%0 Journal Article %1 WOS:000460591600003 %A de Souza, Ticyano P %A Abreu, Dieric S %A Carepo, Marta S P %A Silva, Maria A S %A Zampieri, Davila %A Eberlin, Marcos N %A Paulo, Tercio F %A Sousa, Eduardo H S %A Longhinotti, Elisane %A Diogenes, Izaura C N %C 233 SPRING ST, NEW YORK, NY 10013 USA %D 2019 %I SPRINGER %J JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY %K Modified Myoglobin; Snake Surface electrode; plasmon resonance} venom; {Electrochemistry; %N 2 %P 171-178 %R 10.1007/s00775-019-01636-7 %T Effect of Crotalus basiliscus snake venom on the redox reaction of myoglobin %V 24 %X In this work, we have studied the effect of Crotalus basiliscus snake venom on the redox reaction of myoglobin (Mb), and by means of electrochemical techniques, we have shown that this reaction is undoubtedly affected following the interaction with the venom. Surface plasmon resonance, electrophoresis, UV-Vis, and circular dichroism showed that the interaction involves the attachment of some constituent of the venom to the protein, although not affecting its first and secondary structures. Mass spectra support this suggestion by showing the appearance of signals assigned to the Mb dimer and to a new species resulting from the interaction between Mb and the venom proteins. In addition, the mass spectra suggest the aromatic amino acids of myoglobin, mainly tryptophan and phenylalanine, are more exposed to the solvent medium upon the exposure to the venom solution. The results altogether indicate that the harmful effects of the venom of Crotalus basiliscus snake are likely connected to the blocking of the redox site of Mb.

@article{WOS:000460591600003, abstract = {In this work, we have studied the effect of Crotalus basiliscus snake venom on the redox reaction of myoglobin (Mb), and by means of electrochemical techniques, we have shown that this reaction is undoubtedly affected following the interaction with the venom. Surface plasmon resonance, electrophoresis, UV-Vis, and circular dichroism showed that the interaction involves the attachment of some constituent of the venom to the protein, although not affecting its first and secondary structures. Mass spectra support this suggestion by showing the appearance of signals assigned to the Mb dimer and to a new species resulting from the interaction between Mb and the venom proteins. In addition, the mass spectra suggest the aromatic amino acids of myoglobin, mainly tryptophan and phenylalanine, are more exposed to the solvent medium upon the exposure to the venom solution. The results altogether indicate that the harmful effects of the venom of Crotalus basiliscus snake are likely connected to the blocking of the redox site of Mb.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {233 SPRING ST, NEW YORK, NY 10013 USA}, author = {de Souza, Ticyano P and Abreu, Dieric S and Carepo, Marta S P and Silva, Maria A S and Zampieri, Davila and Eberlin, Marcos N and Paulo, Tercio F and Sousa, Eduardo H S and Longhinotti, Elisane and Diogenes, Izaura C N}, biburl = {https://www.bibsonomy.org/bibtex/2dbc473a553bb62855e307e5bfb864e01/ppgfis_ufc_br}, doi = {10.1007/s00775-019-01636-7}, interhash = {2ba085bbe8d1d950878c8f3d897764b6}, intrahash = {dbc473a553bb62855e307e5bfb864e01}, issn = {0949-8257}, journal = {JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY}, keywords = {Modified Myoglobin; Snake Surface electrode; plasmon resonance} venom; {Electrochemistry;}, number = 2, pages = {171-178}, publisher = {SPRINGER}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Effect of Crotalus basiliscus snake venom on the redox reaction of myoglobin}, tppubtype = {article}, volume = 24, year = 2019 }