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Gene Review

TTHA1423  -  cytochrome C-552

Thermus thermophilus HB8

 
 
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Disease relevance of TTHA1423

 

High impact information on TTHA1423

 

Chemical compound and disease context of TTHA1423

  • 3. The effect of guanidine hydrochloride on the heme iron-methionine bond of Thermus and horse cytochromes c was also investigated; a comparison of the free-energy changes for the displacement of the bond indicated that the coordination in cytochrome c-552 is highly stable [7].
 

Biological context of TTHA1423

  • When prokaryotic cytochrome c-552 oxidase (ba(3)) of Thermus thermophilus turns over, three different metal centres (cytochromes b, a(3) and CuA) share the steady state electrons; it is the fourth, CuB, that apparently remains almost fully oxidized until anaerobiosis [8].
 

Associations of TTHA1423 with chemical compounds

 

Analytical, diagnostic and therapeutic context of TTHA1423

References

  1. Amino acid sequence of cytochrome c-552 from Thermus thermophilus HB8. Titani, K., Ericsson, L.H., Hon-nami, K., Miyazawa, T. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  2. Integrity of thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: biochemical, spectral, and structural characterization of the recombinant protein. Fee, J.A., Chen, Y., Todaro, T.R., Bren, K.L., Patel, K.M., Hill, M.G., Gomez-Moran, E., Loehr, T.M., Ai, J., Thöny-Meyer, L., Williams, P.A., Stura, E., Sridhar, V., McRee, D.E. Protein Sci. (2000) [Pubmed]
  3. Different interaction modes of two cytochrome-c oxidase soluble CuA fragments with their substrates. Maneg, O., Ludwig, B., Malatesta, F. J. Biol. Chem. (2003) [Pubmed]
  4. Exploring the cytochrome c folding mechanism: cytochrome c552 from thermus thermophilus folds through an on-pathway intermediate. Travaglini-Allocatelli, C., Gianni, S., Morea, V., Tramontano, A., Soulimane, T., Brunori, M. J. Biol. Chem. (2003) [Pubmed]
  5. Cloning and expression in Escherichia coli of the cytochrome c552 gene from Thermus thermophilus HB8. Evidence for genetic linkage to an ATP-binding cassette protein and initial characterization of the cycA gene products. Keightley, J.A., Sanders, D., Todaro, T.R., Pastuszyn, A., Fee, J.A. J. Biol. Chem. (1998) [Pubmed]
  6. Respiratory proteins from the extremely thermophilic aerobic bacterium, Thermus thermophilus. Purification procedures for cytochromes c552, c555,549, and c1aa3 and chemical evidence for a single subunit cytochrome aa3. Yoshida, T., Lorence, R.M., Choc, M.G., Tarr, G.E., Findling, K.L., Fee, J.A. J. Biol. Chem. (1984) [Pubmed]
  7. Denaturation of thermophilic ferricytochrome c-552 by acid, guanidine hydrochloride, and heat. Hon-nami, K., Oshima, T. Biochemistry (1979) [Pubmed]
  8. The mixed valence state of the oxidase binuclear centre: how Thermus thermophilus cytochrome ba3 differs from classical aa3 in the aerobic steady state and when inhibited by cyanide. Nicholls, P., Soulimane, T. Biochim. Biophys. Acta (2004) [Pubmed]
  9. Cytochrome-c552 from Thermus thermophilus: a functional and crystallographic investigation. Soulimane, T., von Walter, M., Hof, P., Than, M.E., Huber, R., Buse, G. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  10. A homologous expression system for obtaining engineered cytochrome ba3 from Thermus thermophilus HB8. Chen, Y., Hunsicker-Wang, L., Pacoma, R.L., Luna, E., Fee, J.A. Protein Expr. Purif. (2005) [Pubmed]
  11. Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide. Kihara, H., Nakatani, H., Hiromi, K., Hon-Nami, K. Biochim. Biophys. Acta (1977) [Pubmed]
  12. Alkaline isomerization of thermoresistant cytochrome c-552 and horse heart cytochrome c studied by absorption and resonance Raman spectroscopy. Kihara, H., Hon-Nami, K., Kitagawa, T. Biochim. Biophys. Acta (1978) [Pubmed]
 
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