Literature DB >> 2317555

Ligand dynamics in the photodissociation of carboxyhemoglobin by subpicosecond transient infrared spectroscopy.

L Rothberg1, T M Jedju, R H Austin.   

Abstract

Time-resolved infrared spectroscopy with 0.5-ps resolution is used to track the evolution of the CO stretching vibration after visible photoexcitation of carboxyhemoglobin in water at room temperature. Polarization measurements determine that the iron-complexed CO is oriented nearly perpendicular to the porphyrin plane. The dissociation appears to proceed via a metastable excited state with 2 +/- 1 ps lifetime. The dissociated CO binds weakly in the heme pocket for at least 500 ps. This state correlates with the internally bound state observed by Frauenfelder et al. at low temperatures in myoglobin.

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Year:  1990        PMID： 2317555      PMCID： PMC1280677          DOI： 10.1016/S0006-3495(90)82538-8

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


  19 in total

1.  Time-resolved spectroscopy of hemoglobin and its complexes with subpicosecond optical pulses.

Authors:  C V Shank; E P Ippen; R Bersohn
Journal:  Science       Date:  1976-07-02       Impact factor: 47.728

Review 2.  Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron.

Authors:  M F Perutz
Journal:  Annu Rev Biochem       Date:  1979       Impact factor: 23.643

3.  Dynamics of ligand binding to heme proteins.

Authors:  D A Case; M Karplus
Journal:  J Mol Biol       Date:  1979-08-15       Impact factor: 5.469

4.  Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation.

Authors:  B I Greene; R M Hochstrasser; R B Weisman; W A Eaton
Journal:  Proc Natl Acad Sci U S A       Date:  1978-11       Impact factor: 11.205

5.  Mechanisms for excited state relaxation and dissociation of oxymyoglobin and carboxymyoglobin.

Authors:  A H Reynolds; S D Rand; P M Rentzepis
Journal:  Proc Natl Acad Sci U S A       Date:  1981-04       Impact factor: 11.205

6.  Geminate recombination of O2 and hemoglobin.

Authors:  D A Chernoff; R M Hochstrasser; A W Steele
Journal:  Proc Natl Acad Sci U S A       Date:  1980-10       Impact factor: 11.205

7.  The structure of human carbonmonoxy haemoglobin at 2.7 A resolution.

Authors:  J M Baldwin
Journal:  J Mol Biol       Date:  1980-01-15       Impact factor: 5.469

8.  An x-ray study of azide methaemoglobin.

Authors:  M F Perutz; F S Mathews
Journal:  J Mol Biol       Date:  1966-10-28       Impact factor: 5.469

9.  Dynamics of ligand binding to myoglobin.

Authors:  R H Austin; K W Beeson; L Eisenstein; H Frauenfelder; I C Gunsalus
Journal:  Biochemistry       Date:  1975-12-02       Impact factor: 3.162

10.  Photophysics and reactivity of heme proteins: a femtosecond absorption study of hemoglobin, myoglobin, and protoheme.

Authors:  J W Petrich; C Poyart; J L Martin
Journal:  Biochemistry       Date:  1988-05-31       Impact factor: 3.162
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  2 in total

1.  Metastable CO binding sites in the photoproduct of a novel cooperative dimeric hemoglobin.

Authors:  S Song; L Rothberg; D L Rousseau; A Boffi; E Chiancone
Journal:  Biophys J       Date:  1993-11       Impact factor: 4.033

2.  A novel method to stabilize meat colour: ligand coordinating with hemin.

Authors:  Cunliu Zhou; Shengjiang Tan; Jun Li; Xiaoyan Chu; Kezhou Cai
Journal:  J Food Sci Technol       Date:  2012-01-31       Impact factor: 2.701
  2 in total

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