Visualization of coherent nuclear motion in a membrane protein by femtosecond spectroscopy
Article Abstract:
The nuclear dynamics of protein micromolecules helps them to adopt conformation varying in structures and properties. The dynamics occur in terms of the subpiosecond and piosecond time scale. The piosecond time scale indicates the role of low frequency (1 - 100 cm (super - 1) 0.05 x 10h (super 12) HZ) global protein motions. The calculation of global protein molecules is applicable in cases where electron transfer does not take place. This suggests that near-adiabetic electron transfer from a non-dephased multiple vibration level is more effective than in non-adiabatic transfers.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Coherent reaction dynamics in a bacterial cytochrome c oxidase
Article Abstract:
Biological reactions in protein complexes involve structural activities encompassing many degrees of time. A new study uses the bacterium Paracoccus denitrificans to study haem dynamics during the photo-initiated transfer of carbon monoxide from haem a3 to CuB by femtosecond spectroscopy. Results show evidence that coherent motions drive a reaction in a protein complex and suggest the importance of vibrational coherence operating on an ultrashort timescale.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Intraprotein radical transfer during photoactivation of DNA photolyase
Article Abstract:
It has been possible to reach a consistent mechanism for the radical transfer during photoactivation of photolyase in which sequential electron transfer among amino-acid residues produces transient cation radicals prior to charge neutralization by proton release to the solvent.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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