The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins(333 views) Merlino A, Vergara A, Sica F, Mazzarella L
Keywords: Bis-Histidine, Heme, Protein Data Bank, Structural Analyses,
Affiliations: *** IBB - CNR ***
Department of Chemistry, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cintia, I-80126 Naples, Italy
Institute of Biostructures and Bioimages, CNR, Via Mezzocannone 16, I-80134 Naples, Italy
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Ma, J. G., Laberge, M., Song, X. Z., Jentzen, W., Jia, S. L., Zhang, J., Vanderkooi, J. M., Shelnutt, J. A., Protein-induced changes in nonplanarity of the porphyrin in nickel cytochrome c probed by resonance Raman spectroscopy (1998) Biochemistry, 37, pp. 5118-5128
Menyhard, D. K., Keseru, G. M., Stereoelectronic control on the coordination of substrates to globin proteins. The role of proximal His93 on the NO release from myoglobin [10] (1998) J. Am. Chem. Soc., 120, pp. 7991-7992
Mitchell, D. T., Ernst, S. R., Wu, W., Hackert, M., Three-dimensional structure of a hemichrome hemoglobin from Caudina arenicola (1995) Acta Crystallogr. D, 51, pp. 647-653
Murzin, A. G., Brenner, S. E., Hubbard, T., Chothia, C., SCOP: a structural classification of proteins database for the investigation of sequences and structures (1995) J. Mol. Biol., 247, pp. 536-540
Rakic, A. A., Medakovic, V. B., Zaric, S. D., Orientations of axially coordinated imidazoles and pyridines in crystal structures of model systems of cytochromes (2006) J. Inorg. Biochem., 100, pp. 133-142
Reedy, C. J., Elvekrog, M. M., Gibney, B. R., Development of a heme protein structure-electrochemical function database (2008) Nucleic Acids Res., 36, pp. D307-D313
Rifkind, J. M., Abugo, O., Levy, A., Heim, J. M., Detection, formation, and relevance of hemichrome and hemochrome (1994) Methods Enzymol., 231, pp. 449-480
Robinson, V. L., Smith, B. B., Arnone, A., A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin (2003) Biochemistry, 42, pp. 10113-10125
Shelnutt, J. A., Rousseau, D. L., Dethmers, J. K., Margoliashi, E., Protein influence on the heme in cytochrome c: evidence from Raman difference spectroscopy (1979) Proc. Natl. Acad. Sci. U. S. A., 76, pp. 3865-3869
Walker, F. A., Magnetic spectroscopic (EPR, ESEEM, Mossbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins (1999) Coord. Chem. Rev., 186, pp. 471-534
Walker, F. A., Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes (2004) Chem. Rev., 104, pp. 589-615
Zaric, S. D., Popovic, D. M., Knapp, E. W., Factors determining the orientation of axially coordinated imidazoles in heme proteins (2001) Biochemistry, 40, pp. 7914-7928
The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins
The properties of hemoproteins strictly depend on the type and orientation of axial ligands. Here, the orientations of axially coordinated His in bis-His complexes and the heme geometry in protein data bank have been analyzed. The effect of the bis-histidyl formation on the heme cavity of Antarctic fish hemoglobins has been also evaluated. The results show that protein matrix exerts a major effect on the conformation of axially ligated histidines: the imidazoles in bis-His complexes occupy a preferred relative orientation in globins and in model systems, whereas they adopt a variety of relative orientations in other hemoproteins. The bis-histidyl adducts affect the heme geometry inducing larger distortions from planarity with respect to other ligands. These deviations are larger in bis-His multiheme cytochromes than in globins. In Antarctic fish hemoglobins the bis-histidyl adduct adopts preferentially a distorted coordination and the formation of the bis-His complex induces a slight but significant modification in the shape, area and volume of the heme cavity. (C) 2009 Elsevier B.V. All rights reserved.
The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins