Structural highlights
Function
[CYCP_RHOPA] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We employed fluorescence energy-transfer probes to investigate the polypeptide dynamics accompanying cytochrome c' folding. Analysis of fluorescence energy-transfer kinetics from wild-type Trp-72 or Trp-32 in a crystallographically characterized (1.78 A) Q1A/F32W/W72F mutant shows that there is structural heterogeneity in denatured cytochrome c'. Even at guanidine hydrochloride concentrations well beyond the unfolding transition, a substantial fraction of the polypeptides ( approximately 50%) adopts compact conformations (tryptophan-to-heme distance, approximately 25 A) in both pseudo-wild-type (Q1A) and mutant proteins. A burst phase (< or =5 ms) is revealed when stopped flow-triggered refolding is probed by tryptophan intensity: measurements on the Q1A protein show that approximately 75% of the Trp-72 fluorescence (83% for Trp-32) is quenched within the mixing deadtime, suggesting that most of the polypeptides have collapsed.
Structural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics.,Lee JC, Engman KC, Tezcan FA, Gray HB, Winkler JR Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14778-82. Epub 2002 Oct 29. PMID:12407175[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee JC, Engman KC, Tezcan FA, Gray HB, Winkler JR. Structural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14778-82. Epub 2002 Oct 29. PMID:12407175 doi:10.1073/pnas.192574099
