Abstract
The energy hypersurface of the dominant tautomer states of mesoporphyrin-substituted horseradish peroxidase was determined by creation of a nonequilibrium population of these states through photochemical transformation at 5 K and measurement of the temperature changes of the respective spectral bands as they were warmed to room temperature.
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- Ansari A., Berendzen J., Bowne S. F., Frauenfelder H., Iben I. E., Sauke T. B., Shyamsunder E., Young R. D. Protein states and proteinquakes. Proc Natl Acad Sci U S A. 1985 Aug;82(15):5000–5004. doi: 10.1073/pnas.82.15.5000. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Berendzen J., Braunstein D. Temperature-derivative spectroscopy: a tool for protein dynamics. Proc Natl Acad Sci U S A. 1990 Jan;87(1):1–5. doi: 10.1073/pnas.87.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fidy J., Vanderkooi J. M., Zollfrank J., Friedrich J. More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. High resolution optical spectroscopic study. Biophys J. 1992 Feb;61(2):381–391. doi: 10.1016/S0006-3495(92)81844-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Frauenfelder H., Parak F., Young R. D. Conformational substates in proteins. Annu Rev Biophys Biophys Chem. 1988;17:451–479. doi: 10.1146/annurev.bb.17.060188.002315. [DOI] [PubMed] [Google Scholar]
- Frauenfelder H., Sligar S. G., Wolynes P. G. The energy landscapes and motions of proteins. Science. 1991 Dec 13;254(5038):1598–1603. doi: 10.1126/science.1749933. [DOI] [PubMed] [Google Scholar]
- Friedrich J., Gafert J., Zollfrank J., Vanderkooi J., Fidy J. Spectral hole burning and selection of conformational substates in chromoproteins. Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):1029–1033. doi: 10.1073/pnas.91.3.1029. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Köhler W, Friedrich J. Distribution of barrier heights in amorphous organic materials. Phys Rev Lett. 1987 Nov 9;59(19):2199–2202. doi: 10.1103/PhysRevLett.59.2199. [DOI] [PubMed] [Google Scholar]
- Köhler W, Friedrich J, Scheer H. Conformational barriers in low-temperature proteins and glasses. Phys Rev A Gen Phys. 1988 Jan 15;37(2):660–662. doi: 10.1103/physreva.37.660. [DOI] [PubMed] [Google Scholar]
- Köhler W, Zollfrank J, Friedrich J. Thermal irreversibility in optically labeled low-temperature glasses. Phys Rev B Condens Matter. 1989 Mar 15;39(8):5414–5424. doi: 10.1103/physrevb.39.5414. [DOI] [PubMed] [Google Scholar]
- Nienhaus G. U., Mourant J. R., Chu K., Frauenfelder H. Ligand binding to heme proteins: the effect of light on ligand binding in myoglobin. Biochemistry. 1994 Nov 15;33(45):13413–13430. doi: 10.1021/bi00249a030. [DOI] [PubMed] [Google Scholar]
- Powers L., Chance B., Chance M., Campbell B., Friedman J., Khalid S., Kumar C., Naqui A., Reddy K. S., Zhou Y. Kinetic, structural, and spectroscopic identification of geminate states of myoglobin: a ligand binding site on the reaction pathway. Biochemistry. 1987 Jul 28;26(15):4785–4796. doi: 10.1021/bi00389a028. [DOI] [PubMed] [Google Scholar]
- TEALE F. W. Cleavage of the haem-protein link by acid methylethylketone. Biochim Biophys Acta. 1959 Oct;35:543–543. doi: 10.1016/0006-3002(59)90407-x. [DOI] [PubMed] [Google Scholar]
- Teklu Y., Storm C. B. Nitrogen-hydrogen tautomerism in porphyrins and chlorins. J Am Chem Soc. 1972 Mar 8;94(5):1745–1746. doi: 10.1021/ja00760a056. [DOI] [PubMed] [Google Scholar]
- Vanderkooi J. M., Moy V. T., Maniara G., Koloczek H., Paul K. G. Site-selected fluorescence spectra of porphyrin derivatives of heme proteins. Biochemistry. 1985 Dec 31;24(27):7931–7935. doi: 10.1021/bi00348a013. [DOI] [PubMed] [Google Scholar]


