Reductive nitrosylation of ferric cyanide horse heart myoglobin is limited by cyanide dissociation

Biochemical and Biophysical Research Communications

Volumn 393, Issue 2, 2010, Pages 196-200

  Ascenzi, Paolo ^a   di Masi, Alessandra ^a   Gullotta, Francesca ^a   Mattu, Marco ^a   Ciaccio, Chiara ^b,c   Coletta, Massimo ^b,c  

^a ROMA TRE UNIVERSITY   (Italy)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

^c Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems (CIRCMS   (Italy)

Author keywords

Ferric cyanide horse heart myoglobin; Kinetics; Nitrogen monoxide; Reductive nitrosylation

Indexed keywords

FERRICYANIDE; MYOGLOBIN;

ABSORPTION; ARTICLE; BINDING AFFINITY; DISSOCIATION; KINETICS; NITROSYLATION; PH; PRIORITY JOURNAL; REDUCTION; TEMPERATURE;

ANIMALS; FERRICYANIDES; HEMOGLOBINS; HORSES; METMYOGLOBIN; MYOCARDIUM; NITRIC OXIDE; OXIDATION-REDUCTION;

EQUIDAE;

EID: 77649190692     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.01.092     Document Type: Article

References (13)

1. Milani M., Ouellet Y., Ouellet H., Guertin M., Boffi A., Antonini G., Bocedi A., Mattu M., Bolognesi M., and Ascenzi P. Cyanide binding to truncated hemoglobins: a crystallographic and kinetic study. Biochemistry 43 (2004) 5213-5221
2. Bolli A., Ciaccio C., Coletta M., Nardini M., Bolognesi M., Pesce A., Guertin M., Visca P., and Ascenzi P. Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide: a comparative study. FEBS J. 275 (2008) 633-645
3. Antonini E., and Brunori M. Hemoglobin and Myoglobin in their Reactions with Ligands (1971), North-Holland Publishing Co., Amsterdam
4. Hoshino M., Ozawa K., Seki H., and Ford P.C. Photochemistry of nitric oxide adducts of water-soluble iron(III) porphyrin and ferrihemoproteins studied by nanosecond laser photolysis. J. Am. Chem. Soc. 115 (1993) 9568-9575
5. Hoshino M., Maeda M., Konishi R., Seki H., and Ford P.C. Studies on the reaction mechanism for reductive nitrosylation of ferrihemoproteins in buffer solutions. J. Am. Chem. Soc. 118 (1996) 5702-5707
6. Boffi A., Sarti P., Amiconi G., and Chiancone E. The interplay between heme iron and protein sulfhydryls in the reaction of dimeric Scapharca inaequivalvis hemoglobin with nitric oxide. Biophys. Chem. 98 (2002) 209-216
7. Herold S., Fago A., Weber R.E., Dewilde S., and Moens L. Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress. J. Biol. Chem. 279 (2004) 22841-22847
8. Herold S., and Puppo A. Kinetics and mechanistic studies of the reactions of metleghemoglobin, ferrylleghemoglobin, and nitrosylleghemoglobin with reactive nitrogen species. J. Biol. Inorg. Chem. 10 (2005) 946-957
9. Ascenzi P., Bocedi A., Antonini G., Bolognesi M., and Fasano M. Reductive nitrosylation and peroxynitrite-mediated oxidation of heme-hemopexin. FEBS J. 274 (2007) 551-562
10. Bateman H. Solution of a system of differential equations occurring in the theory of radio-active transformations. Proc. Cambridge Phyl. Soc. 15 (1910) 423-427
11. Cassoly R., and Gibson Q.H. Conformation, co-operativity and ligand binding in human hemoglobin. J. Mol. Biol. 91 (1975) 301-313
12. Brunori M., Coletta M., Ascenzi P., and Bolognesi M. Kinetic control of ligand binding processes in hemoproteins. J. Mol. Liquids 42 (1989) 175-193
13. Bellelli A., Antonini G., Brunori M., Springer B.A., and Sligar S.G. Transient spectroscopy of the reaction of cyanide with ferrous myoglobin. Effect of distal side residues. J. Biol. Chem. 265 (1990) 18898-18901