Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 116, Issue 13, Pages 4106-4114Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp300849y
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- Fondation pour la Recherche Medicale
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To study the ultrafast movement of the heme iron induced by nitric oxide (NO) binding to hemoglobin (Hb) and myoglobin (Mb), we probed the picosecond spectral evolution of absorption band III (similar to 760 nm) and vibrational modes (iron-histidine stretching, v(4) and v(7) in-plane modes) in time-resolved resonance Raman spectra. The time constants of band III intensity kinetics induced by NO rebinding (25 ps for hemoglobin and 40 ps for myoglobin) are larger than in Soret bands and Q bands. Band III intensity kinetics is retarded with respect to NO rebinding to Hb and to Mb. Similarly, the v((Fe-His)) stretching intensity kinetics are retarded with respect to the v(4) and v(7) heme modes and to Soret absorption. In contrast, band III spectral shift kinetics do not coincide with band III intensity kinetics but follows Soret kinetics. We concluded that, namely, the band III intensity depends on the heme iron out-of-plane position, as theoretically predicted (Stavrov, S. S. Biopolymers 2004, 74, 37-40).
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