A novel microperoxidase activity: Methyl viologen-linked nitrite reducing activity of microperoxidase

Biochemical and Biophysical Research Communications

Volumn 315, Issue 4, 2004, Pages 815-822

  Suruga, Kohei ^a   Murakami, Kiriko ^a   Taniyama, Yohei ^a   Hama, Toshiyuki ^a   Chida, Hirotaka ^a   Satoh, Tadashi ^b   Yamada, Seiji ^c   Hakamata, Wataru ^d   Kawachi, Ryu ^a   Isogai, Yasuhiro ^e   Nishio, Toshiyuki ^a   Oku, Tadatake ^a  

^a NIHON UNIVERSITY   (Japan)

^b INSTITUTE OF MATERIALS STRUCTURE SCIENCE   (Japan)

^c RIKEN HARIMA INSTITUTE   (Japan)

^d NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

^e RIKEN   (Japan)

Author keywords

Cytochrome c; Hemoprotein; Microperoxidase; Nitrite reducing activity; Peptide chain

Indexed keywords

PEROXIDASE;

ARTICLE; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTON TRANSPORT;

EQUIDAE; ESCHERICHIA COLI;

EID: 10744230570     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.01.133     Document Type: Article

References (39)

1. Matsubara T. Studies on denitrication. XII. Gas production from amines and nitrite. J. Biochem. (Tokyo). 67:1970;229-235.
2. Alefounder P.R., Ferguson S.J. The location of dissimilatory nitrite reductase and the control of dissimilatory nitrate reductase by oxygen in Paracoccus denitrificans. Biochem. J. 192:1980;231-240.
3. Lazzarini R.A., Atkinson D.E. A triphospyridine nucleotide-specific nitrite reductase from Escherichia coli. J. Biol. Chem. 256:1961;9711-9717.
4. Ida S., Morita Y. Purification and general properties of spinach leaf nitrite reductase. Plant Cell Physiol. 14:1973;661-671.
5. Eisle O., Messerschmidt A., Stach P., Bourenkov G.P., Bartunik H.D., Huber R., Kroneck P.M.H. Structure of cytochrome. c nitrite reductase Nature. 400:1999;476-480.
6. Santucci R., Picciau A., Antonini G., Campanella L. A complex of microperoxidase with a synthetic peptide: structure and functional characterization. Biochim. Biophys. Acta. 1250:1995;183-188.
7. Laberge M., Vreugdenhil A.J., Butler I.S. Microperoxidase-11: molecular dynamics and Q-band excited resonance Raman of the oxidized, reduced and carbonyl forms. J. Biomol. Struct. Dyn. 15:1998;1039-1050.
8. Sharma V.S., Renney H.M., Geibel J.F., Traylor T.G. A new for the determination of ligand dissociation rate constant of carboxyhemoglobin. Biochem. Biophys. Res. Commun. 66:1975;1301-1306.
9. Sharma V.S., Schmidt M.R., Ranney H.M. Dissociation of CO from carboxyhemoglobin. J. Biol. Chem. 251:1976;4267-4272.
10. Ricoux R., Boucher J.L., Mansuy D., Mehy J.P. Formation of iron (II)-nitrosoalkane complex: a new activity of microperoxidase 8. Biochem. Biophys. Res. Commun. 278:2000;217-223.
11. Plattner H., Wachter E., Grobner P. A heme-nonapeptide tracer for electron microscopy. Histochemistry. 53:1977;223-242.
12. 6 from the red alga Porphyra yezoensis at 1.57 Å resolution Acta Cryst. D. 56:2000;1577-1578.
13. Satoh T., Itoga A., Isogai Y., Kurihara M., Yamada S., Natori M., Suzuki N., Suruga K., Kawachi R., Arahira M., Nishio T., Fukazawa C., Oku T. Increasing the conformational stability by replacement of heme axial ligand in. c -type cytochrome FEBS Lett. 531:2002;543-547.
14. Yamada S., Suruga K., Ogawa M., Hama T., Satoh T., Kawachi R., Nishio T., Oku T. Appearance of nitrite reducing activity of cytochrome. c upon heat denaturation Biosci. Biotechnol. Biochem. 66(10):2002;2044-2051.
15. Cheek J., Low D.W., Gray H.B., Dawson J.H. Histidine-tailed microperoxidase-10: a pH-dependent ligand switch. Biochem. Biophys. Res. Commun. 253:1998;195-198.
16. Hoshino M., Kawata Y., Goto Y. Interaction of GroEL with conformational states of horse heart cytochrome. c J. Mol. Biol. 262:1996;575-587.
17. Vega J.M., Cardenas J., Losada M. Ferredoxin-nitrite reductase. Methods Enzymol. 69:1980;255-270.
18. Ramirez J., Campo F.F.D., Paneque A., Losada M. Ferredoxin-nitrite reductase from spinach. Biochim. Biophys. Acta. 118:1966;58-71.
19. Scheiner D. Determination of ammonia and Kjeldahl nitrogen by indophenol method. Water Res. 10:1976;31-36.
20. Drabkin D.L. Spectrophotometric studies. J. Biol. Chem. 146:1942;605-617.
21. Pace C.N., Shirly B.A., Thompson J.A. Protein Structure: A Practical Approach. 1989;IRL, Oxford. pp. 311-330.
22. 6 from two strains of the green alga Chlorella vulgaris Biosci. Biotechnol. Biochem. 64:2000;628-632.
23. Duton P.L. Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54:1978;411-435.
24. + reductase. J. Biochem. (Tokyo). 83:1978;357-361.
25. Wallace J.M., Cardenes I. Functional role of heme ligation in cytochrome. c J. Biol. Chem. 267:1992;3852-3861.
26. Bushnell G.W., Louie G.V., Brayer G.D. High-resolution three-dimensional structure of horse heart cytochrome. c J. Mol. Biol. 20:1990;585-595.
27. Santucci R., Fiorucci L., Sinibaldi F., Polizio F., Desideri A., Ascoli F. The heme-containing N-fragment (residues 1-56) of cytochrome. c is a bis-histidine functional system Arch. Biochem. Biophys. 379:2000;331-336.
28. Iizuka T., Yonetani T. Spin changes in hemoproteins. Adv. Biophys. 1:1970;157-182.
29. Marques H.M., Perry C.B. Hemepeptide models for hemoproteins: the behavior of. N -acetylmicroperoxidase-11 in aqueous solution J. Inorg. Biochem. 75:1999;281-291.
30. Battistuzzi G., Borsari M., Cowan J.A., Ranieri A., Sola M. Control of cytochrome. c redox potential: axial ligation and protein environment effects J. Am. Chem. Soc. 124:2002;5315-5324.
31. Huang W., Zheling Z., Han X., Tang J., Peng Z., Dong S., Wang E. Electrochemistry and spectroscopy study on the interaction of microperoxidase-11 with lipid membrane. Biophys. Chem. 94:2001;165-173.
32. Margoliash E., Smith E., Kreil G., Tuppy H. The complete amino-acid sequence. Nature. 192:1961;1125-1127.
33. Cornelius P.A., Steele A.W., Chernoff D.A., Hochstrasser R.M. Different dissociation pathways and observation of an excited deoxy state in picosecond photolysis of oxy-and carboxymyoglobin. Proc. Natl. Acad. Sci. USA. 78:1981;7526-7529.
34. Ho C.-H., Tamura G. Purification and properties of nitrite reductase from spinach leaves. Agric. Biol. Chem. 37:1973;37-44.
35. Guerreo M.G., Vega J.M., Losada M. The assimilatory nitrite-reducing system and its regulation. Ann. Rev. Plant Physiol. 32:1981;169-204.
36. Kemp J.D., Atkinson D.E. Nitrite reductase of Escherichia coli specific for reduced nicotinamide adenine dinucleotide. J. Bacteriol. 92:1966;628-634.
37. Hirasawasoga M., Horie S., Tamura G. Further characterization of ferredoxin nitrite reductase and the relationship between the enzyme and methyl viologen-dependent nitrite reductase. Agric. Biol. Chem. 46:1982;1319-1328.
38. Vega J.M., Kamin H. Spinach nitrite reductase. J. Biol. Chem. 252:1977;896-909.
39. Zumft W.G. Ferredoxin: nitrite oxidoreductase from Chlorella purification and properties. Biochim. Biophys. Acta. 1040:1990;237-244.