18 assignment establishes that the 1511 cm(-1) difference band, which is a useful indicator of ...Continue Reading

References

Jan 15, 1980·Journal of Molecular Biology·J M Baldwin

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Citations

Nov 21, 2008·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Lijun MaYihong Ding
Dec 22, 2005·Journal of Molecular Biology·Janina KneippThomas G Spiro

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