Bis-methionine ligation to heme iron in mutants of cytochrome b562. 1. Spectroscopic and electrochemical characterization of the electronic properties.
作者： Paul D. Barker , Edmund P. Nerou , Myles R. Cheesman , Andrew J. Thomson , Pedro de Oliveira
DOI: 10.1021/BI961127X
关键词:
摘要: We have generated mutants of cytochrome b562 in which the histidine ligand to heme iron (His102) has been replaced by a methionine. The resulting proteins can bis-methionine coordination iron, but stability this arrangement is dependent on oxidation state and solution pH. used optical, MCD, EPR spectroscopies study nature environment under variety conditions. Optical spectra reduced single variant, H102M, are consistent with ligation. In its oxidized state, protein high-spin all conditions studied, spectroscopic properties only one methionine ligands being coordinated. cannot identify what, if anything, provides other axial ligand. A double R98C/H102M (in covalently attached through c-type thioether linkage), also coordinated ferrous significantly different ...
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Ariki MATSUOKA, Nagao KOBAYASHI, Keiji SHIKAMA, The Soret magnetic circular dichroism of ferric high-spin myoglobins. A probe for the distal histidine residue. FEBS Journal. ,vol. 210, pp. 337- 341 ,(1992) , 10.1111/J.1432-1033.1992.TB17426.X
A. Dolla, L. Florens, P. Bianco, J. Haladjian, G. Voordouw, E. Forest, J. Wall, F. Guerlesquin, M. Bruschi, Characterization and oxidoreduction properties of cytochrome c3 after heme axial ligand replacements. Journal of Biological Chemistry. ,vol. 269, pp. 6340- 6346 ,(1994) , 10.1016/S0021-9258(17)37377-5
Eiji Itagaki, Lowell P. Hager, Studies on Cytochrome b562 of Escherichia coli I. PURIFICATION AND CRYSTALLIZATION OF CYTOCHROME b562 Journal of Biological Chemistry. ,vol. 241, pp. 3687- 3695 ,(1966) , 10.1016/S0021-9258(18)99827-3
I Mus-Veteau, A Dolla, F Guerlesquin, F Payan, M Czjzek, R Haser, P Bianco, J Haladjian, B.J. Rapp-Giles, J.D. Wall, Site-directed mutagenesis of tetraheme cytochrome c3. Modification of oxidoreduction potentials after heme axial ligand replacement. Journal of Biological Chemistry. ,vol. 267, pp. 16851- 16858 ,(1992) , 10.1016/S0021-9258(18)41862-5
M R Cheesman, N E le Brun, F H A Kadir, A J Thomson, G R Moore, S C Andrews, J R Guest, P M Harrison, J M A Smith, S J Yewdall, Haem and non-haem iron sites in Escherichia coli bacterioferritin: spectroscopic and model building studies Biochemical Journal. ,vol. 292, pp. 47- 56 ,(1993) , 10.1042/BJ2920047
Paul D. Barker, A. Grant Mauk, PH-linked conformational regulation of a metalloprotein oxidation-reduction equilibrium : electrochemical analysis of the alkaline form of cytochrome c Journal of the American Chemical Society. ,vol. 114, pp. 3619- 3624 ,(1992) , 10.1021/JA00036A006
R. S. Nicholson, Irving. Shain, Theory of Stationary Electrode Polarography. Single Scan and Cyclic Methods Applied to Reversible, Irreversible, and Kinetic Systems. Analytical Chemistry. ,vol. 36, pp. 706- 723 ,(1964) , 10.1021/AC60210A007
Hans Senn, Kurt Wüthrich, Conformation of the axially bound ligands of the heme iron and electronics structure of heme c in the cytochromes c-551 from pseudomonas mendocina and pseudomonas stutzeri and in cytochrome c2 from rhodospirillum rubrum Biochimica et Biophysica Acta. ,vol. 746, pp. 48- 60 ,(1983) , 10.1016/0167-4838(83)90009-2
Abel Schejter, Batya Plotkin, Ida Vig, The reactivity of cytochromecwith soft ligands FEBS Letters. ,vol. 280, pp. 199- 201 ,(1991) , 10.1016/0014-5793(91)80292-B
Juan C. Ferrer, J. Guy Guillemette, Ralf Bogumil, Stephen C. Inglis, Michael Smith, A. Grant Mauk, Identification of Lys79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c Journal of the American Chemical Society. ,vol. 115, pp. 7507- 7508 ,(1993) , 10.1021/JA00069A062