Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin
- PMID: 3207839
- PMCID: PMC1330353
- DOI: 10.1016/S0006-3495(88)82987-4
Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin
Abstract
The optical transient absorption spectra at 30 ps and 6.5 ns after photolysis are compared for both carboxy hemoglobin (HbCO) and carboxy myoglobin (MbCO). Both 355- and 532-nm excitation pulses were used. In all cases the shapes of the optical difference spectra thus generated are stationary over the complete time-scale studied. The photolysis spectra for MbCO are not significantly different from the equilibrium difference spectra generated on the same picosecond spectrometer when measured to an accuracy of +/- 0.5 nm. In addition, spectral parameters for delegated HbCO generated on the same spectrometer but detected by two different techniques, either by a Vidicon detector or point by point with photomultiplier tubes, are reported; the results are different from some of the previously reported picosecond experiments.
Similar articles
-
Different dissociation pathways and observation of an excited deoxy state in picosecond photolysis of oxy- and carboxymyoglobin.Proc Natl Acad Sci U S A. 1981 Dec;78(12):7526-9. doi: 10.1073/pnas.78.12.7526. Proc Natl Acad Sci U S A. 1981. PMID: 6950394 Free PMC article.
-
Transient and time-resolved optical studies of photolyzed carbonmonoxy hemoglobin and myoglobin.Photochem Photobiol. 1990 Jun;51(6):741-8. Photochem Photobiol. 1990. PMID: 2195562 Review. No abstract available.
-
Different relaxations in myoglobin after photolysis.Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14402-7. doi: 10.1073/pnas.0406062101. Epub 2004 Sep 22. Proc Natl Acad Sci U S A. 2004. PMID: 15385677 Free PMC article.
-
Picosecond resonance Raman evidence for unrelaxed heme in the (carbonmonoxy)myoglobin photoproduct.Biochemistry. 1985 Sep 24;24(20):5295-7. doi: 10.1021/bi00341a003. Biochemistry. 1985. PMID: 4074696
-
Time dependence of near-infrared spectra of photodissociated hemoglobin and myoglobin.Biochemistry. 1987 Jun 2;26(11):3092-8. doi: 10.1021/bi00385a022. Biochemistry. 1987. PMID: 3607013
Cited by
-
Subpicosecond resonance Raman spectroscopy of carbonmonoxy- and oxyhemoglobin.Biophys J. 1990 Oct;58(4):931-7. doi: 10.1016/S0006-3495(90)82437-1. Biophys J. 1990. PMID: 2248996 Free PMC article.
-
Reactions of excited triplet states of metal substituted myoglobin with dioxygen and quinone.Biophys J. 1990 Jul;58(1):177-86. doi: 10.1016/S0006-3495(90)82363-8. Biophys J. 1990. PMID: 2383630 Free PMC article.
-
Internal water and microsecond dynamics in myoglobin.J Phys Chem B. 2013 Nov 27;117(47):14676-87. doi: 10.1021/jp409234g. Epub 2013 Nov 19. J Phys Chem B. 2013. PMID: 24195787 Free PMC article.
-
Dynamics of proteins encapsulated in silica sol-gel glasses studied with IR vibrational echo spectroscopy.J Am Chem Soc. 2006 Mar 29;128(12):3990-7. doi: 10.1021/ja058745y. J Am Chem Soc. 2006. PMID: 16551107 Free PMC article.
-
Dynamics of hemoglobin in human erythrocytes and in solution: influence of viscosity studied by ultrafast vibrational echo experiments.J Am Chem Soc. 2004 Dec 8;126(48):15702-10. doi: 10.1021/ja0454790. J Am Chem Soc. 2004. PMID: 15571392 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Miscellaneous