Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy.

ABSTRACT: The UV-vis absorption, Raman imaging, and resonance Raman (rR) spectroscopy methods were employed to study cyanohemoglobin (HbCN) adducts inside living functional red blood cells (RBCs). The cyanide ligands are especially optically sensitive probes of the active site environment of heme proteins. The rR studies of HbCN and its isotopic analogues (¹³CN^-, C¹⁵N^-, and ¹³C¹⁵N^-), as well as a careful deconvolution of spectral data, revealed that the ν(Fe-CN) stretching, δ(Fe-CN) bending, and ν(C≡N) stretching modes occur at 454, 382, and 2123 cm^-1, respectively. Interestingly, while the ν(Fe-CN) modes exhibit the same frequencies in both the isolated and RBC-enclosed hemoglobin molecules, small frequency diff

SUBMITTER: Dybas J 

PROVIDER: S-EPMC8154613 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature