Literature DB >> 2285804

A photoacoustic calorimetric study of horse myoglobin.

J A Westrick1, K S Peters.   

Abstract

The dynamics of the enthalpy and volume changes for the photodissociation of CO from horse myoglobin has been studied by time-resolved photoacoustic calorimetry which measures the dynamics of enthalpy and volume changes on the nanosecond time scale. The role of the Lys 45 salt bridge in the ligand dissociation is discussed.

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Year:  1990        PMID： 2285804     DOI： 10.1016/0301-4622(90)88008-g

Source DB:  PubMed          Journal:  Biophys Chem        ISSN： 0301-4622            Impact factor:   2.352


  5 in total

1.  Diffractive optics-based heterodyne-detected four-wave mixing signals of protein motion: from "protein quakes" to ligand escape for myoglobin.

Authors:  G Dadusc; J P Ogilvie; P Schulenberg; U Marvet; R J Miller
Journal:  Proc Natl Acad Sci U S A       Date:  2001-05-08       Impact factor: 11.205

2.  Volume and enthalpy profiles of CO rebinding to horse heart myoglobin.

Authors:  Jaroslava Miksovská; Jason H Day; Randy W Larsen
Journal:  J Biol Inorg Chem       Date:  2003-05-06       Impact factor: 3.358

3.  The efficiency of malachite green, free and protein bound, as a photon-to-heat converter.

Authors:  G L Indig; D G Jay; J J Grabowski
Journal:  Biophys J       Date:  1992-03       Impact factor: 4.033

4.  Submillisecond conformational changes in proteins resolved by photothermal beam deflection.

Authors:  Walter G Gonzalez; Jaroslava Miksovska
Journal:  J Vis Exp       Date:  2014-02-18       Impact factor: 1.355

5.  A photoacoustic calorimetry study of horse carboxymyoglobin on the 10-nanosecond time scale.

Authors:  C L Norris; K S Peters
Journal:  Biophys J       Date:  1993-10       Impact factor: 4.033
  5 in total

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