Tanzima Yeasmin
Department of Biochemistry, Rajshahi University, Rajshahi 6205, Bangladesh
Yoshihiro Fukumori
Department of Life Science, Faculty of Bioscience and Biotechnology,
Tokyo Institute of Technology, Japan
ABSTRACT
Terminal respiratory system of an autotrophic nitrite- oxidizing bacterium, Nitrobacter winogradskyi was reconstructed with the purified components in vitro. Cytochrome aa3-type cytochrome c oxidase, soluble cytochrome c oxidase, soluble cytochrome c-550 and membrane-bound c-551 were purified from the bacterium to electrophoretically homogeneous states, respectively. Oxidations of the soluble ferro-cytochrome c-550 and membrane-bound ferrocytochrome c-551 by the cytochrome c oxidase was kinetically analyzed. Value of affinity constant (Km) and maximum velocity (Vmax) for the soluble cytochrome c-550 were 5.78 μ M and 251.5 sec-1 respectively, while values of Km and Vmax for the membrane-bound cytochrome c-551 were 3.2 μM and 88.7 sec-1respectively. The oxidation of membrane-bound ferro-cytochrome c-551 with the cytochrome c oxidase was accelerated by the addition of soluble cytochrome c-550, while oxidation of soluble cytochrome c-550 with enzyme was inhibited by the addition of membrane bound cytochrome c-551. Although membrane-bound cytochrome c-551 could be electron donor for cytochrome c oxidase, the soluble cytochrome c-550 seems to function as electron mediator between membrane bound cytochrome c-551 and cytochrome c oxidase in vivo.
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How to cite this article
Tanzima Yeasmin and Yoshihiro Fukumori, 2001. Studies
on the Physiological Electron Donor for Cytochrome C Oxidase
in Nitrobacter winogradskyi. Journal of Biological Sciences, 1: 846-851.
DOI: 10.3923/jbs.2001.846.851
URL: https://scialert.net/abstract/?doi=jbs.2001.846.851
DOI: 10.3923/jbs.2001.846.851
URL: https://scialert.net/abstract/?doi=jbs.2001.846.851
REFERENCES
- Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
CrossRefDirect Link - Aleem, M.I.H. and. M. Alexander, 1958. Cell free nitrification by Nitrobacter. J. Bacteriol., 76: 510-514.
Direct Link - Aleem, M.I.H. and D.L. Sewell, 1981. Mechanism of nitrite oxidation and oxidoreductase system in Nitrobacter agilis. Curr. Microbiol., 5: 67-272.
CrossRefDirect Link - Drabkin, D.L., 1942. Spectrophotometeric studies X. structural interpretation of spectra of cyanide, pyridine and carbon monoxide derivatives of cytochrome C and hemoglobin. J. Biol. Chem., 146: 605-617.
Direct Link - Fukuoka, M., Y. Fukumori and T. Yamanaka, 1987. Nitrobacter winogradskyi cytochrome A1C1 is an iron-sulfer molybdoenzyme having heme A and C. J. Biochem., 102: 525-530.
PubMedDirect Link - Haltia, T., A. Puustien and M. Finel, 1988. The Paracoccus denitrificans cytochrome AA3 has A third subunit. Eur. J. Biochem., 172: 543-546.
PubMedDirect Link - Ludwig, B., 1987. Cytochrome c oxidase in prokaryotes. FEMS Microbiol. Rev., 46: 41-56.
CrossRefDirect Link - Malstrom, B.G., 1979. Cytochrome c oxidase, structure and catalytic activity. Biochem. Biophys. Acta, 549: 281-303.
PubMedDirect Link - Sundermeyer, K.H., B. Warnighoff and E. Bock, 1984. Membrane bound nitrite oxidoreductase of Nitrobacter: Evidence for a nitrite oxidation system. Arch. Microbiol., 135: 265-271.
CrossRefDirect Link - Tanaka, Y., Y. Fukumori and. T. Yamanaka, 1982. The complete amino acid sequence of N. Agilis cytochrome c-550. Biochem. Biophys. Acta, 707: 14-20.
PubMedDirect Link