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Structural and chemical changes of the P(M) intermediate of paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidine.
Iwaki M, Puustinen A, Wikström M, Rich PR. Iwaki M, et al. Among authors: puustinen a. Biochemistry. 2006 Sep 12;45(36):10873-85. doi: 10.1021/bi061114b. Biochemistry. 2006. PMID: 16953573
Prior studies of P(M) minus oxidized (O) IR difference spectra of unlabeled, universally (15)N-labeled and ring-d(4)-tyrosine-labeled proteins (Iwaki, M., Puustinen, A., Wikstrom, M., and Rich, P. R. (2004) Biochemistry 43, 14370-14378). provided a basis for …
Prior studies of P(M) minus oxidized (O) IR difference spectra of unlabeled, universally (15)N-labeled and ring-d(4)-tyrosine-labeled protei …
Binding of O(2) and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans.
Riistama S, Puustinen A, Verkhovsky MI, Morgan JE, Wikström M. Riistama S, et al. Among authors: puustinen a. Biochemistry. 2000 May 30;39(21):6365-72. doi: 10.1021/bi000123w. Biochemistry. 2000. PMID: 10828950
The crystal structure of the heme-copper oxidases suggested a putative channel of oxygen entry into the heme-copper site of O(2) reduction. Changing a conserved valine near this center in cytochrome bo(3) of Escherichia coli to isoleucine caused a significant …
The crystal structure of the heme-copper oxidases suggested a putative channel of oxygen entry into the heme-copper site of O(2) redu …
64 results