NMR comparison of prokaryotic and eukaryotic cytochromes c.
NMR comparison of prokaryotic and eukaryotic cytochromes c.
复制标题
原核和真核细胞色素的 NMR 比较 c.
DOI:
10.1021/bi00473a012
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发表时间:
1990
期刊:
影响因子:
2.9
通讯作者:
Timkovich,R
中科院分区:
文献类型:
--
作者:
Chau,MH;Cai,ML;Timkovich,R
Department of Chemistry, University of Alabama, Tuscaloosa, Alabama 35687-0336 Received October 27, 1989; Revised Manuscript Received January 30, 1990 abstract:* H NMR spectroscopy has been used toexamine ferrocytochrome c-551 from Pseudomonas aeruginosa (ATCC 19429) over the pH range 3.5-10.6 and the temperature range 4-60 C. Resonance assignments are proposed for main-chain and side-chain protons. Comparison of results for cytochrome c-551 torecently assigned spectra for horse cytochrome c (Wand et al.(1989) Biochemistry 28, 186-194) and mutants of yeast iso-1 cytochrome (Pielak et al.(1988) Eur. J. Biochem. 177, 167-177) reveals some unique resonances with unusual chemical shifts in all cytochromes that may serve as markers for the heme region. Results for cytochrome c-551 indicate that in the smaller prokaryotic cytochrome, all benzoid side chains are rapidly flipping on the NMR time scale. In contrast, in eukaryotic cytochromes there are some rings flipping slowly on the NMR time scale. The ferrocytochrome c-551 undergoes a transition linked to pH with a pK around 7. The pH behavior of assigned resonances provides evidence that the site of protonation is the inner or buried 17-propionic acid heme substituent (IUPAC-IUB porphyrin nomenclature). Conformational heterogeneity has been observed for segments near the inner heme propionate substituent.