The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins (333 views)
Marine Genomics (ISSN: 1874-7787), 2009 Mar; 2(1): 51-56.
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Paper type: Journal Article,
Impact factor: 1.2, 5-year impact factor: 1.2
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-65549149904&partnerID=40&md5=9ce5a5ec8fe3ca397c930d9ecd0b7d74
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
References:
Arnold, E.V., Bohle, D.S., Jordan, P.A., Observation of myoglobin hemichromes (1999) Book of Abstracts, 217th ACS National Meeting, Anaheim, Calif., March 21-25, , INOR-39
Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., The Protein Data Bank (2000) Nucl. Ac. Res., 28, pp. 235-242
Burmester, T., Weich, B., Reinhardt, S., Hankeln, T., A vertebrate globin expressed in the brain (2000) Nature, 407, pp. 520-523
Burmester, T., Ebner, B., Weich, B., Hankeln, T., Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues (2002) Mol. Biol. Evol., 19, pp. 416-421
de Sanctis, D., Pesce, A., Nardini, M., Bolognesi, M., Bocedi, A., Ascenzi, P., Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family (2004) IUBMB Life, 56, pp. 643-651
Dokmanic, I., Sikic, M., Tomic, S., Metals in proteins: correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination (2008) Acta Crystallogr., D. Biol. Crystallogr., 64, pp. 257-263
Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., Liang, J., CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues (2006) Nucl. Ac. Res., pp. W116-W118
Feng, L., Zhou, S., Gu, L., Gell, D., Mackay, J., Weiss, M., Gow, A., Shi, Y., Structure of oxidized a-haemoglobin bound to AHSP reveals a protective mechanism for haem (2005) Nature (London), 435, pp. 697-701
Galstyan, A.S., Zaric, S.D., Knapp, E.W., Computational studies on imidazole heme conformations (2005) J. Biol. Inorg. Chem., 10, pp. 343-354
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
Merlino, A., Verde, C., di Prisco, G., Mazzarella, L., Vergara, A., Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase (2008) Spectroscopy, 22, pp. 143-152
Merlino, A., Vitagliano, L., Howes, B.D., Verde, C., di Prisco, G., Smulevich, G., Sica, F., Vergara, A., Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins (2009) Biopolymers, , Apr 16, Epub ahead of print, doi:10.1002/bip.21206
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
Pesce, A., De Sanctis, D., Nardini, M., Dewilde, S., Moens, L., Hankeln, T., Burmester, T., Bolognesi, M., Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin (2004) IUBMB Life, 56, pp. 657-664
Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., Bolognesi, T., Human brain neuroglobin three-dimensional structure (2003) Structure, 11, p. 1087
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
Reuss, S., Saaler-Reinhardt, S., Weich, B., Wystub, S., Reuss, M.H., Burmester, T., Hankeln, T., Expression analysis of neuroglobin mRNA in rodent tissues (2002) Neuroscience, 115, pp. 645-656
Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A., Mazzarella, L., The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (2002) Proc. Natl. Acad. Sci. U. S. A., 99, pp. 9801-9806
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
Vergara, A., Franzese, M., Merlino, A., Vitagliano, L., Verde, C., di Prisco, G., Lee, H.C., Mazzarella, L., Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder notothenioidei (2007) Biophys. J., 93, pp. 2822-2829
Vergara, A., Vitagliano, L., Verde, C., di Prisco, G., Mazzarella, L., Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins (2008) Methods Enzymol., 436, pp. 425-444
Vitagliano, L., Bonomi, G., Riccio, A., di Prisco, G., Smulevich, G., Mazzarella, L., The oxidation process of Antarctic fish hemoglobins (2004) Eur. J. Biochem., 271, pp. 1651-1659
Vitagliano, L., Vergara, A., Bonomi, G., Merlino, A., Verde, C., di Prisco, G., Howes, B.D., Mazzarella, L., Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (2008) J. Am. Chem. Soc., 130, pp. 10527-10535
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
Zhou, S., Olson, J.S., Fabian, M., Weiss, M.J., Gow, A.J., Biochemical fates of a hemoglobin bound to a hemoglobin-stabilizing protein AHSP (2006) J. Biol. Chem., 281, pp. 32611-32618
Arnold, E. V., Bohle, D. S., Jordan, P. A., Observation of myoglobin hemichromes (1999) Book of Abstracts, 217th ACS National Meeting, Anaheim, Calif., March 21-25, , INOR-39
Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., Bourne, P. E., The Protein Data Bank (2000) Nucl. Ac. Res., 28, pp. 235-242
Galstyan, A. S., Zaric, S. D., Knapp, E. W., Computational studies on imidazole heme conformations (2005) J. Biol. Inorg. Chem., 10, pp. 343-354
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
Marine Genomics (ISSN: 1874-7787), 2009 Mar; 2(1): 51-56.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.2, 5-year impact factor: 1.2
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-65549149904&partnerID=40&md5=9ce5a5ec8fe3ca397c930d9ecd0b7d74
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
References:
Arnold, E.V., Bohle, D.S., Jordan, P.A., Observation of myoglobin hemichromes (1999) Book of Abstracts, 217th ACS National Meeting, Anaheim, Calif., March 21-25, , INOR-39
Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., The Protein Data Bank (2000) Nucl. Ac. Res., 28, pp. 235-242
Burmester, T., Weich, B., Reinhardt, S., Hankeln, T., A vertebrate globin expressed in the brain (2000) Nature, 407, pp. 520-523
Burmester, T., Ebner, B., Weich, B., Hankeln, T., Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues (2002) Mol. Biol. Evol., 19, pp. 416-421
de Sanctis, D., Pesce, A., Nardini, M., Bolognesi, M., Bocedi, A., Ascenzi, P., Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family (2004) IUBMB Life, 56, pp. 643-651
Dokmanic, I., Sikic, M., Tomic, S., Metals in proteins: correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination (2008) Acta Crystallogr., D. Biol. Crystallogr., 64, pp. 257-263
Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., Liang, J., CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues (2006) Nucl. Ac. Res., pp. W116-W118
Feng, L., Zhou, S., Gu, L., Gell, D., Mackay, J., Weiss, M., Gow, A., Shi, Y., Structure of oxidized a-haemoglobin bound to AHSP reveals a protective mechanism for haem (2005) Nature (London), 435, pp. 697-701
Galstyan, A.S., Zaric, S.D., Knapp, E.W., Computational studies on imidazole heme conformations (2005) J. Biol. Inorg. Chem., 10, pp. 343-354
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
Merlino, A., Verde, C., di Prisco, G., Mazzarella, L., Vergara, A., Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase (2008) Spectroscopy, 22, pp. 143-152
Merlino, A., Vitagliano, L., Howes, B.D., Verde, C., di Prisco, G., Smulevich, G., Sica, F., Vergara, A., Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins (2009) Biopolymers, , Apr 16, Epub ahead of print, doi:10.1002/bip.21206
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
Pesce, A., De Sanctis, D., Nardini, M., Dewilde, S., Moens, L., Hankeln, T., Burmester, T., Bolognesi, M., Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin (2004) IUBMB Life, 56, pp. 657-664
Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., Bolognesi, T., Human brain neuroglobin three-dimensional structure (2003) Structure, 11, p. 1087
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
Reuss, S., Saaler-Reinhardt, S., Weich, B., Wystub, S., Reuss, M.H., Burmester, T., Hankeln, T., Expression analysis of neuroglobin mRNA in rodent tissues (2002) Neuroscience, 115, pp. 645-656
Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A., Mazzarella, L., The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (2002) Proc. Natl. Acad. Sci. U. S. A., 99, pp. 9801-9806
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
Vergara, A., Franzese, M., Merlino, A., Vitagliano, L., Verde, C., di Prisco, G., Lee, H.C., Mazzarella, L., Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder notothenioidei (2007) Biophys. J., 93, pp. 2822-2829
Vergara, A., Vitagliano, L., Verde, C., di Prisco, G., Mazzarella, L., Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins (2008) Methods Enzymol., 436, pp. 425-444
Vitagliano, L., Bonomi, G., Riccio, A., di Prisco, G., Smulevich, G., Mazzarella, L., The oxidation process of Antarctic fish hemoglobins (2004) Eur. J. Biochem., 271, pp. 1651-1659
Vitagliano, L., Vergara, A., Bonomi, G., Merlino, A., Verde, C., di Prisco, G., Howes, B.D., Mazzarella, L., Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (2008) J. Am. Chem. Soc., 130, pp. 10527-10535
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
Zhou, S., Olson, J.S., Fabian, M., Weiss, M.J., Gow, A.J., Biochemical fates of a hemoglobin bound to a hemoglobin-stabilizing protein AHSP (2006) J. Biol. Chem., 281, pp. 32611-32618
Arnold, E. V., Bohle, D. S., Jordan, P. A., Observation of myoglobin hemichromes (1999) Book of Abstracts, 217th ACS National Meeting, Anaheim, Calif., March 21-25, , INOR-39
Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., Bourne, P. E., The Protein Data Bank (2000) Nucl. Ac. Res., 28, pp. 235-242
Galstyan, A. S., Zaric, S. D., Knapp, E. W., Computational studies on imidazole heme conformations (2005) J. Biol. Inorg. Chem., 10, pp. 343-354
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 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
| ▼ The fine structure of proteins as a new tool for protein structure validation, quality assessment, and prediction |
The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins
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Verde C, Giordano D, Russo R, Riccio A, Vergara A, Mazzarella L, Di Prisco G
* Hemoproteins in the cold (276 views)
Marine Genomics (ISSN: 1874-7787), 2009 Mar; 2(1): 67-73.
Impact Factor: 1.2
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De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (486 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
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* Biochemical, structural, and computational studies of a γ-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei (10 views)
Comput Struct Biotechnol J (ISSN: 2001-0370linking), 2022 Jul 27; 20: 4185-4194.
Impact Factor: 6.155
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Alterio V, Langella E, Buonanno M, Esposito D, Nocentini A, Berrino E, Bua S, Polentarutti M, Supuran CT, Monti SM, De Simone G
* Zeta-carbonic anhydrases show CS(2) hydrolase activity: A new metabolic carbon acquisition pathway in diatoms? (26 views)
Comput Struct Biotechnol J (ISSN: 2001-0370linking), 2021 Jun 5; 19: 3427-3436.
Impact Factor: 7.271
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Cozzolino S, Balasco N, Vigorita M, Ruggiero A, Smaldone G, Del Vecchio P, Vitagliano L, Graziano G
* Guanidinium binding to proteins: The intriguing effects on the D1 and D2 domains of Thermotoga maritima Arginine Binding Protein and a comprehensive analysis of the Protein Data Bank (66 views)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2020 Nov 15; 163: 375-385.
Impact Factor: 5.162
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Buonanno M, Di Fiore A, Langella E, D’ambrosio K, Supuran CT, Monti SM, De Simone G
* The Crystal Structure of a hCA VII Variant Provides Insights into the Molecular Determinants Responsible for Its Catalytic Behavior (304 views)
Int J Mol Sc (ISSN: 1661-6596, 1422-0067, 1422-0067electronic), 2018 May; 19(6): 19-24.
Impact Factor: 3.687
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Kamnev AA, Tugarova AV, Dyatlova YA, Tarantilis PA, Grigoryeva OP, Fainleib AM, De Luca S
* Methodological effects in Fourier transform infrared (FTIR) spectroscopy: Implications for structural analyses of biomacromolecular samples (220 views)
Spectrochim Acta A (ISSN: 1386-1425, 1386-1425linking), 2017 Dec 17; 193: 558-564.
Impact Factor: 2.88
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Berisio R, Vitagliano L
* Polyproline and triple helix motifs in Host-Pathogen recognition (765 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 855-865.
Impact Factor: 2.326
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Verde C, Giordano D, Russo R, Riccio A, Vergara A, Mazzarella L, Di Prisco G
* Hemoproteins in the cold (276 views)
Marine Genomics (ISSN: 1874-7787), 2009 Mar; 2(1): 67-73.
Impact Factor: 1.2
View Export to BibTeX Export to EndNote
De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (486 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
View Export to BibTeX Export to EndNote
8 Records (8 excluding Abstracts).
Total impact factor: 30.482 (30.482 excluding Abstracts).
Total 5 year impact factor: 14.478 (14.478 excluding Abstracts).
Total impact factor: 30.482 (30.482 excluding Abstracts).
Total 5 year impact factor: 14.478 (14.478 excluding Abstracts).
333 views. Last view on Saturday 03 June 2023, 20:02:46
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