Literature DB >> 3390516

Time-resolved circular dichroism and absorption studies of the photolysis reaction of (carbonmonoxy)myoglobin.

S J Milder1, S C Bjorling, I D Kuntz, D S Kliger.   

Abstract

Time-resolved circular dichroism (TRCD) and absorption spectroscopy are used to follow the photolysis reaction of (carbonmonoxy)myoglobin (MbCO). Following the spectral changes associated with the initial loss of CO, a subtle change is observed in the visible absorption spectrum of the Mb product on a time scale of a few hundred nanoseconds. No changes are seen in the CD spectrum of Mb in the visible and near-UV regions subsequent to the loss of CO. The data suggest the existence of an intermediate found after ligand loss from MbCO that is similar in structure to the final Mb product.

Mesh:

Substances:

Year:  1988        PMID: 3390516      PMCID: PMC1330243          DOI: 10.1016/S0006-3495(88)83146-1

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


  18 in total

1.  Circular dichroism studies of myoglobin and leghemoglobin.

Authors:  N A Nicola; E Minasian; C A Appleby; S J Leach
Journal:  Biochemistry       Date:  1975-11-18       Impact factor: 3.162

2.  Mössbauer spectroscopic investigations of photodissociated myoglobin-CO at low temperatures.

Authors:  H E Marcolin; R Reschke; A Trautwein
Journal:  Eur J Biochem       Date:  1979-05-02

3.  Circular dichroism studies of myoglobin and cytochrome c derivatives.

Authors:  J Bolard; A Garnier
Journal:  Biochim Biophys Acta       Date:  1972-05-18

4.  Different dissociation pathways and observation of an excited deoxy state in picosecond photolysis of oxy- and carboxymyoglobin.

Authors:  P A Cornelius; A W Steele; D A Chernoff; R M Hochstrasser
Journal:  Proc Natl Acad Sci U S A       Date:  1981-12       Impact factor: 11.205

5.  Physical methods for the study of myoglobin.

Authors:  T M Rothgeb; F R Gurd
Journal:  Methods Enzymol       Date:  1978       Impact factor: 1.600

6.  Kinetics and temperature dependence of carboxymyoglobin ligand photodissociation.

Authors:  A H Reynolds; P M Rentzepis
Journal:  Biophys J       Date:  1982-04       Impact factor: 4.033

7.  Experimental errors and their effect on analyzing circular dichroism spectra of proteins.

Authors:  J P Hennessey; W C Johnson
Journal:  Anal Biochem       Date:  1982-09-01       Impact factor: 3.365

8.  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

9.  Low temperature photodissociation studies of ferrous hemoglobin and myoglobin complexes by Mössbauer spectroscopy.

Authors:  K Spartalian; G Lang; T Yonetani
Journal:  Biochim Biophys Acta       Date:  1976-04-23

10.  Time dependence of near-infrared spectra of photodissociated hemoglobin and myoglobin.

Authors:  M Sassaroli; D L Rousseau
Journal:  Biochemistry       Date:  1987-06-02       Impact factor: 3.162

View more
  3 in total

1.  Nanosecond time-resolved polarization spectroscopies: tools for probing protein reaction mechanisms.

Authors:  Eefei Chen; Robert A Goldbeck; David S Kliger
Journal:  Methods       Date:  2010-05-11       Impact factor: 3.608

2.  Nanosecond optical rotatory dispersion spectroscopy: application to photolyzed hemoglobin-CO kinetics.

Authors:  D B Shapiro; R A Goldbeck; D Che; R M Esquerra; S J Paquette; D S Kliger
Journal:  Biophys J       Date:  1995-01       Impact factor: 4.033

Review 3.  Probing kinetic mechanisms of protein function and folding with time-resolved natural and magnetic chiroptical spectroscopies.

Authors:  David S Kliger; Eefei Chen; Robert A Goldbeck
Journal:  Int J Mol Sci       Date:  2012-01-10       Impact factor: 6.208

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.