Biochemical and Cellular Investigation of Vitreoscilla Hemoglobin (VHb) Variants Possessing Efficient Peroxidase Activity |
Isarankura-Na-Ayudhya, Chartchalerm
(Department of Clinical Microbiology, Faculty of Medical Technology, Mahidol University)
Tansila, Natta (Department of Clinical Microbiology, Faculty of Medical Technology, Mahidol University) Worachartcheewan, Apilak (Department of Clinical Microbiology, Faculty of Medical Technology, Mahidol University) Bulow, Leif (Department of Pure and Applied Biochemistry, Center for Chemistry and Chemical Engineering, Lund University) Prachayasittikul, Virapong (Department of Clinical Microbiology, Faculty of Medical Technology, Mahidol University) |
1 | Kvist, M., E. S. Ryabova, E. Nordlander, and L. Bulow. 2007. An investigation of the peroxidase activity of Vitreoscilla hemoglobin. J. Biol. Inorg. Chem. 12: 324-334. DOI ScienceOn |
2 | Yang, G., R. Yuan, and Y. Q. Chai. 2008. A high-sensitive amperometric hydrogen peroxide biosensor based on the immobilization of hemoglobin on gold colloid/L-cysteine/gold colloid/nanoparticles Pt-chitosan composite film-modified platinum disk electrode. Colloids Surf. B Biointerfaces 61: 93-100. DOI ScienceOn |
3 | Adams, P. A. 1990. The peroxidasic activity of the haem octapeptide microperoxidase-8(MP-8): The kinetic mechanism of the catalytic reduction of by MP-8 using 2,2-azinobis-(3-ethylbenzothiazoline-6-sulphonate) (ABTS) as reducing substrate. J. Chem. Soc. Perkin Trans. 2: 1407-1414. |
4 | Allocatelli, C. T., F. Cutruzzola, A. Brancaccio, M. Brunori, J. Qin, and G. N. La Mar. 1993. Structural and functional characterization of sperm whale myoglobin mutants: Role of arginine (E10) in ligand stabilization. Biochemistry 32: 6041-6049. DOI ScienceOn |
5 | Bauer, F. and H. Sticht. 2007. A proline to glycine mutation in the Lck SH3-domain affects conformational sampling and increases ligand binding affinity. FEBS Lett. 581: 1555-1560. DOI ScienceOn |
6 | Geckil, H., S. Gencer, H. Kahraman, and S. O. Erenler. 2003. Genetic engineering of Enterobacter aerogenes with the Vitreoscilla hemoglobin gene: Cell growth, survival, and antioxidant enzyme status under oxidative stress. Res. Microbiol. 154: 425-431. DOI ScienceOn |
7 | Nagababu, E., F. J. Chrest, and J. M. Rifkind. 2003. Hydrogenperoxide-induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase. Biochim. Biophys. Acta 1620: 211-217. DOI ScienceOn |
8 | George, P. 1953. The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. I. Titration with reducing agents. Biochem. J. 54: 267-276. |
9 | Liu, C. Y. and D. A. Webster. 1974. Spectral characteristics and interconversions of the reduced oxidized and oxygenated forms of purified cytochrome o. J. Biol. Chem. 249: 4261-4266. |
10 | Miessler, G. L. and D. A. Tarr. 2004. Inorganic Chemistry, 3rd Ed. Prentice Hall, Upper Saddle River, New Jersey. |
11 | Rodriguez-Lopez, J. N., A. T. Smith, and R. N. Thorneley. 1996. Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis. J. Biol. Chem. 271: 4023-4030. DOI |
12 | Roos, V., C. I. Andersson, C. Arfvidsson, K. G. Wahlund, and L. Bulow. 2002. Expression of double Vitreoscilla hemoglobin enhances growth and alters ribosome and tRNA levels in Escherichia coli. Biotechnol. Prog. 18: 652-656. DOI ScienceOn |
13 | Wakabayashi, S., H. Matsubara, and D. A. Webster. 1986. Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla. Nature 322: 481-483. DOI ScienceOn |
14 | Zhang, K., L. Mao, and R. Cai. 2000. Stopped-flow spectrophotometric determination of hydrogen peroxide with hemoglobin as catalyst. Talanta 51: 179-186. DOI ScienceOn |
15 | Nagababu, E. and J. M. Rifkind. 2000. Heme degradation during autoxidation of oxyhemoglobin. Biochem. Biophys. Res. Commun. 273: 839-845. DOI ScienceOn |
16 | Delano, W. L. 1998. The PyMOL Molecular Graphic System. Delano Scientific LLC, San Carlos, CA (http://www.pymol.org). |
17 | Berglund, G. I., G. H. Carlsson, A. T. Smith, H. Szoke, A. Henriksen, and J. Hajdu. 2002. The catalytic pathway of horseradish peroxidase at high resolution. Nature 417: 463-468. DOI ScienceOn |
18 | Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254. DOI ScienceOn |
19 | Fan, C., J. Zhong, R. Guan, and G. Li. 2003. Direct electrochemical characterization of Vitreoscilla sp. hemoglobin entrapped in organic films. Biochim. Biophys. Acta 1649: 123-126. DOI ScienceOn |
20 | Zhang, L., Y. Li, Z. Wang, Y. Xia, W. Chen, and K. Tang. 2007. Recent developments and future prospects of Vitreoscilla hemoglobin application in metabolic engineering. Biotechnol. Adv. 25: 123-136. DOI ScienceOn |
21 | Khosla, C. and J. E. Bailey. 1988. Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli. Nature 331: 633-635. DOI ScienceOn |
22 | Zhang, J. and M. Oyama. 2004. A hydrogen peroxide sensor based on the peroxidase activity of hemoglobin immobilized on gold nanoparticles-modified ITO electrode. Electrochim. Acta 50: 85-90. DOI ScienceOn |
23 | Matsui, T., S. Ozaki, E. Liong, G. N. Phillips Jr., and Y. Watanabe. 1999. Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide. J. Biol. Chem. 274: 2838-2844. DOI |
24 | Patapas, J., M. M. Al-Ansari, K. E. Taylor, J. K. Bewtra, and N. Biswas. 2007. Removal of dinitrotoluenes from water via reduction with iron and peroxidase-catalyzed oxidative polymerization: A comparison between Arthromyces ramosus peroxidase and soybean peroxidase. Chemosphere 67: 1485-1491. DOI ScienceOn |
25 | Tarricone, C., A. Galizzi, A. Coda, P. Ascenzi, and M. Bolognesi. 1997. Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp. Structure 5: 497-507. DOI ScienceOn |
26 | Tsuruga, M., A. Matsuoka, A. Hachimori, Y. Sugawara, and K. Shikama. 1998. The molecular mechanism of autoxidation for human oxyhemoglobin. Tilting of the distal histidine causes nonequivalent oxidation in the beta chain. J. Biol. Chem. 273: 8607-8615. DOI |
27 | Bolognesi, M., A. Boffi, M. Coletta, A. Mozzarelli, A. Pesce, C. Tarricone, and P. Ascenzi. 1999. Anticooperative ligand binding properties of recombinant ferric Vitreoscilla homodimeric hemoglobin: A thermodynamic, kinetic and X-ray crystallographic study. J. Mol. Biol. 291: 637-650. DOI ScienceOn |
28 | Khosla, C., J. E. Curtis, J. DeModena, U. Rinas, and J. E. Bailey. 1990. Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli. Biotechnology (NY) 8: 849-853. DOI ScienceOn |
29 | Verma, S., S. Patel, R. Kaur, Y. T. Chung, B. T. Duk, K. L. Dikshit, B. C. Stark, and D. A. Webster. 2005. Mutational study of the bacterial hemoglobin distal heme pocket. Biochem. Biophys. Res. Commun. 326: 290-297. DOI ScienceOn |
30 | Bodalo, A., J. L. Gomez, E. Gomez, A. M. Hidalgo, M. Gomez, and A. M. Yelo. 2007. Elimination of 4-chlorophenol by soybean peroxidase and hydrogen peroxide: Kinetic model and intrinsic parameters. Biochem. Eng. J. 34: 242-247. DOI ScienceOn |
31 | Ascenzi, P., M. Brunori, M. Coletta, and A. Desideri. 1989. pH effects on the haem iron co-ordination state in the nitric oxide and deoxy derivatives of ferrous horseradish peroxidase and cytochrome c peroxidase. Biochem. J. 258: 473-478. |
32 | Farres, J. and P. T. Kallio. 2002. Improved cell growth in tobacco suspension cultures expressing Vitreoscilla hemoglobin. Biotechnol. Prog. 18: 229-233. DOI ScienceOn |
33 | Ling, K. Q. and L. M. Sayre. 2005. Horseradish peroxidasemediated aerobic and anaerobic oxidations of 3-alkylindoles. Bioorg. Med. Chem. 13: 3543-3551. DOI ScienceOn |
34 | Suzuki, T., Y. H. Watanabe, M. Nagasawa, A. Matsuoka, and K. Shikama. 2000. Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin comparison of the H64 mutants. Eur. J. Biochem. 267: 6166-6174. DOI ScienceOn |
35 | Andersson, C. I., C. Arfvidsson, P. T. Kallio, K. G. Wahlund, and L. Bulow. 2003. Enhanced ribosome and tRNA contents in Escherichia coli expressing a truncated Vitreoscilla hemoglobin mutant analyzed by flow field-flow fractionation. Biotechnol. Lett. 25: 1499-1504. DOI ScienceOn |
36 | Dubrac, S. and D. Touati. 2002. Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli. Microbiology 148: 147-156. |
37 | Fee, J. A. 1991. Regulation of sod genes in Escherichia coli: Relevance to superoxide dismutase function. Mol. Microbiol. 5: 2599-2610. DOI ScienceOn |
38 | Frey, A. D., B. T. Oberle, J. Farres, and P. T. Kallio. 2004. Expression of Vitreoscilla haemoglobin in tobacco cell cultures relieves nitrosative stress in vivo and protects from NO in vitro. Plant Biotechnol. J. 2: 221-231. DOI ScienceOn |
39 | Veitch, N. C. 2004. Horseradish peroxidase: A modern view of a classic enzyme. Phytochemistry 65: 249-259. DOI ScienceOn |
40 | Winterbourn, C. C. 1985. Free-radical production and oxidative reactions of hemoglobin. Environ. Health Perspect. 64: 321-330. DOI |
41 | Isarankura-Na-Ayudhya, C., P. Panpumthong, T. Tangkosakul, S. Boonpangrak, and V. Prachayasittikul. 2008. Shedding light on the role of Vitreoscilla hemoglobin on cellular catabolic regulation by proteomic analysis. Int. J. Biol. Sci. 4: 71-80. |
42 | Kaur, R., R. Pathania, V. Sharma, S. C. Mande, and K. L. Dikshit. 2002. Chimeric Vitreoscilla hemoglobin (VHb) carrying a flavoreductase domain relieves nitrosative stress in Escherichia coli: New insight into the functional role of VHb. Appl. Environ. Microbiol. 68: 152-160. DOI ScienceOn |
43 | Redaelli, C., E. Monzani, L. Santagostini, L. Casella, A. M. Sanangelantoni, R. Pierattelli, and L. Banci. 2002. Characterization and peroxidase activity of a myoglobin mutant containing a distal arginine. Chembiochem 3: 226-233. DOI ScienceOn |
44 | Wei, X. X. and G. Q. Chen. 2008. Applications of the VHb gene vgb for improved microbial fermentation processes. Methods Enzymol. 436: 273-287. DOI |
45 | Schiodt, C. B., N. C. Veitch, and K. G. Welinder. 2007. Roles of distal arginine in activity and stability of Coprinus cinereus peroxidase elucidated by kinetic and NMR analysis of the Arg51Gln, -Asn, -Leu, and -Lys mutants. J. Inorg. Biochem. 101: 336-347. DOI ScienceOn |
46 | Arseguel, D. and M. Baboulne. 2004. Removal of phenol from coupling of talc and peroxidase: Application for depollution of waste water containing phenolic compounds. J. Chem. Technol. Biotechnol. 61: 331-335. |
47 | Finzel, B. C., T. L. Poulos, and J. Kraut. 1984. Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution. J. Biol. Chem. 259: 13027-13036. |
48 | Nagababu, E. and J. M. Rifkind. 2000. Reaction of hydrogen peroxide with ferrylhemoglobin: Superoxide production and heme degradation. Biochemistry 39: 12503-12511. DOI ScienceOn |
49 | Suwanwong, Y., M. Kvist, C. Isarankura-Na-Ayudhya, N. Tansila, L. Bulow, and V. Prachayasittikul. 2006. Chimeric antibodybinding Vitreoscilla hemoglobin (VHb) mediates redox-catalysis reaction: New insight into the functional role of VHb. Int. J. Biol. Sci. 2: 208-215. |
50 | Beale, S. I. 1990. Biosynthesis of the tetrapyrrole pigment precursor, delta-aminolevulinic acid, from glutamate. Plant Physiol. 93: 1273-1279. DOI ScienceOn |