Resonance Raman spectra are reported for hemoglobin (Hb) with deep UV excitation at 212 and 200 nm. At 200 nm, strongly enhanced amide bands appear, but the spectra are dominated by tyrosine residues, and substantial enhancement is seen for the Y7aº mode, a sensitive monitor of H-bond status. T-R di †erence spectra between deoxyHb and HbCO reveal a positive Y7aº band at 1249 cm-1 and a negative band at 1263 cm-1. This result implies that acceptance by one or more Tyr residues, rather than donation by, an H-bond in the T state, and supports previous evidence that the T state H-bond partner of Tyr a42, the carboxylate side chain of Asp b99, is protonated in the T state. At 212 nm, the X-Pro amide II bands are clearly observed, and the position of the T-R di †erence band, 1464 cm-1, implies that one or more X-Pro carbonyls forms a stronger H-bond in the T state. This residue may be Pro a37, whose carbonyl interacts with a water molecule that in turn interacts with His b146 in the T state. The X-Pro di †erence signal may be an indicator of the His b146 protonation status, and therefore of an important contributor to the Bohr e †ect.