ArticleProceedings of the National Academy of Sciences of the United States of America2005
Early events in the folding of four-helix-bundle heme proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Unfolding cytochromes c-bJournal of inorganic biochemistry · 2020Article
- Domain-swapped cytochromeChemical science · 2015Article
- Computational study of elements of stability of a four-helix bundle protein biosurfactant.Journal of computer-aided molecular design · 2015Article
- Intrachain contact dynamics in unfolded cytochrome cb562.The journal of physical chemistry. B · 2013Article
- Snapshots of a protein folding intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Folding energy landscape of cytochrome cb562.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Probing the cytochrome c' folding landscape.Journal of inorganic biochemistry · 2007Article
- Site-specific collapse dynamics guide the formation of the cytochrome c' four-helix bundle.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Solvent-tuning the collapse and helix formation time scales of lambda(6-85)*.Protein science : a publication of the Protein Society · 2006Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Topologically homologous four-helix-bundle heme proteins exhibit striking diversity in their refolding kinetics. Cytochrome b562 has been reported to fold on a sub-millisecond time scale, whereas cytochrome c' refolding requires 10 s or more to complete. Heme dissociation in cytochrome b562 interferes with studies of folding kinetics, so a variant of cytochrome b562 (cytochrome c-b562) with a covalent c-type linkage to the heme has been expressed in Escherichia coli. Early events in the electron transfer-triggered folding of Fe(II)-cytochrome c-b562, along with those of Fe(II)-cytochrome c556, have been examined by using time-resolved absorption spectroscopy. Coordination of S(Met) to Fe(II) occurs within 10 mus after reduction of the denatured Fe(III)-cytochromes, and shortly thereafter (100 micros) the heme spectra are indistinguishable from those of the folded proteins. Under denaturing conditions, carbon monoxide binds to the Fe(II)-hemes in approximately 15 ms. By contrast, CO binding cannot compete with refolding in the Fe(II)-cytochromes, thereby confirming that the polypeptide encapsulates the heme in <10 ms. We suggest that Fe-S(Met) ligation facilitates refolding in these four-helix-bundle heme proteins by reducing the conformational freedom of the polypeptide chain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.