Table 1 - In-silico inferrence of function mechanisms: A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei

	Electronic Journal of Biotechnology ISSN: 0717-3458
	© 2003 by Universidad Católica de Valparaíso -- Chile
	Vol. 6 No. 1, Issue of April 15, 2003

Table 1. Functions and residue sequence position comparisons table for functionally important amino acid residues in subunits of the cytochrome c oxidase from P. denitrificans, bovine heart mitochondria and predicted protein sequence from B. pseudomallei.

-			Residue position
-	-	Residue	P. denitrificans	Bovine heart mitochondria	T. thermophilus	B. pseudomallei
Heme ligands	a a₃	His His His	94 413 411	61 378 376	72	24 339 337
Cu_B ligands	-	His* His His	276 325 326	240 290 291	233 282 283	186 235 236
Proton pathways	K-pathway	Thr Tyr*	351 280	316 244	309 (Ser) 237	262 190
Electron transfer	Cu_A heme a	Arg Arg	473 474	438 439	450 451	400 401
Electron transfer	heme heme a₃	Phe	412	377	385	338

*Tyrosine is covalently bound to a CuB histidine ligand.

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