Multiply Excited Vibration of Carbon Monoxide in the Primary Docking Site of Hemoglobin Following Photolysis from the Heme-Reference-Cited by-同舟云学术

Multiply Excited Vibration of Carbon Monoxide in the Primary Docking Site of Hemoglobin Following Photolysis from the Heme

Published:2010-06-21 Issue:14 Volume:1 Page:2077-2081
ISSN:1948-7185
Container-title:The Journal of Physical Chemistry Letters
language:en
Short-container-title:J. Phys. Chem. Lett.

Author:

Nuernberger Patrick¹,Lee Kevin F.¹,Bonvalet Adeline¹,Vos Marten H.¹,Joffre Manuel¹

Affiliation:

1. Laboratoire d’Optique et Biosciences, Ecole Polytechnique, Centre National de la Recherche Scientifique, 91128 Palaiseau, France, and Institut National de la Santé et de la Recherche Médicale, U696, 91128 Palaiseau, France

Publisher

American Chemical Society (ACS)

Subject

General Materials Science,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jz1006324

Reference34 articles.

1. Direct observations of ligand dynamics in hemoglobin by subpicosecond infrared spectroscopy.

2. Mid‐infrared vibrational spectrum of CO after photodissociation from heme: Evidence for a ligand docking site in the heme pocket of hemoglobin and myoglobin

3. Binding of CO to Myoglobin from a Heme Pocket Docking Site to Form Nearly Linear Fe-C-O

4. The Orientation of CO in Heme Proteins Determined by Time-Resolved Mid-IR Spectroscopy: Anisotropy Correction for Finite Photolysis of an Optically Thick Sample

5. Orientational Distribution of CO before and after Photolysis of MbCO and HbCO: A Determination Using Time-Resolved Polarized Mid-IR Spectroscopy

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